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Coenzyme F430 from Methanogenic Bacteria: Oxidation of F430 Pentamethyl Ester to the Ni(III) Form
Author(s) -
Jaun Bernhard
Publication year - 1990
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19900730818
Subject(s) - chemistry , reductase , cofactor , methanogenesis , context (archaeology) , bacteria , nickel , stereochemistry , electron transfer , unpaired electron , methane , enzyme , medicinal chemistry , photochemistry , organic chemistry , molecule , paleontology , genetics , biology
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 UV/VIS and ESR spectrum. The strongly anisotropic and nearly axial ESR spectrum is consistent with a S = ½ species with the unpaired‐electron spin density predominantly in a d z 2‐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.