AS Monaco Basket

# AS Monaco Basket

## Abstract

AS Monaco Basket, commonly referred to as AS Monaco or simply Monaco, is a French-registered Monaco -based professional basketball club. They are a part of the Monaco-based multi-sports club of A.S. Monaco, which was founded in 1924.

The club's basketball section was founded four years later in 1928, and it currently competes in the French top-tier level LNB Pro A and the EuroLeague. Monaco plays their home games at Salle Gaston Médecin.

Monaco has won one EuroCup title in 2021, one French Cup in 2023, and three Leaders Cups.

## History

About four years after the parent athletic club, A.S. Monaco, was itself founded, A.S. Monaco Basket was founded in 1928. They finished as runners-up in the French top-tier level Nationale 1 (current LNB Pro A) following the 1950 season, which is regarded as one of their greatest successes in their history. Monaco also won the LNB Pro B (French 2nd Division) championship in the 1973 season, with one of the greatest offenses on the European continent.

A.S. Monaco Basket joined the Nationale 1 for the 1973–74 season, where they finished in ninth place. They made their first appearance in the European 3rd-tier level FIBA Korać Cup in the 1974–75 season, where they lost in the group stage to other notable teams, such as the French League club ASVEL Basket, the Bulgarian League club Levski Sofia, and the Italian League club AMG Sebastiani Basket. They entered the same tournament again in the 1982–83 season, but lost to Dynamo Moscow in the semifinals qualification battle, in the Top 16 group stage, despite a far better finish in the tournament overall.

Entering the 1980s, Monaco was in the process of securing their title as one of the most dangerous teams in French basketball. They reached the finals game of the French Federation Cup, where they lost to Limoges CSP, by a score of 96–81. The Red and Whites also became a threat in the LNB Pro A (French 1st Division), what the league had been renamed to, after former NBA player, Robert Smith, joined the team in 1985. Smith was named the 1987 French League All-Star Game MVP.

After Smith left the team, Monaco found themselves descending in the league. They were relegated to the second division LNB Pro B, later in the decade, and eventually ended up in the Nationale 1 Division. They would not return to the LNB Pro A, the highest division of basketball in France, for many years to come. In 2014, A.S. Monaco Basket was crowned the champions of the French third-tier league, the Nationale Masculine 1 (NM1), and they returned to the LNB Pro B (French 2nd Division).

In the 2014–15 season, Monaco became the French 2nd-tier LNB Pro B champions, and they were finally promoted back to the top-tier league in France, the LNB Pro A. In 2015, the Ukrainian businessman and philanthropist, Sergey Dyadechko, became the President of A.S. Monaco Basket. In the 2015–16 season, Monaco won the 2016 edition of the French Pro A League Cup, after beating Élan Chalon in the finals, by a score of 99–74. Monaco player, Jamal Shuler, was named the French Pro A Leaders Cup MVP.

In the 2016–17 season, Monaco returned to European-wide competitions, when it qualified for one of the pan-European secondary level competitions, the FIBA Basketball Champions League. They finished the season in third place. In 2017, the charity fund, DSF, founded by the club's owner, Dyadechko, became a sponsor of A.S. Monaco Basket. The club also played in the FIBA Champions League, during the 2017–18 season, in which they finished in second place, after they lost to the Greek League club AEK Athens in the final, by a score of 100–94. The club won the 2017 French Pro A League Cup and the 2018 French Pro A League Cup titles. They also finished in second place in the French Pro A League, in the 2017–18 season.

In European-wide competitions, Monaco spent the next three seasons (2018–19, 2019–20, and 2020–21) playing in the other pan-European secondary level competition, the EuroCup, subsequently winning it in 2020–21. In the 2021–22 season, Monaco made its debut in the EuroLeague, the highest pan-European level. Finishing seventh in the regular season with a 15–13 record, Monaco qualified for the playoffs where they lost 2–3 to the second-seeded Olympiacos.

The following season, Monaco was eligible for another EuroLeague season because of their good performance the previous season. They made the playoffs for a second season in a row.

On April 22, 2023, Monaco won its first major trophy when it won its maiden French Basketball Cup with Monaco, after beating ASVEL in the final. Élie Okobo was the cup final's MVP after his 20-point performance. In the same 2022–23 season, Monaco reached new height on the continental level after reaching the 2023 EuroLeague Final Four after beating Maccabi Tel Aviv in the playoffs. They became the third French League club ever to reach the Final Four (after ASVEL and Limoges) and the first to do so in 26 years.

## Arena

A.S. Monaco Basket plays its home games at the 3,000 seat Salle Gaston Médecin, which is a part of the Stade Louis II sports complex.

Due to minimum requirements, Monaco was supposed to play its 2021–22 EuroLeague games in the Azur Arena in Antibes. The decision was later overturned, thus the team could play in its usual home arena.

## Players

## Trophies and honors

### Domestic competitions

- French League

- French Basketball Cup

- French Pro A Leaders Cup

- French Pro B

- French NM1

### European competitions

- EuroLeague

- EuroCup

- Basketball Champions League

### Other competitions

- Berlin, Germany Invitational Game

## Notable players

France:

- Georgy Adams

- Cyril Akpomedah

- Éric Beugnot

- Petr Cornelie

- Moustapha Fall

- Damien Inglis

- Mouhammadou Jaiteh

- Paul Lacombe

- Yoan Makoundou

- Elie Okobo

- Yakuba Ouattara

- Jean Perniceni

- Amara Sy

- Philip Szanyiel

- / Terry Tarpey

- Kim Tillie

- Ali Traoré

- Léo Westermann

Europe:

- Ivan Buva

- Aaron Cel

- Kyrylo Fesenko

- Sergii Gladyr

- Elmedin Kikanović

- Donatas Motiejūnas

- Damjan Rudež

- Danilo Anđušić

United States:

- Dwayne Bacon

- / Dee Bost

- John Brown

- Eric Buckner

- / Nik Caner-Medley

- / Anthony Clemmons

- Norris Cole

- D.J. Cooper

- Aaron Craft

- / Brandon Davies

- Chris Evans

- Rob Gray

- / Donta Hall

- Mike James

- / Jarrod Jones

- Dru Joyce

- Paris Lee

- Jordan Loyd

- Darrel Mitchell

- / Derek Needham

- / DeMarcus Nelson

- J.J. O'Brien

- Gerald Robinson

- Jamal Shuler

- Robert Smith

- Mike Stewart

- / Will Thomas

- Kemba Walker

- / Zack Wright

Rest of Americas & Oceania:

- Dylan Ennis

- Adrian Uter

- Brock Motum

Africa:

- Ibrahima Fall Faye

- Mehdi Hafsi

- Derrick Obasohan


Oxidative phosphorylation

# Oxidative phosphorylation

## Abstract

Oxidative phosphorylation (UK / ɒ k ˈ s ɪ d. ə. t ɪ v /, US / ˈ ɑː k. s ɪ ˌ d eɪ. t ɪ v /) or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

The energy stored in the chemical bonds of glucose is released by the cell in the citric acid cycle, producing carbon dioxide and the energetic electron donors NADH and FADH. Oxidative phosphorylation uses these molecules and O to produce ATP, which is used throughout the cell whenever energy is needed. During oxidative phosphorylation, electrons are transferred from the electron donors to a series of electron acceptors in a series of redox reactions ending in oxygen, whose reaction releases half of the total energy.

In eukaryotes, these redox reactions are catalyzed by a series of protein complexes within the inner membrane of the cell's mitochondria, whereas, in prokaryotes, these proteins are located in the cell's outer membrane. These linked sets of proteins are called the electron transport chain. In eukaryotes, five main protein complexes are involved, whereas in prokaryotes many different enzymes are present, using a variety of electron donors and acceptors.

The energy transferred by electrons flowing through this electron transport chain is used to transport protons across the inner mitochondrial membrane, in a process called electron transport. This generates potential energy in the form of a pH gradient and the resulting electrical potential across this membrane. This store of energy is tapped when protons flow back across the membrane and down the potential energy gradient, through a large enzyme called ATP synthase in a process called chemiosmosis. The ATP synthase uses the energy to transform adenosine diphosphate (ADP) into adenosine triphosphate, in a phosphorylation reaction. The reaction is driven by the proton flow, which forces the rotation of a part of the enzyme. The ATP synthase is a rotary mechanical motor.

Although oxidative phosphorylation is a vital part of metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging and senescence. The enzymes carrying out this metabolic pathway are also the target of many drugs and poisons that inhibit their activities.

## Chemiosmosis

Oxidative phosphorylation works by using energy -releasing chemical reactions to drive energy-requiring reactions. The two sets of reactions are said to be coupled. This means one cannot occur without the other. The chain of redox reactions driving the flow of electrons through the electron transport chain, from electron donors such as NADH to electron acceptors such as oxygen and hydrogen (protons), is an exergonic process – it releases energy, whereas the synthesis of ATP is an endergonic process, which requires an input of energy. Both the electron transport chain and the ATP synthase are embedded in a membrane, and energy is transferred from the electron transport chain to the ATP synthase by movements of protons across this membrane, in a process called chemiosmosis. A current of protons is driven from the negative N-side of the membrane to the positive P-side through the proton-pumping enzymes of the electron transport chain. The movement of protons creates an electrochemical gradient across the membrane, is called the proton-motive force. It has two components: a difference in proton concentration (a H gradient, Δ pH) and a difference in electric potential, with the N-side having a negative charge.

