Sarkar, Sabyasachi ; Das, Samar K. (1992) Synthesis of the active sites of molybdoenzymes: MoO2(VI) and MoO(IV)-dithiolene complexes mimicking enzymatic reactions of sulphite oxidase with saturation kinetics Proceedings of the Indian Academy of Sciences - Chemical Sciences, 104 (3). pp. 437-441. ISSN 0253-4134
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Official URL: http://www.ias.ac.in/j_archive/chemsci/104/4/437-4...
Abstract
[MoVIO2(S2C2(CN)2)2]2- (1) and [MoVIO(S2C2(CN)2)2]2- (2) mimick oxidoreductase enzymatic activities of sulphite oxidase with biological electron donor, SO32−, andin 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
Item Type: | Article |
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Source: | Copyright of this article belongs to Indian Academy of Sciences. |
Keywords: | Sulphite Oxidase; Proton Coupled Electron Transfer; Saturation Kinetics; Inhibition; Functional Analogues; Trimethylamine N-oxide Reductase |
ID Code: | 98339 |
Deposited On: | 24 Jun 2014 05:02 |
Last Modified: | 19 May 2016 10:21 |
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