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

dc.contributor.author	Sarkar, Sabyasachi
dc.contributor.author	Das, Samar K.
dc.date.accessioned	2022-03-27T08:45:26Z
dc.date.available	2022-03-27T08:45:26Z
dc.date.issued	1992-01-01
dc.description.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.
dc.identifier.citation	Proceedings of the Indian Academy of Sciences - Chemical Sciences. v.104(3)
dc.identifier.issn	02534134
dc.identifier.uri	10.1007/BF02839554
dc.identifier.uri	https://link.springer.com/10.1007/BF02839554
dc.identifier.uri	https://dspace.uohyd.ac.in/handle/1/11705
dc.subject	functional analogues
dc.subject	inhibition
dc.subject	proton coupled electron transfer
dc.subject	saturation kinetics
dc.subject	Sulphite oxidase
dc.subject	trimethylamine N-oxide reductase
dc.title	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
dc.type	Journal. Article
dspace.entity.type

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