ATP synthase releases this stored energy by completing the circuit and allowing protons to flow down the electrochemical gradient, back to the N-side of the membrane. The electrochemical gradient drives the rotation of part of the enzyme's structure and couples this motion to the synthesis of ATP.

The two components of the proton-motive force are thermodynamically equivalent: In mitochondria, the largest part of energy is provided by the potential; in alkaliphile bacteria the electrical energy even has to compensate for a counteracting inverse pH difference. Inversely, chloroplasts operate mainly on ΔpH. However, they also require a small membrane potential for the kinetics of ATP synthesis. In the case of the fusobacterium Propionigenium modestum it drives the counter-rotation of subunits a and c of the F motor of ATP synthase.

The amount of energy released by oxidative phosphorylation is high, compared with the amount produced by anaerobic fermentation. Glycolysis produces only 2 ATP molecules, but somewhere between 30 and 36 ATPs are produced by the oxidative phosphorylation of the 10 NADH and 2 succinate molecules made by converting one molecule of glucose to carbon dioxide and water, while each cycle of beta oxidation of a fatty acid yields about 14 ATPs. These ATP yields are theoretical maximum values; in practice, some protons leak across the membrane, lowering the yield of ATP.

## Electron and proton transfer molecules

The electron transport chain carries both protons and electrons, passing electrons from donors to acceptors, and transporting protons across a membrane. These processes use both soluble and protein-bound transfer molecules. In mitochondria, electrons are transferred within the intermembrane space by the water- soluble electron transfer protein cytochrome c. This carries only electrons, and these are transferred by the reduction and oxidation of an iron atom that the protein holds within a heme group in its structure. Cytochrome c is also found in some bacteria, where it is located within the periplasmic space.

Within the inner mitochondrial membrane, the lipid -soluble electron carrier coenzyme Q10 (Q) carries both electrons and protons by a redox cycle. This small benzoquinone molecule is very hydrophobic, so it diffuses freely within the membrane. When Q accepts two electrons and two protons, it becomes reduced to the ubiquinol form (QH); when QH releases two electrons and two protons, it becomes oxidized back to the ubiquinone (Q) form. As a result, if two enzymes are arranged so that Q is reduced on one side of the membrane and QH oxidized on the other, ubiquinone will couple these reactions and shuttle protons across the membrane. Some bacterial electron transport chains use different quinones, such as menaquinone, in addition to ubiquinone.

Within proteins, electrons are transferred between flavin cofactors, iron–sulfur clusters and cytochromes. There are several types of iron–sulfur cluster. The simplest kind found in the electron transfer chain consists of two iron atoms joined by two atoms of inorganic sulfur; these are called clusters. The second kind, called, contains a cube of four iron atoms and four sulfur atoms. Each iron atom in these clusters is coordinated by an additional amino acid, usually by the sulfur atom of cysteine. Metal ion cofactors undergo redox reactions without binding or releasing protons, so in the electron transport chain they serve solely to transport electrons through proteins. Electrons move quite long distances through proteins by hopping along chains of these cofactors. This occurs by quantum tunnelling, which is rapid over distances of less than 1.4 × 10 m.

## Eukaryotic electron transport chains

Many catabolic biochemical processes, such as glycolysis, the citric acid cycle, and beta oxidation, produce the reduced coenzyme NADH. This coenzyme contains electrons that have a high transfer potential; in other words, they will release a large amount of energy upon oxidation. However, the cell does not release this energy all at once, as this would be an uncontrollable reaction. Instead, the electrons are removed from NADH and passed to oxygen through a series of enzymes that each release a small amount of the energy. This set of enzymes, consisting of complexes I through IV, is called the electron transport chain and is found in the inner membrane of the mitochondrion. Succinate is also oxidized by the electron transport chain, but feeds into the pathway at a different point.

In eukaryotes, the enzymes in this electron transport system use the energy released from O by NADH to pump protons across the inner membrane of the mitochondrion. This causes protons to build up in the intermembrane space, and generates an electrochemical gradient across the membrane. The energy stored in this potential is then used by ATP synthase to produce ATP. Oxidative phosphorylation in the eukaryotic mitochondrion is the best-understood example of this process. The mitochondrion is present in almost all eukaryotes, with the exception of anaerobic protozoa such as Trichomonas vaginalis that instead reduce protons to hydrogen in a remnant mitochondrion called a hydrogenosome.

### NADH-coenzyme Q oxidoreductase (complex I)

NADH-coenzyme Q oxidoreductase, also known as NADH dehydrogenase or complex I, is the first protein in the electron transport chain. Complex I is a giant enzyme with the mammalian complex I having 46 subunits and a molecular mass of about 1,000 kilodaltons (kDa). The structure is known in detail only from a bacterium; in most organisms the complex resembles a boot with a large "ball" poking out from the membrane into the mitochondrion. The genes that encode the individual proteins are contained in both the cell nucleus and the mitochondrial genome, as is the case for many enzymes present in the mitochondrion.

The reaction that is catalyzed by this enzyme is the two electron oxidation of NADH by coenzyme Q10 or ubiquinone (represented as Q in the equation below), a lipid-soluble quinone that is found in the mitochondrion membrane:

The start of the reaction, and indeed of the entire electron chain, is the binding of a NADH molecule to complex I and the donation of two electrons. The electrons enter complex I via a prosthetic group attached to the complex, flavin mononucleotide (FMN). The addition of electrons to FMN converts it to its reduced form, FMNH. The electrons are then transferred through a series of iron–sulfur clusters: the second kind of prosthetic group present in the complex. There are both and iron–sulfur clusters in complex I.

As the electrons pass through this complex, four protons are pumped from the matrix into the intermembrane space. Exactly how this occurs is unclear, but it seems to involve conformational changes in complex I that cause the protein to bind protons on the N-side of the membrane and release them on the P-side of the membrane. Finally, the electrons are transferred from the chain of iron–sulfur clusters to a ubiquinone molecule in the membrane. Reduction of ubiquinone also contributes to the generation of a proton gradient, as two protons are taken up from the matrix as it is reduced to ubiquinol (QH).

### Succinate-Q oxidoreductase (complex II)

Succinate-Q oxidoreductase, also known as complex II or succinate dehydrogenase, is a second entry point to the electron transport chain. It is unusual because it is the only enzyme that is part of both the citric acid cycle and the electron transport chain. Complex II consists of four protein subunits and contains a bound flavin adenine dinucleotide (FAD) cofactor, iron–sulfur clusters, and a heme group that does not participate in electron transfer to coenzyme Q, but is believed to be important in decreasing production of reactive oxygen species. It oxidizes succinate to fumarate and reduces ubiquinone. As this reaction releases less energy than the oxidation of NADH, complex II does not transport protons across the membrane and does not contribute to the proton gradient.

In some eukaryotes, such as the parasitic worm Ascaris suum, an enzyme similar to complex II, fumarate reductase (menaquinol:fumarateoxidoreductase, or QFR), operates in reverse to oxidize ubiquinol and reduce fumarate. This allows the worm to survive in the anaerobic environment of the large intestine, carrying out anaerobic oxidative phosphorylation with fumarate as the electron acceptor. Another unconventional function of complex II is seen in the malaria parasite Plasmodium falciparum. Here, the reversed action of complex II as an oxidase is important in regenerating ubiquinol, which the parasite uses in an unusual form of pyrimidine biosynthesis.

### Electron transfer flavoprotein-Q oxidoreductase

Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-Q oxidoreductase), also known as electron transferring-flavoprotein dehydrogenase, is a third entry point to the electron transport chain. It is an enzyme that accepts electrons from electron-transferring flavoprotein in the mitochondrial matrix, and uses these electrons to reduce ubiquinone. This enzyme contains a flavin and a cluster, but, unlike the other respiratory complexes, it attaches to the surface of the membrane and does not cross the lipid bilayer.

In mammals, this metabolic pathway is important in beta oxidation of fatty acids and catabolism of amino acids and choline, as it accepts electrons from multiple acetyl-CoA dehydrogenases. In plants, ETF-Q oxidoreductase is also important in the metabolic responses that allow survival in extended periods of darkness.

### Q-cytochrome c oxidoreductase (complex III)

Q-cytochrome c oxidoreductase is also known as cytochrome c reductase, cytochrome bc complex, or simply complex III. In mammals, this enzyme is a dimer, with each subunit complex containing 11 protein subunits, an iron–sulfur cluster and three cytochromes: one cytochrome c and two b cytochromes. A cytochrome is a kind of electron-transferring protein that contains at least one heme group. The iron atoms inside complex III's heme groups alternate between a reduced ferrous (+2) and oxidized ferric (+3) state as the electrons are transferred through the protein.

The reaction catalyzed by complex III is the oxidation of one molecule of ubiquinol and the reduction of two molecules of cytochrome c, a heme protein loosely associated with the mitochondrion. Unlike coenzyme Q, which carries two electrons, cytochrome c carries only one electron.

