Abstract
Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea and most probably also the methane-oxidizing step in methanotrophic archaea. The enzyme contains coenzyme F(430) as prosthetic group. F(430) is a nickel porphinoid that has to be in the reduced Ni(I) state for the enzyme to be active. The presently discussed catalytic mechanisms of MCR can in principle be divided into two basic models. In one model the key intermediate features a methyl-Ni(III) species being either formed in a nucleophilic substitution reaction or in an oxidative addition reaction. In the other model first the thioether sulfur of methyl-coenzyme M binds to the Ni(I), which subsequently results in the release of the methyl group as methyl radical leaving behind a Ni(II)-sulfur bond. The experimental evidence for and against a methyl-nickel intermediate is reviewed.
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