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Coenzyme F430 from Methanogenic Bacteria: Mechanistic studies on the reductive cleavage of sulfonium ions catalyzed by F430 pentamethyl ester

✍ Scribed by Shu-Kun Lin; Bernhard Jaun

Publisher: John Wiley and Sons
Year: 1992
Tongue: German
Weight: 678 KB
Volume: 75
Category: Article
ISSN: 0018-019X
DOI: 10.1002/hlca.19920750504

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✦ Synopsis

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

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Coenzyme F430 from Methanogenic Bacteria

Coenzyme F430 from Methanogenic Bacteria: Oxidation of F430 Pentamethyl Ester to the Ni(III) Form

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## ~ ~~ 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 spectr

Coenzyme F430 from Methanogenic Bacteria

Coenzyme F430 from Methanogenic Bacteria: Detection of a Paramagnetic Methylnickel(II) Derivative of the Pentamethyl Ester by 2H-NMR Spectroscopy

✍ Shu-Kun Lin; Bernhard Jaun 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 German ⚖ 740 KB

## Abstract A methylnickel(II) derivative of coenzyme F430 (1) was proposed as an intermediate in the enzymic process catalyzed by methyl‐CoM reductasc. Indirect evidence points to formation of CH~3~–F430M^II^ in the reaction of F30M^1^ (obtained from F430M^II^ (2)) with eleclrophilic methyl donors