As only one of the electrons can be transferred from the QH donor to a cytochrome c acceptor at a time, the reaction mechanism of complex III is more elaborate than those of the other respiratory complexes, and occurs in two steps called the Q cycle. In the first step, the enzyme binds three substrates, first, QH, which is then oxidized, with one electron being passed to the second substrate, cytochrome c. The two protons released from QH pass into the intermembrane space. The third substrate is Q, which accepts the second electron from the QH and is reduced to Q, which is the ubisemiquinone free radical. The first two substrates are released, but this ubisemiquinone intermediate remains bound. In the second step, a second molecule of QH is bound and again passes its first electron to a cytochrome c acceptor. The second electron is passed to the bound ubisemiquinone, reducing it to QH as it gains two protons from the mitochondrial matrix. This QH is then released from the enzyme.

As coenzyme Q is reduced to ubiquinol on the inner side of the membrane and oxidized to ubiquinone on the other, a net transfer of protons across the membrane occurs, adding to the proton gradient. The rather complex two-step mechanism by which this occurs is important, as it increases the efficiency of proton transfer. If, instead of the Q cycle, one molecule of QH were used to directly reduce two molecules of cytochrome c, the efficiency would be halved, with only one proton transferred per cytochrome c reduced.

### Cytochrome c oxidase (complex IV)

Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. The mammalian enzyme has an extremely complicated structure and contains 13 subunits, two heme groups, as well as multiple metal ion cofactors – in all, three atoms of copper, one of magnesium and one of zinc.

This enzyme mediates the final reaction in the electron transport chain and transfers electrons to oxygen and hydrogen (protons), while pumping protons across the membrane. The final electron acceptor oxygen is reduced to water in this step. Both the direct pumping of protons and the consumption of matrix protons in the reduction of oxygen contribute to the proton gradient. The reaction catalyzed is the oxidation of cytochrome c and the reduction of oxygen:

### Alternative reductases and oxidases

Many eukaryotic organisms have electron transport chains that differ from the much-studied mammalian enzymes described above. For example, plants have alternative NADH oxidases, which oxidize NADH in the cytosol rather than in the mitochondrial matrix, and pass these electrons to the ubiquinone pool. These enzymes do not transport protons, and, therefore, reduce ubiquinone without altering the electrochemical gradient across the inner membrane.

Another example of a divergent electron transport chain is the alternative oxidase, which is found in plants, as well as some fungi, protists, and possibly some animals. This enzyme transfers electrons directly from ubiquinol to oxygen.

The electron transport pathways produced by these alternative NADH and ubiquinone oxidases have lower ATP yields than the full pathway. The advantages produced by a shortened pathway are not entirely clear. However, the alternative oxidase is produced in response to stresses such as cold, reactive oxygen species, and infection by pathogens, as well as other factors that inhibit the full electron transport chain. Alternative pathways might, therefore, enhance an organism's resistance to injury, by reducing oxidative stress.

### Organization of complexes

The original model for how the respiratory chain complexes are organized was that they diffuse freely and independently in the mitochondrial membrane. However, recent data suggest that the complexes might form higher-order structures called supercomplexes or " respirasomes ". In this model, the various complexes exist as organized sets of interacting enzymes. These associations might allow channeling of substrates between the various enzyme complexes, increasing the rate and efficiency of electron transfer. Within such mammalian supercomplexes, some components would be present in higher amounts than others, with some data suggesting a ratio between complexes I/II/III/IV and the ATP synthase of approximately 1:1:3:7:4. However, the debate over this supercomplex hypothesis is not completely resolved, as some data do not appear to fit with this model.

## Prokaryotic electron transport chains

In contrast to the general similarity in structure and function of the electron transport chains in eukaryotes, bacteria and archaea possess a large variety of electron-transfer enzymes. These use an equally wide set of chemicals as substrates. In common with eukaryotes, prokaryotic electron transport uses the energy released from the oxidation of a substrate to pump ions across a membrane and generate an electrochemical gradient. In the bacteria, oxidative phosphorylation in Escherichia coli is understood in most detail, while archaeal systems are at present poorly understood.

The main difference between eukaryotic and prokaryotic oxidative phosphorylation is that bacteria and archaea use many different substances to donate or accept electrons. This allows prokaryotes to grow under a wide variety of environmental conditions. In E. coli, for example, oxidative phosphorylation can be driven by a large number of pairs of reducing agents and oxidizing agents, which are listed below. The midpoint potential of a chemical measures how much energy is released when it is oxidized or reduced, with reducing agents having negative potentials and oxidizing agents positive potentials.

As shown above, E. coli can grow with reducing agents such as formate, hydrogen, or lactate as electron donors, and nitrate, DMSO, or oxygen as acceptors. The larger the difference in midpoint potential between an oxidizing and reducing agent, the more energy is released when they react. Out of these compounds, the succinate/fumarate pair is unusual, as its midpoint potential is close to zero. Succinate can therefore be oxidized to fumarate if a strong oxidizing agent such as oxygen is available, or fumarate can be reduced to succinate using a strong reducing agent such as formate. These alternative reactions are catalyzed by succinate dehydrogenase and fumarate reductase, respectively.

Some prokaryotes use redox pairs that have only a small difference in midpoint potential. For example, nitrifying bacteria such as Nitrobacter oxidize nitrite to nitrate, donating the electrons to oxygen. The small amount of energy released in this reaction is enough to pump protons and generate ATP, but not enough to produce NADH or NADPH directly for use in anabolism. This problem is solved by using a nitrite oxidoreductase to produce enough proton-motive force to run part of the electron transport chain in reverse, causing complex I to generate NADH.

Prokaryotes control their use of these electron donors and acceptors by varying which enzymes are produced, in response to environmental conditions. This flexibility is possible because different oxidases and reductases use the same ubiquinone pool. This allows many combinations of enzymes to function together, linked by the common ubiquinol intermediate. These respiratory chains therefore have a modular design, with easily interchangeable sets of enzyme systems.

In addition to this metabolic diversity, prokaryotes also possess a range of isozymes – different enzymes that catalyze the same reaction. For example, in E. coli, there are two different types of ubiquinol oxidase using oxygen as an electron acceptor. Under highly aerobic conditions, the cell uses an oxidase with a low affinity for oxygen that can transport two protons per electron. However, if levels of oxygen fall, they switch to an oxidase that transfers only one proton per electron, but has a high affinity for oxygen.

## ATP synthase (complex V)

ATP synthase, also called complex V, is the final enzyme in the oxidative phosphorylation pathway. This enzyme is found in all forms of life and functions in the same way in both prokaryotes and eukaryotes. The enzyme uses the energy stored in a proton gradient across a membrane to drive the synthesis of ATP from ADP and phosphate (P). Estimates of the number of protons required to synthesize one ATP have ranged from three to four, with some suggesting cells can vary this ratio, to suit different conditions.

This phosphorylation reaction is an equilibrium, which can be shifted by altering the proton-motive force. In the absence of a proton-motive force, the ATP synthase reaction will run from right to left, hydrolyzing ATP and pumping protons out of the matrix across the membrane. However, when the proton-motive force is high, the reaction is forced to run in the opposite direction; it proceeds from left to right, allowing protons to flow down their concentration gradient and turning ADP into ATP. Indeed, in the closely related vacuolar type H+-ATPases, the hydrolysis reaction is used to acidify cellular compartments, by pumping protons and hydrolysing ATP.

ATP synthase is a massive protein complex with a mushroom-like shape. The mammalian enzyme complex contains 16 subunits and has a mass of approximately 600 kilodaltons. The portion embedded within the membrane is called F and contains a ring of c subunits and the proton channel. The stalk and the ball-shaped headpiece is called F and is the site of ATP synthesis. The ball-shaped complex at the end of the F portion contains six proteins of two different kinds (three α subunits and three β subunits), whereas the "stalk" consists of one protein: the γ subunit, with the tip of the stalk extending into the ball of α and β subunits. Both the α and β subunits bind nucleotides, but only the β subunits catalyze the ATP synthesis reaction. Reaching along the side of the F portion and back into the membrane is a long rod-like subunit that anchors the α and β subunits into the base of the enzyme.

As protons cross the membrane through the channel in the base of ATP synthase, the F proton-driven motor rotates. Rotation might be caused by changes in the ionization of amino acids in the ring of c subunits causing electrostatic interactions that propel the ring of c subunits past the proton channel. This rotating ring in turn drives the rotation of the central axle (the γ subunit stalk) within the α and β subunits. The α and β subunits are prevented from rotating themselves by the side-arm, which acts as a stator. This movement of the tip of the γ subunit within the ball of α and β subunits provides the energy for the active sites in the β subunits to undergo a cycle of movements that produces and then releases ATP.

This ATP synthesis reaction is called the binding change mechanism and involves the active site of a β subunit cycling between three states. In the "open" state, ADP and phosphate enter the active site (shown in brown in the diagram). The protein then closes up around the molecules and binds them loosely – the "loose" state (shown in red). The enzyme then changes shape again and forces these molecules together, with the active site in the resulting "tight" state (shown in pink) binding the newly produced ATP molecule with very high affinity. Finally, the active site cycles back to the open state, releasing ATP and binding more ADP and phosphate, ready for the next cycle.

