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The Biological Methane‐Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate
Author(s) -
Shima Seigo
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201606269
Subject(s) - methane , catalysis , chemistry , cofactor , stereochemistry , reductase , reaction mechanism , mechanism (biology) , methanogenesis , methyl group , enzyme , biochemistry , organic chemistry , group (periodic table) , philosophy , epistemology
Find your path : Methyl‐coenzyme M reductase (MCR, turquoise) reversibly catalyzes the reduction of methyl‐coenzyme M (methyl‐S‐CoM) with coenzyme B (CoB‐SH) to form methane and the heterodisulfide. Recently, spectroscopic methods were used to detect trapped intermediates in a stopped‐flow system, and CoM‐S‐Ni II was identified after half a turnover of the MCR reaction (F 430 =nickel porphinoid). This finding supports a methyl‐radical catalytic mechanism.