Synthesis of the active sites of molybdoenzymes: MoO < inf > 2 < /inf > (VI) and MoO(IV)-dithiolene complexes mimicking enzymatic reactions of sulphite oxidase with saturation kinetics

Abstract

[MoVIO2(S2C2(CN)2)2]2− (┘1) and [MoIVO(S2C2(CN)2)2]2− (2) mimick oxidoreductase enzymatic activities of sulphite oxidase with biological electron donor, SO(Formula presented.), and in vitro electron acceptor, [Fe(CN)6]3−, demonstrating proton coupled electron transfer reaction in water and inhibition of the oxidation of (2) in the presence of KCN. The sulphite exidizing system is characterized by substrate saturation kinetics indicating the biological significance of the reactions © 1992, Indian Academy of Sciences. All rights reserved.