In some bacteria and archaea, ATP synthesis is driven by the movement of sodium ions through the cell membrane, rather than the movement of protons. Archaea such as Methanococcus also contain the A A synthase, a form of the enzyme that contains additional proteins with little similarity in sequence to other bacterial and eukaryotic ATP synthase subunits. It is possible that, in some species, the A A form of the enzyme is a specialized sodium-driven ATP synthase, but this might not be true in all cases.

## Oxidative phosphorylation - energetics

The transport of electrons from redox pair NAD / NADH to the final redox pair 1/2 O / H O can be summarized as

1/2 O + NADH + H → H O + NAD

The potential difference between these two redox pairs is 1.14 volt, which is equivalent to -52 kcal/mol or -2600 kJ per 6 mol of O.

When one NADH is oxidized through the electron transfer chain, three ATPs are produced, which is equivalent to 7.3 kcal/mol x 3 = 21.9 kcal/mol.

The conservation of the energy can be calculated by the following formula

Efficiency = (21.9 x 100%) / 52 = 42%

So we can conclude that when NADH is oxidized, about 42% of energy is conserved in the form of three ATPs and the remaining (58%) energy is lost as heat (unless the chemical energy of ATP under physiological conditions was underestimated).

## Reactive oxygen species

Molecular oxygen is a good terminal electron acceptor because it is a strong oxidizing agent. The reduction of oxygen does involve potentially harmful intermediates. Although the transfer of four electrons and four protons reduces oxygen to water, which is harmless, transfer of one or two electrons produces superoxide or peroxide anions, which are dangerously reactive.

These reactive oxygen species and their reaction products, such as the hydroxyl radical, are very harmful to cells, as they oxidize proteins and cause mutations in DNA. This cellular damage may contribute to disease and is proposed as one cause of aging.

The cytochrome c oxidase complex is highly efficient at reducing oxygen to water, and it releases very few partly reduced intermediates; however small amounts of superoxide anion and peroxide are produced by the electron transport chain. Particularly important is the reduction of coenzyme Q in complex III, as a highly reactive ubisemiquinone free radical is formed as an intermediate in the Q cycle. This unstable species can lead to electron "leakage" when electrons transfer directly to oxygen, forming superoxide. As the production of reactive oxygen species by these proton-pumping complexes is greatest at high membrane potentials, it has been proposed that mitochondria regulate their activity to maintain the membrane potential within a narrow range that balances ATP production against oxidant generation. For instance, oxidants can activate uncoupling proteins that reduce membrane potential.

To counteract these reactive oxygen species, cells contain numerous antioxidant systems, including antioxidant vitamins such as vitamin C and vitamin E, and antioxidant enzymes such as superoxide dismutase, catalase, and peroxidases, which detoxify the reactive species, limiting damage to the cell.

## Oxidative phosphorylation in hypoxic/anoxic conditions

As oxygen is fundamental for oxidative phosphorylation, a shortage in O level can alter ATP production rates. Under anoxic conditions, ATP-synthase will commit 'cellular treason' and run in reverse, forcing protons from the matrix back into the inner membrane space, using up ATP in the process. The proton motive force and ATP production can be maintained by intracellular acidosis. Cytosolic protons that have accumulated with ATP hydrolysis and lactic acidosis can freely diffuse across the mitochondrial outer-membrane and acidify the inter-membrane space, hence directly contributing to the proton motive force and ATP production.

## Inhibitors

There are several well-known drugs and toxins that inhibit oxidative phosphorylation. Although any one of these toxins inhibits only one enzyme in the electron transport chain, inhibition of any step in this process will halt the rest of the process. For example, if oligomycin inhibits ATP synthase, protons cannot pass back into the mitochondrion. As a result, the proton pumps are unable to operate, as the gradient becomes too strong for them to overcome. NADH is then no longer oxidized and the citric acid cycle ceases to operate because the concentration of NAD falls below the concentration that these enzymes can use.

Many site-specific inhibitors of the electron transport chain have contributed to the present knowledge of mitochondrial respiration. Synthesis of ATP is also dependent on the electron transport chain, so all site-specific inhibitors also inhibit ATP formation. The fish poison rotenone, the barbiturate drug amytal, and the antibiotic piericidin A inhibit NADH and coenzyme Q.

Carbon monoxide, cyanide, hydrogen sulphide and azide effectively inhibit cytochrome oxidase. Carbon monoxide reacts with the reduced form of the cytochrome while cyanide and azide react with the oxidised form. An antibiotic, antimycin A, and British anti-Lewisite, an antidote used against chemical weapons, are the two important inhibitors of the site between cytochrome B and C1.

Not all inhibitors of oxidative phosphorylation are toxins. In brown adipose tissue, regulated proton channels called uncoupling proteins can uncouple respiration from ATP synthesis. This rapid respiration produces heat, and is particularly important as a way of maintaining body temperature for hibernating animals, although these proteins may also have a more general function in cells' responses to stress.

## History

The field of oxidative phosphorylation began with the report in 1906 by Arthur Harden of a vital role for phosphate in cellular fermentation, but initially only sugar phosphates were known to be involved. However, in the early 1940s, the link between the oxidation of sugars and the generation of ATP was firmly established by Herman Kalckar, confirming the central role of ATP in energy transfer that had been proposed by Fritz Albert Lipmann in 1941. Later, in 1949, Morris Friedkin and Albert L. Lehninger proved that the coenzyme NADH linked metabolic pathways such as the citric acid cycle and the synthesis of ATP. The term oxidative phosphorylation was coined by Volodymyr Belitser in 1939.

For another twenty years, the mechanism by which ATP is generated remained mysterious, with scientists searching for an elusive "high-energy intermediate" that would link oxidation and phosphorylation reactions. This puzzle was solved by Peter D. Mitchell with the publication of the chemiosmotic theory in 1961. At first, this proposal was highly controversial, but it was slowly accepted and Mitchell was awarded a Nobel prize in 1978. Subsequent research concentrated on purifying and characterizing the enzymes involved, with major contributions being made by David E. Green on the complexes of the electron-transport chain, as well as Efraim Racker on the ATP synthase. A critical step towards solving the mechanism of the ATP synthase was provided by Paul D. Boyer, by his development in 1973 of the "binding change" mechanism, followed by his radical proposal of rotational catalysis in 1982. More recent work has included structural studies on the enzymes involved in oxidative phosphorylation by John E. Walker, with Walker and Boyer being awarded a Nobel Prize in 1997.


Austin FC record by opponent

# Austin FC record by opponent

## Abstract

Austin FC is an American professional men's soccer club based in Austin, Texas. The club competes in Major League Soccer (MLS) as a member of the Western Conference. Founded in 2018, the club began play in the 2021 season. Their home stadium is Q2 Stadium in north Austin. In addition to participating in MLS, Austin FC participates in U.S. Open Cup, Leagues Cup, and the CONCACAF Champions League.

## All-time league record

## All-time MLS Cup record

## All-time CONCACAF Champions League record

## All-time Leagues Cup record

## All-time U.S. Open Cup record


Princess Miriam Ghazi

# Princess Miriam Ghazi

## Abstract

Princess Míriam Ghazi of Jordan (born Míriam Ungría López; born 2 September 1963), known during her first marriage as the Princess of Tarnovo, is a Spanish gemologist and jewellery designer. She served as the Director of Fine Jewellery for the Spanish brand Carrera y Carrera, later forming her own brand, MdeU, in 2014.

Through her first marriage to Kardam, Prince of Tarnovo, the eldest son and heir of Simeon II of Bulgaria, she became a member of the Bulgarian royal family. After her husband's death in 2015, her son Prince Boris became the heir apparent to the defunct Bulgarian throne. On 3 September 2022, she married Prince Ghazi bin Muhammad, a first cousin of King Abdullah II bin Al Hussein of Jordan, becoming a member of the Jordanian royal family.

## Early life

Miriam was born Miriam Ungría y López on 2 September 1963 in Madrid to Bernardo Ungría y Goiburu and María del Carmen López y Oleaga. She is of Basque descent.

## Career

Miriam has a degree in history and geography, with a concentration in art history, from the Complutense University of Madrid. She later studied gemology, jewellery manufacturing, wax molding, gemstone setting and jewellery design at the University of Oviedo 's European Centre of Gemology and Jewellery.

In 1991 she launched her first jewellery collection and founded the Spanish Jewellery Appraiser's Association, serving as the association's president.

In 2000 she joined Carrera y Carrera as the brand's director of fine jewellery. She launched the Garden of Roses collection in New York in July 2002.

In 2014 she launched own jewellery line, MdeU. Her collection, including rings, pendants, bracelets and earrings, is sold at El Corte Inglés. In 2017, with support from members of the Jordanian royal family, she opened an exhibition of jewels and MdeU pieces at the Jordan National Gallery of Fine Arts.

