Background: Metalloproteins and metal-protein complexes play key roles in all
organisms. For example, certain metalloproteins are involved in metal homeostasis and
detoxification, or oxidative stress protection; whereas, metals serve as essential cofactors
in a large number of metal-protein complexes.
Objective: Present work attempts to critically review methods for assessing the structure,
characterization of the metal binding sites, with RNA involved in the various process of a
living being are discussed.
Method: The binding of Hg(II) and Mo (II) ions have been studied with RNA at different
pH values and temperatures by the polarographic and spectrometric techniques. It is
observed that binding data depend on pH and temperature.
Results: The intrinsic association constants (k) and the number of binding sites (n) were
calculated from Scatchard plots. The free energies of aggregation, ΔG associated with the
binding interaction of the Hg (II) and Mo(II) and RNA were calculated. The negative
values of the ΔG confirm the feasibility of interaction between the metals and RNA.
Conclusion: All the observations recorded in this paper indicate that the Hg (II) and Mo
(II) ions have a good affinity of binding with RNA and the number of binding sites is
dependent on various physical and chemical factors. Both ions when bind with the RNA
induce metabolic function at tissue level in fishes in the aquatic environment.