You will be shown an abstract from a biomedical research paper. Given this abstract, your task is to extract all unique entities of the following types: ["Protein", "Chemical"].

Please return the output as a JSON object of the format: {"Chemical" : ["Dexamethasone", ...], "Protein" : ["BRCA-1", ...]}. The keys should be entity types and values should be lists of extracted entities belonging to the corresponding type. If you cannot find entities belonging to a specific type, the value should be [].

Only output the JSON object and do not include any additional text.

Abstract:

Tyrosinase catalyzes an unusual oxidative decarboxylation of 3,4-dihydroxymandelate.
Tyrosinase usually catalyzes the conversion of monophenols to o-diphenols and oxidation of diphenols to the corresponding quinones. However, when 3,4-dihydroxymandelic acid was provided as the substrate, it catalyzed an unusual oxidative decarboxylation reaction generating 3,4-dihydroxybenzaldehyde as the sole product. The identity of the product was confirmed by high-performance liquid chromatography (HPLC) as well as ultraviolet and infrared spectral studies. None of the following enzymes tested catalyzed the new reaction: galactose oxidase, ceruloplasmin, superoxide dismutase, ascorbate oxidase, dopamine beta-hydroxylase, and peroxidase. Phenol oxidase inhibitors such as phenylthiourea, potassium cyanide, and sodium azide inhibited the reaction drastically, suggesting the participation of the active site copper of the enzyme in the catalysis. Mimosine, a well-known competitive inhibitor of tyrosinase, competitively inhibited the new reaction also. 4-Hydroxymandelic acid and 3-methoxy-4-hydroxymandelic acid neither served as substrates nor inhibited the reaction. Putative intermediates such as 3,4-dihydroxybenzyl alcohol and (3,4-dihydroxybenzoyl)formic acid did not accumulate during the reaction. Oxidation to a quinone methide derivative rather than conventional quinone accounts for this unusual oxidative decarboxylation reaction. Earlier from this laboratory, we reported the conversion of 4-alkylcatechols to quinone methides catalyzed by a cuticular phenol oxidase [Sugumaran, M., & Lipke, H. (1983) FEBS Lett. 155, 65-68]. Present studies demonstrate that mushroom tyrosinase will also catalyze quinone methide production with the same active site copper if a suitable substrate such as 3,4-dihydroxymandelic acid is provided.
{"Chemical": ["4-Hydroxymandelic acid", "phenylthiourea", "dopamine", "Mimosine", "Phenol", "3,4-dihydroxymandelate", "sodium azide", "ascorbate", "quinone", "3,4-dihydroxymandelic acid", "3,4-dihydroxybenzyl alcohol", "(3,4-dihydroxybenzoyl)formic acid", "quinone methide", "monophenols", "3-methoxy-4-hydroxymandelic acid", "copper", "superoxide", "diphenols", "3,4-dihydroxybenzaldehyde", "quinone methides", "potassium cyanide", "galactose", "4-alkylcatechols", "phenol"], "Protein": ["superoxide dismutase", "tyrosinase", "galactose oxidase", "mushroom tyrosinase", "ascorbate oxidase", "Phenol oxidase", "Tyrosinase", "peroxidase", "dopamine beta-hydroxylase", "ceruloplasmin"]}