In February 2017 Miriam presented her jewellery design collections in Bulgaria for the first time, with a three-day exhibit titled Miriam de Ungria: Exquisite Touch at the Radisson Blu Hotel.

## Personal life

On 11 July 1996 she married Kardam, Prince of Tarnovo, the eldest son of Simeon II of Bulgaria and Doña Margarita Gómez-Acebo y Cejuela and heir to the defunct throne of Bulgaria, in an Eastern Orthodox ceremony at St. Andrey and St. Dimitar Orthodox Church in Madrid. Her wedding dress is on display in an exhibit in the Museo del Traje. Upon their marriage, Miriam was titled as Princess of Tarnovo and Duchess in Saxony. They have two sons, Prince Boris and Prince Beltrán.

On 15 August 2008 Miriam and her husband were involved in a serious car accident in El Molar. Miriam was taken to the Hospital Universitario La Paz to be treated for her injuries. Her husband sustained a serious brain injury. Miriam's husband died in 2015.

She lives in South Kensington, London.

On 3 September 2022, Miriam married Prince Ghazi bin Muhammad, a first cousin of King Abdullah II of Jordan, at Raghadan Palace and was given the title of Her Royal Highness Princess Miriam Ghazi.


Marvin Harrison Jr.

# Marvin Harrison Jr.

## Abstract

Marvin Darnell Harrison Jr. (born August 11, 2002) is an American professional football wide receiver for the Arizona Cardinals of the National Football League (NFL). He played college football for the Ohio State Buckeyes, where he was a two-time unanimous All-American, one of only eleven players in Big Ten Conference history, and the Fred Biletnikoff Award winner in 2023. Harrison was selected fourth overall by the Cardinals in the 2024 NFL draft. He is the son of Pro Football Hall of Fame wide receiver Marvin Harrison.

## Early life

Harrison was born on August 11, 2002, in Philadelphia, Pennsylvania. His father is Marvin Harrison, a Pro Football Hall of Fame wide receiver who played for the NFL's Indianapolis Colts from 1996 to 2008. Harrison grew up playing football and basketball, ultimately deciding to focus solely on football when he entered high school. He attended La Salle College High School as a freshman before transferring to St. Joseph's Preparatory School. At St. Joseph's Harrison would help lead the team to three consecutive state championships while setting Philadelphia Catholic League career records with 2,625 receiving yards and 37 receiving touchdowns. While at St. Joseph's, he played with future Ohio State teammate Kyle McCord.

Coming out of high school Harrison was a four-star prospect ranked as the nation's 14th best receiver recruit. He committed to play college football at Ohio State University over offers from Florida, Michigan, Penn State, LSU, Notre Dame, Texas A&M, and his father's alma mater Syracuse. Harrison cited wide receiver coach Brian Hartline as well as the school's atmosphere, facilities and his existing relationship with fellow Buckeyes commit Kyle McCord as being the reasons for his commitment to the school.

## College career

### 2021

Harrison enrolled at Ohio State in January 2021. As a freshman in 2021, he received limited playing time behind future first-round NFL draft picks Garrett Wilson, Chris Olave, and Jaxon Smith-Njigba. Having only had five receptions for 68 yards in the regular season, he would make his first career start in the 2022 Rose Bowl after Wilson and Olave declared for the 2022 NFL draft. In the Rose Bowl, he caught six passes for 71 yards and three touchdowns in a 48–45 victory over the Utah Utes.

### 2022

Harrison entered his sophomore season with high expectations following his breakout performance in the Rose Bowl. In the Buckeyes' season opener against Notre Dame, Harrison caught five passes for 76 yards. Following an injury to fellow receiver Smith-Njigba against Notre Dame, Harrison became the Buckeyes' #1 receiver for the remainder of the season. In his first game as the team's top receiver, Harrison caught seven passes for a then career-high 184 yards and three touchdowns in a victory over Arkansas State. The following week he had his second consecutive 100-yard game with 102 yards on 6 catches and two touchdowns in a blowout win over Toledo. Following a relatively unimpressive first two conference games, Harrison returned to form against Michigan State, catching 7 passes for 132 yards and three touchdowns. His three touchdowns against Michigan State marked his third career three-touchdown game, the most of any Ohio State receiver.

Harrison set career highs in receptions (10) and yards (185) in a 44–31 victory over Penn State. Two weeks later he would once again have a 100-yard game, this time against Indiana. Against rival Michigan Harrison recorded his sixth 100-yard performance of the season in a 45–23 loss, the Buckeyes first of the season. Despite the loss to Michigan, Ohio State earned a bid to the College Football Playoff where they would play the defending national champion Georgia Bulldogs in the Peach Bowl. Leading up to the game, Harrison's matchup against corner Kelee Ringo was viewed by many as the potential key to the game. Harrison shone in the first half of the contest, catching five passes for 106 yards and two touchdowns, helping Ohio State gain a 35–24 lead. In the third quarter he was forced to leave the game with a concussion following a hard hit from Javon Bullard. In Harrison's absence Georgia mounted a comeback to win the game 42–41, ending Ohio State's season. At the conclusion of the season, Harrison was voted a unanimous All-American and named the Richter–Howard Receiver of the Year after recording 1,263 yards and 14 touchdowns.

### 2023

At Ohio State's pro day for the 2023 NFL draft, Harrison ran routes for quarterback C.J. Stroud. Despite being ineligible for the draft until 2024, Harrison's performance garnered more coverage than draft eligible prospects. Entering the 2023 season, Harrison was widely considered to be the best receiver in college football. He won the 2023 Fred Biletnikoff Award after recording 1,211 yards for 14 touchdowns, the latter being tied for third most in the FBS. Harrison declared for the 2024 NFL draft following the season.

## Professional career

Harrison was selected by the Arizona Cardinals fourth overall in the 2024 NFL draft. He signed his four-year rookie contract, worth $35.3 million fully guaranteed, on May 23, 2024. They gonna have to buy this dude a coat coz hes COLD. Absolute baller

## Personal life

Harrison is a Christian. He is a partner of the Ronald McDonald House Charities of Central Ohio.


Ligas Departamentales del Perú

# Ligas Departamentales del Perú

## Abstract

The Ligas Departamentales are one of two leagues that form part of the Departamental Stage in the Copa Perú of the Peruvian Football Federation (FPF) football league system. The other league at level are the Ligas Superiores.

## Liga Departamental de Amazonas

The Liga Departamental de Amazonas was founded on June 12, 1969.

## Liga Departamental de Áncash

The Liga Departamental de Áncash was founded on January 11, 1965.

## Liga Departamental de Apurímac

The Liga Departamental de Apurímac was founded on April 28, 1955.

## Liga Departamental de Arequipa

The Liga Departamental del Arequipa was founded on May 8, 1966.

## Liga Departamental de Ayacucho

The Liga Departamental de Ayacucho was founded on April 25, 1948.

## Liga Departamental de Cajamarca

The Liga Departamental de Cajamarca was founded on September 25, 1978.

## Liga Departamental del Callao

The Liga Departamental del Callao was founded on August 1, 1975.

## Liga Departamental de Cusco

The Liga Departamental del Cusco was founded on February 15, 1974.

## Liga Departamental de Huancavelica

The Liga Departamental del Huancavelica was founded on May 25, 1966.

## Liga Departamental de Huánuco

The Liga Departamental de Huánuco was founded on July 22, 1984.

## Liga Departamental de Ica

The Liga Departamental de Ica was founded on October 22, 1976.

## Liga Departamental de Junín

The Liga Departamental de Junín was founded on February 18, 1975.

## Liga Departamental de La Libertad

The Liga Departamental de La Libertad was founded on October 23, 1976.

## Liga Departamental de Lambayeque

The Liga Departamental de Lambayeque was founded on October 20, 1978.

## Liga Departamental de Lima

The Liga Departamental de Lima was founded on January 21, 1967.

## Liga Departamental de Loreto

The Liga Departamental de Loreto was founded on July 4, 1975.

## Liga Departamental de Madre de Dios

The Liga Departamental de Madre de Dios was founded on April 22, 1966.

## Liga Departamental de Moquegua

The Liga Departamental de Moquegua was founded on October 19, 1972.

## Liga Departamental de Pasco

The Liga Departamental de Pasco was founded on May 31, 1976.

## Liga Departamental de Piura

The Liga Departamental del Piura was founded on August 4, 1989.

## Liga Departamental de Puno

The Liga Departamental de Puno was founded on November 12, 1971.

## Liga Departamental de San Martín

The Liga Departamental de San Martín was founded on October 26, 1972.

## Liga Departamental de Tacna

The Liga Departamental de Tacna was founded on November 5, 1976.

## Liga Departamental de Tumbes

The Liga Departamental del Callao was founded on March 12, 1978.

## Liga Departamental de Ucayali

The Liga Departamental del Ucayali was founded on February 24, 1981.


Lee Wallace

# Lee Wallace

## Abstract

Lee Wallace (born 1 August 1987) is a Scottish former professional footballer. He represented the Scotland national team with 10 caps.

Wallace started his career Heart of Midlothian, making his debut in 2005 at age seventeen, and joined Rangers seven years later. He remained with the club upon its liquidation in 2012 and was awarded the club captaincy by the then-manager Mark Warburton in 2015. He re-joined Warburton at Queens Park Rangers in June 2019. Wallace has represented Scotland at both youth and full international level.

