Substrate specificity of soluble methane monooxygenase. Mechanistic implications.
摘要：
Following the example set by studies of the mechanistic aspects of the substrate specificity of various cytochrome P-450 enzymes, we have undertaken a parallel investigation of the soluble methane monooxygenase from Methylococcus capsulatus (Bath). Soluble methane monooxygenase is a multicomponent enzyme with a broad substrate specificity. Using substrates previously tested with cytochrome P-450 enzymes and using purified enzyme preparations, this work indicates that soluble methane monooxygenase has a similar oxidative reaction mechanism to cytochrome P-450 enzymes. The evidence suggests that soluble methane monooxygenase oxidizes substrates via a nonconcerted reaction mechanism (hydrogen abstraction preceding hydroxylation) with radical or carbocation intermediates. Aromatic hydroxylation proceeds by epoxidation followed by an NIH shift.
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关键词：
LGIC SUPERFAMILY PROTO-BINDING SITE CYS-LOOP MOTIF DOCKING MODEL ANIONIC SITE SPECIFICITY RESIDUE
DOI：
10.1016/S0005-2728(89)80013-1
被引量：
年份：
1989
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