1. Introduction. the hydrocorphinoid nickel complex 1 (F430) [l] is the cofactor of methyl-coenzyme M reductase which catalyzes the last step of methane formation in methanogenic bacteria according to Scheme l a . The mechanism by which the enzyme
Coenzyme F430 from Methanogenic Bacteria: Oxidation of F430 Pentamethyl Ester to the Ni(III) Form
β Scribed by Bernhard Jaun
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- German
- Weight
- 452 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0018-019X
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β¦ Synopsis
~ ~~
F430M, the pentamethyl ester of coenzyme F430, can be oxidized reversibly by one electron. The oxidation potential has been determined, and the electrolytically prepared oxidation product was characterized by its UVjVIS and ESR spectrum. The strongly anisotropic and nearly axial ESR spectrum is consistent with a S = ' / > species with the unpaired-electron spin density predominantly in a dZ2-type orbital of the central nickel ion. The properties of Ni(III)F430M are discussed in the context of two hypothetical mechanisms for the catalytic role of coenzyme F430 in methyl coenzyme M reductase, which catalyses the last step of methane formation in methanogenic bacteria.
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## Abstract A methylnickel(II) derivative of coenzyme F430 (1) was proposed as an intermediate in the enzymic process catalyzed by methylβCoM reductasc. Indirect evidence points to formation of CH~3~βF430M^II^ in the reaction of F30M^1^ (obtained from F430M^II^ (2)) with eleclrophilic methyl donors