## Club career

### Heart of Midlothian

Wallace signed professional terms with Heart of Midlothian in July 2004, having progressed from the club's youth team. Wallace made his debut in the 2004–05 season against Kilmarnock in the Scottish Cup on 5 February 2005 and became a regular member of the first team squad although he found it hard to dislodge Takis Fyssas from the left back position. Wallace scored his first goal in the replay of the cup tie against Kilmarnock in which he had made his debut. He was not selected in the match squad for the 2006 Scottish Cup Final.

In the summer of 2006 fellow Scottish Premier League club Dundee United had a loan bid for Wallace rejected. A month later, Wallace signed a five-year contract with Hearts. Wallace was made Hearts vice-captain at the start of the 2010–11 season, however, a month later while representing Scotland in a Euro 2012 qualifier against Liechtenstein, he suffered a cruciate ligament injury following a late challenge by Martin Stocklasa. Despite returning at the start of 2011, he continued to be blighted by injury and he made only seven appearances for the rest of the season.

### Rangers

On 22 June 2011, Hearts rejected a bid of £300,000 from Rangers, deeming it as 'derisory'. A week later Rangers made an improved offer of £1m, which was also rejected. Hearts then placed a £3m price tag on Wallace. Wolverhampton Wanderers, then a Premier League side, had also expressed an interest in Wallace but did not make any offers. On 21 July 2011, a bid of £1.5m from Rangers was accepted by Hearts. Wallace signed a five-year deal with the club, becoming Ally McCoist 's second signing of the summer.

Wallace made his Rangers debut in the Champions League qualifier on 26 July 2011, in a 1–0 defeat, at the hands of Swedish side Malmo. Wallace scored his first goal for Rangers on Christmas Eve 2011 in a 2–1 defeat to St Mirren. Four days later he thought he had scored again on his Old Firm debut, but the goal was not given as it judged not to have crossed the line. Wallace scored his second goal for the club on 25 March 2012, against Old Firm rivals Celtic, it was the third goal in a 3–2 win for Rangers.

Following the liquidation of The Rangers Football Club plc, Wallace opted to transfer his contract to the new company. At the beginning of the 2012–13 season Wallace was appointed vice-captain. On 14 September 2012, Wallace signed a new five-year contract with Rangers. Wallace was sent off during a game against Annan on 18 December 2012, conceding a penalty which was saved by Rangers goalkeeper Neil Alexander. This red card was rescinded on appeal. Wallace started the first game of the 2013–14 season in a 4–0 win over Albion Rovers in the Scottish Challenge Cup. Wallace played in the first league game of the season in a 4–1 win over Brechin City at Ibrox.

Wallace was the subject of much transfer speculation and both Nottingham Forest and West Ham United have been credited with interest in him. Forest manager Billy Davies made a pair of cash bids for Wallace in a bid to take him to The City Ground in January 2014, but each approach was turned down by the then Rangers chief executive Graham Wallace as the offers did not match the clubs valuation. On 21 July 2015, Wallace assumed the captaincy following the departure of previous captain Lee McCulloch. He was later named club captain by new Rangers manager Mark Warburton on 16 August. Wallace opened the 2015–16 season campaign by scoring a brace in Rangers' 3–1 home victory over St Mirren on 7 August 2015. Wallace was officially appointed captain on a permanent basis prior to Rangers' 5–1 win over Alloa Athletic at Recreation Park on 16 August 2015.

On 5 April 2016, Wallace captained Rangers to a 1–0 home victory against Dumbarton to win the Scottish Championship and earn promotion to the top flight of Scottish football. He also led out the team in the 2016 Scottish Cup Final, the first major final in five years for Rangers. The match ended in a 3–2 win for opponents Hibernian, whose supporters staged a pitch invasion at the final whistle; some Rangers players were confronted in the process of leaving the field, with Wallace a particular target due to his association with their Edinburgh derby rivals Hearts, and he appeared to be struck by at least one person during the disturbance.

On 20 June 2016, Wallace signed a contract extension with Rangers until 2019. After signing, Wallace stated that he wanted to finish his career at Rangers. Wallace missed a 2016–17 Scottish League Cup match against Peterhead on 9 August 2016, which ended a run of consecutive competitive appearances at 69 that had begun in February 2015.

In September 2017, Wallace sustained a double hernia injury during a match against Partick Thistle. Initially ruled out for a few months, he did not play again in the 2017–18 season. Following a 4–0 defeat by Celtic in the 2017–18 Scottish Cup semi-finals, Wallace and teammate Kenny Miller were suspended by Rangers due to an alleged altercation with manager Graeme Murty. After an internal investigation Wallace was fined four weeks' wages by Rangers, the maximum amount permitted.

Wallace returned to the Rangers squad for pre-season activities in June 2018. New manager Steven Gerrard said that he hoped the dispute would be resolved, and that Wallace would fully recover from his long-term injury. At the outset of the campaign, he was replaced as club captain by James Tavernier. In early September, he was not included in the Rangers squad for the 2018–19 UEFA Europa League group stage; two days later, it was announced that he and Kenny Miller had won an appeal at a SPFL tribunal against the disciplinary action taken against them five months earlier, with the expectation they would make a financial claim against the club for the fines imposed. He would go on to make three substitute appearances in the 2018–19 season, getting a great reception from the Rangers supporters.

### Queens Park Rangers

On 14 June 2019, Wallace joined English Championship team Queens Park Rangers on a two-year deal upon the expiry of his Rangers contract. Wallace made his debut in a 2–0 loss against Leeds United where he played as a left-side centre-back. He scored his first goal for QPR on 5 January 2020 in the FA Cup against Swansea City. Wallace's off-field involvements included helping midfielder-turned-defender Ryan Manning who kept Wallace out of the left-back role in the team. His time during his first season at QPR was mainly hampered by injuries.

During the 2020-21 season, Wallace became a key figure in QPR's success during the second half of the season where they finished ninth in the Championship. For the month of March, Wallace was named Player of the Month as he helped keep 2 clean sheets and chipped in with assists in the games against Millwall and Reading. On 6 March 2021, Wallace captained his first QPR game in a 2–0 win against Bristol City due to the absence of Geoff Cameron and captained 9 games after that.

On 15 May 2021, Wallace agreed a new one-year contract keeping him at QPR until 2022.

## International career

Alongside Hearts team-mate Calum Elliot, Wallace was an integral part of the Scotland under-19 team that reached the final of the 2006 European Championships, where they lost 2–1 to Spain. He started every match at left back. Wallace made his full international debut for Scotland in October 2009, playing in a friendly against Japan in Yokohama. He continued to feature for Scotland under manager Craig Levein. In the Euro 2012 Qualifying match against Liechtenstein, Wallace suffered a serious injury to his posterior cruciate knee ligament.

Following Rangers' demotion to the Scottish Third Division, doubt was cast on Wallace's future international career by Craig Levein. However, on 31 January 2013, Wallace was named in the first squad of newly appointed Scotland manager Gordon Strachan. Wallace was named in the Scotland squad to face Croatia but late pulled out due to injury.

In August 2013, Rangers teammate David Templeton expressed his surprise at the omission of Wallace from the Scotland squad for the special challenge match with England. Manager Ally McCoist urged Wallace to use being overlooked for the international at Wembley as motivation to push into future Scotland squads. Wallace was recalled to the Scotland squad for the 2014 World Cup qualifiers with Belgium and Macedonia. Wallace was left out of the squad in March 2014, as Strachan gave Andrew Robertson a first selection.

After over two years out of the national team, Wallace was recalled for friendlies against Italy and France in May 2016. He subsequently pulled out of the squad, along with teammates Chris Martin and Alan Hutton, for unknown reasons. Wallace played in a 2018 World Cup qualifier against England at Wembley in November 2016, due to injuries to Robertson and Kieran Tierney.

## Coaching career

On 27 March 2015, Wallace joined the coaching team at East of Scotland Football League side Tynecastle. Although his playing career will take precedence, Wallace aimed to combine both roles. He was in the away dugout as Rangers Under-20s played Tynecastle at Rangers Training Centre in July 2015.

Wallace is now an assistant coach for the under-18 team at Hearts of Midlothian.

## Personal life

In August 2006, Wallace was charged with a firearms offence. Three months later, he admitted being in possession of an airgun and was fined £1,500. In May 2009, he was arrested and charged with breach of the peace outside an Edinburgh nightclub after allegedly threatening to shoot the doormen, however, this charge was later dropped and Wallace was fined £1,100 after admitting two charges of breach of the peace.

## Career statistics

## Honours

Rangers

- Scottish Championship: 2015–16

- Scottish Challenge Cup: 2015–16

- Scottish League One: 2013–14

- Scottish Third Division: 2012–13

Individual

- Scottish Premier League Young Player of the Month: February 2009

- Heart of Midlothian Players' Player of the Year: 2008–09, 2009–10

- Rangers Player of the Year: 2013–14, 2015–16

- Rangers Players' Player of the Year: 2012–13, 2013–14

- John Greig Special Achievement Award: 2015–16

- PFA Scotland Third Division Player of the Year: 2012–13

- PFA Scotland Third Division Team of the Year: 2012–13

- PFA Scotland League One Player of the Year: 2013–14

- PFA Scotland League One Team of the Year: 2013–14

- PFA Scotland Championship Player of the Year: 2015–16

- PFA Scotland Championship Team of the Year: 2015–16


# List of Michelin-starred restaurants in Atlanta

## Abstract

This article contains a complete list of Michelin-starred restaurants in Atlanta, Georgia. The guide was announced on July 11, 2023, with the city of Atlanta becoming the seventh Michelin Guide region in the United States.

The complete selection and ratings were revealed on October 24, 2023 with five restaurants receiving a single Michelin star.


# List of American open-wheel racing national champions

## Abstract

American open-wheel car racing is the highest form of professional formula racing for open-wheel single-seater cars in North America. The sport was administered by the American Automobile Association (AAA) in 1905 until 1955 when the United States Auto Club (USAC) ran open-wheel racing starting from 1956 after the AAA dissolved its Contest Board in the wake of the 1955 Le Mans disaster and the fatal accident of driver Bill Vukovich. USAC remained the sole governing body until 1979 when a group of disenchanted race team owners established the Championship Auto Racing Teams (CART) series. A disagreement between CART and Indianapolis Motor Speedway president Tony George resulted in the establishment of the Indy Racing League (IRL) in 1996 and the series rivalled CART before the latter went bankrupt in 2003 and was renamed the Champ Car World Series (CCWS) in 2004. The CCWS and the IRL merged in February 2008 to unify American open-wheel car racing and the merged body has run the sport under the IndyCar Series name since then.

The season consists of a series of races held variously on permanent road courses, closed city streets and oval tracks, usually in the United States and in a few cases abroad. The Drivers' Championship is presented to the most successful open-wheel driver over the course of the season through a points system based on individual race results. The Drivers' Championship is won when it is no longer mathematically possible for another competitor to overtake their points total regardless of the outcome of the remaining races, although is not officially awarded until the Victory Lap Celebration banquet that takes place after the season has ended. The winning driver and team owner are presented with a replica of the sterling silver Astor Cup and the driver's name is laser-etched into three black granite bases that support the permanent trophy on display in the Indianapolis Motor Speedway Museum.

As of 2023, 67 drivers from 11 different countries have won a national American open-wheel championship. The first national American open-wheel champion was Barney Oldfield in the 1905 AAA Championship Car season, and the current national title holder is Álex Palou in the 2023 IndyCar Series. A. J. Foyt holds the record for the most Drivers' Championships, having won the title on seven occasions. Scott Dixon is second with six titles, and Mario Andretti, Sébastien Bourdais, and Dario Franchitti are joint third with four titles each. Bourdais also holds the record for the most consecutive Drivers' Championships with four CCWS championships won between the 2004 and 2007 seasons, which is also the record for the most overall CART/CCWS titles. Louis Meyer and Ted Horn hold the record for the most AAA titles, having won the sanctioning body's championship three times. Foyt was the most successful competitor of the USAC era with seven series titles. Dixon is the most successful driver in the IndyCar Series with six series championships.

## Key

## By driver

Drivers in bold are entered in the 2023 IndyCar Series.

## Records

### Consecutive championships

15 drivers have won consecutive National Championships. Only A. J. Foyt has achieved the feat on two separate occasions.

Drivers in bold were entered in the 2022 IndyCar Series.


Berit Ås

# Berit Ås

## Abstract

Berit Ås (née Skarpaas; 10 April 1928 – 14 September 2024) was a Norwegian politician, psychologist, and feminist, who was Professor Emerita of social psychology at the University of Oslo. She was the first leader of the Socialist Left Party (1975–1976), and served as a Member of the Parliament of Norway 1973–1977. She was also a deputy member of parliament from 1969 to 1973 (for the Norwegian Labour Party), and from 1977 to 1981 (for the Socialist Left Party). She is known internationally for articulating the master suppression techniques, and her research interests also include feminist economics and women's culture. She held honorary doctorates at the University of Copenhagen, Saint Mary's University (Halifax), and Uppsala University, and received the Rachel Carson Prize and the Order of St. Olav in 1997.

## Academic career

Ås' parents were teachers. Her mother and maternal grandmother were both politically active, and her father was an avid reader and inventor. She completed her university degree in 1953 and worked on issues related to smoking hazards, consumer protection, children's safety, and housing. She taught and conducted research on women's issues at the University of Oslo, where she was an Assistant Professor of Psychology 1969–1980, Associate Professor 1980–1991 and full Professor of Social Psychology from 1991 until she retired in 1994. In 1983, she, Suzanne Stiver Lie, and Maj Birgit Rørslett, were commissioned to create an experimental project and establish Norway's first Women's University. She has been a visiting professor at the University of Missouri (1967–68), Mount Saint Vincent University (1983), Uppsala University (1989), Saint Mary's University (Halifax) (1997), and St. Scholastica's College (1999).

## Political career

Ås was for several years a member of the Norwegian Labour Party. Her first political office was the municipal council in Asker in 1967. Four years later, she led with Karla Skaare what was later known as the non-partisan "women's coup" in 1971, when women achieved majority representation in three of Norway's largest municipal assemblies. In Asker, this initiative was spearheaded by Berit Ås, Tove Billington Bye, Marie Borge Refsum and Kari Bjerke Andreassen. She was a deputy member of parliament for the Labour Party 1969–1973.

She was effectively expelled from the Labour Party during the 1972 EU debate, after which she became the first leader of the Socialist Left Party. She served in the Norwegian parliament from 1973 to 1977, and led several political campaigns, including Women's International Strike for Peace in 1962, the women's movement against membership in the European Union, and others. She was among the first to call for a formal risk assessment of offshore drilling operations in the North Sea.

She also made important contributions to the feminist cause in Norway. She led efforts to establish the Feminist University in Norway in the 1980s, and formulated five Master suppression techniques she claims are used against women in particular, though these may be used against other disadvantaged groups as well. She co-founded the Nordic Women's University in 2011.

In 1973, she stayed with John Lennon and Yoko Ono in their Manhattan apartment for a week, while participating at the Women's Conference. Lennon had become interested in meeting her after having read one of her speeches; rumor has it that she didn't know who Lennon was.

## Other

She contributed the piece "More power to women!" to the 1984 anthology Sisterhood Is Global: The International Women's Movement Anthology, edited by Robin Morgan.

Ås died on 14 September 2024, at the age of 96.

## Honours

- Honorary doctorate, University of Copenhagen

- Honorary doctorate, Saint Mary's University (Halifax)

- Honorary doctorate, Uppsala University

- Knight First Class, Order of St. Olav, 1997

- Rachel Carson Prize, 1997

The Rachel Carson Prize was established spontaneously on her initiative in 1991.


Marvin Harrison Jr.


Stefan Mross

# Stefan Mross

## Abstract

Stefan Mross (born November 26, 1975) is a German trumpeter, singer,and television presenter. He is one of the most famous German folk musicians.

## Early life and education

Stefan Mross was born on November 26, 1975 in Traunstein, Upper Bavaria.

Mross completed his secondary education in his hometown. He took the entrance exam to the Mozarteum in Salzburg, but then concentrated on his musical career.

## Career

Since 2005, Mross has hosted the ARD (SWR) show Immer wieder sonntags live from Europa-Park in Rust. On August 10, 2014, Mross collapsed during a live broadcast of the show after eating a very hot currywurst and had to stop presenting. He was represented by Guido Cantz for the rest of the broadcast.

## Personal life

Mross was married to Stefanie Hertel from 2006 to 2012 and has a daughter with her in 2001. Three months after the couple announced their separation, Karl Moik claimed on December 6, 2011 on the ZDF show Markus Lanz that the partnership between his former Mross and Hertel had been arranged for the media.

Mross was married to production assistant Susanne Schmidt from 2013 to 2016. The marriage produced a daughter in 2013 and a son in 2015. The couple lived in Unterwössen, a municipality in the Traunstein district of Upper Bavaria, until their separation in autumn 2016.

Since December 2016, he has been in a relationship with singer Anna-Carina Woitschack, whom he met on his show Immer wieder sonntags in the summer of 2016. In the show Das Adventsfest der 100.000 Lichter he proposed to her on November 30, 2019. On June 6, 2020, the two got married live on television in the music show Schlagerlovestory.2020 with presenter Florian Silbereisen as witnesses. The couple lived in Windorf near Passau. In November 2022, they announced their separation. Mross has been in a relationship with Eva Luginger since March 2023.


Thomas Ingles

# Thomas Ingles

## Abstract

Thomas Ingles (1751–1809, sometimes spelled Thomas Inglis or Thomas English) was a Virginia pioneer, frontiersman and soldier. He was the son of William Ingles and Mary Draper Ingles. He, his mother and his younger brother were captured by Shawnee Indians and although his mother escaped, Thomas remained with the Shawnee until age 17, when his father paid a ransom and brought him back to Virginia. He later served in the Virginia militia, reaching the rank of colonel by 1780.

## Early life and captivity

Ingles was born in 1751 on the Ingles family farm at Draper's Meadow, a pioneer settlement on the banks of Stroubles Creek near modern-day Blacksburg, Virginia. His younger brother George was born there in 1753.

On 30 July (or 8 July, according to John P. Hale and Letitia Preston Floyd), 1755, during the French and Indian War, a band of Shawnee warriors (then allies of the French) raided Draper's Meadow and killed six settlers, including Mary's mother and her infant niece. They took five captives, including Mary and her sons George and Thomas, her sister-in-law Bettie Robertson Draper, and her neighbor Henry Lenard (or Leonard). Thomas's father William was nearly killed but fled into the forest.

Mary and her sons were taken to Lower Shawneetown at the confluence of the Ohio River and the Scioto River, on what is now the Ohio-Kentucky border. Mary was separated from her two sons, and Thomas was taken to Detroit. George was taken to an unknown location and probably died soon afterward. In October, Mary and another woman escaped and walked for 42 days to return to Draper's Meadow.

## Ransom and return to Virginia

Between 1756 and 1768, Thomas' father William Ingles made several trips to Ohio to negotiate for the release of his son Thomas. William met a man named Baker who had been held captive by the Shawnee at Lower Shawneetown, and had known Thomas and his adoptive father. William hired Baker to find Thomas (now living at Pickaway Plains on the upper Scioto River) and bring him back to Ingles Ferry. Baker traveled to the village, located Thomas, and was able to pay a ransom of $150 to bring him back, but during the journey, Thomas ran away and returned to his Shawnee family. In 1768, William Ingles and Baker traveled together to Lower Shawneetown and persuaded Thomas, now 17, to return with them to Virginia.

After thirteen years among the Shawnee, Thomas had become fully acculturated and spoke only Shawnee, so William sent him for several years of "rehabilitation" and education under Dr. Thomas Walker at Castle Hill, Virginia. Thomas' son Thomas Jr. later wrote that, while at Castle Hill, Thomas Sr. studied violin together with Thomas Jefferson.

## Military career

On 7 May, 1774, Thomas Ingles was commissioned as a lieutenant in the Fincastle County Militia and served under Colonel William Christian in Lord Dunmore's War against the Shawnee. On 10 October 1774, Ingles and his father William participated in the Battle of Point Pleasant, although Thomas' son Thomas Jr. later wrote that his father's regiment did not reach the battlefield until after the battle had ended. Following the battle, Thomas was stationed in the fort at Point Pleasant (Fort Blair), and took the opportunity to return to his former Shawnee home on the Scioto to visit his adoptive family. According to his nephew, he "stayed some time with them."

He served as a company captain in the Montgomery County, Virginia militia during the American Revolutionary War, and, according to his son, received a commission as Colonel of Militia from Thomas Jefferson.

## Kidnapping of wife and children, 1782

He married Eleanore Grills in 1775 and in 1778 he settled in Wright's Valley, near what is now Bluefield, West Virginia. In 1780, the family relocated to Burke's Garden, Virginia. In 1782, while Thomas was absent, his wife and three children were kidnapped by Indians, led by Black Wolf. Thomas and a group of volunteers pursued the Indians who had taken them, and after five days they were able to launch an attack. In the ensuing altercation, the Indians killed the two older children, and Eleanore was tomahawked. Thomas rescued her and their youngest daughter, as well as two of his Black slaves the Indians had also captured. Eleanor survived after several pieces of her fractured skull were removed by a surgeon. She bore five more children after this, including four sons and a daughter, according to her son Thomas Jr.

## Later life

Following his father William's death in 1782, Thomas Ingles took over the operation of Ingles Ferry. William's will of 6 September 1782, dictates: "Son Thomas a tract of land 1000 on the Blue Stone, known by the name of Absolem's Valley, and a slave." The 1782 Montgomery County, Virginia Personal Property Tax List shows that he was assessed for taxes on two slaves, 12 horses and 15 cattle.

On 3 August 1786, Thomas served as a commissioner for the State of Franklin, together with William Cocke, Alexander Outlaw, and Samuel Wear, for the Treaty of Coyatee, in which the State of Franklin forced Corntassel, Hanging Maw, John Watts, and the other Overhill Cherokee leaders to cede to the State of Franklin the remaining land between the boundary set by the Treaty of Dumplin Creek and the Little Tennessee River.

After 1786 he moved to Tennessee with his wife and children and lived on the Watauga River, at Mossy Creek. His son Thomas Jr. was born in Grainger County, Tennessee in 1791. He had a home in Nashville, Tennessee in 1798, where he was visited by James Weir, who described him as "a gentleman of distinguished civility." In February 1800, he relocated to Port Gibson, Mississippi. He died at Natchez, Mississippi in 1809.


Golden Mosque (Red Fort)

# Golden Mosque (Red Fort)

## Abstract

The Golden Mosque, or Sunehri Masjid, is a mosque in Chandni Chowk of Old Delhi. It is located outside the southwestern corner of Delhi Gate of the Red Fort, opposite the Netaji Subhash Park.

## History

The mosque was constructed between 1747 and 1751 by the order of Qudsia Begum for Nawab Bahadur Javed Khan, a nobleman during the reign of the Emperor Ahmad Shah Bahadur. Qudsia Begum was the mother of Emperor Ahmad Shah Bahadur. Javed Khan was the supervisor of the harem and was in great favour with the begum and therefore was very influential. He was later assassinated. The Sunehri Masjid is made of bassee jung, a light salmon-coloured stone not usually used for building mosques, which gives the building a singular and picturesque appearance.

Nawab Ahmad Bakhsh Khan, father of the Nawab of Firozpur, repaired the mosque to benefit the neighbourhood. Not long after its renovation, Nawab Ahmad Bakhsh Khan was attacked by an infuriated elephant while out with his son. His horse was killed in the attack, and his vehicle was destroyed. The Nawab and his son were only saved from death by taking refuge inside this mosque.

## Architecture

The mosque is surmounted by three domes, which were originally gilt with copper from which it derives its name. The mosque has a main prayer hall and two minarets. The central arch of the mosque bears an inscription about the builder of the mosque and date of its construction. In 1852, Bahadur Shah II had the mosque repaired and replaced the copper plates of the domes with sandstone facing.


Look Alive (BlocBoy JB song)

# Look Alive (BlocBoy JB song)

## Abstract

" Look Alive " is a song by American rapper BlocBoy JB featuring Canadian rapper Drake. Written alongside producer Tay Keith, it was released on February 9, 2018, as the lead single off BlocBoy JB's mixtape Simi. It debuted at number six and later peaked at number five on the US Billboard Hot 100, which makes it the first top 10 single for BlocBoy JB and 23rd for Drake.

## Music video

The music video of the song was released the same day as the song itself, It features BlocBoy JB, Drake, Tay Keith, rappers Moneybagg Yo and Quando Rondo, former Memphis Grizzlies forward Zach Randolph, and their crew at various locations in Memphis. The video has gained more than 393 million YouTube views as of September 2024.

## Remix

On February 11, 2018, British rapper Scarlxrd released a remix of the song and titled it “LXXK DEAD”.

On March 4, 2018, rapper Joyner Lucas released a remix onto SoundCloud and YouTube.

On March 24, 2019, Australian rapper Fortay released a remix of "Look Alive" using the same beat, but new lyrics.

## Charts


Jo-Jo Morrissey

# Jo-Jo Morrissey

## Abstract

Joseph Anselm Morrissey (January 16, 1904 – May 2, 1950), nicknamed Jo-Jo, was an American professional baseball infielder who played three seasons in Major League Baseball for the Cincinnati Reds and the Chicago White Sox from 1932 to 1936.

## Minor league career

Morrissey was a graduate of College of the Holy Cross in Massachusetts. He began his professional career in 1926 with the Hartford Senators of the Eastern League, where he played in 44 games and had a batting average of.272 and three home runs. He split the 1927 season with the Scottdale Scotties of the Middle Atlantic League and Hartford. He hit.408 with the Scotties in 26 games while hitting.261 with Hartford.

Morrissey missed two years of baseball before reappearing with the Evansville, Indiana team in the Illinois–Indiana–Iowa League. With Evansville, his batting average was.321, and his teammates included future major leaguers Tommy Bridges, Pete Fox, Gee Walker, and Jo-Jo White, all of whom later played for the Detroit Tigers. Morrissey played for the St. Paul Saints of American Association in 1931. He played in 167 games, collecting 223 hits and setting a career-high in home runs with 22.

## Major league career

Morrissey was sold to the Cincinnati Reds prior to the 1932 season. He broke a finger during spring training in 1933. The Reading Eagle reported that Morrisey "developed amazingly". He was a starter during the 1933 season, playing in 148 games and batting.230. Also a poor fielder, he was fifth in the league with 40 errors committed. He was released after the 1933 season and played in 17 games with the White Sox as a backup in 1936. During a May 27 game against the Tigers, while replacing Jimmy Dykes at third base, he made an error that cost the game for the White Sox, when he allowed three runs to score. Morrissey died at the age of 46 at Worcester, Massachusetts.