title: Substrate specificity of soluble methane monooxygenase. Mechanistic implications.
abstract: 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.
authors: Department of Biological Sciences, University of Warwick, Coventry, West Midlands, United Kingdom.
authors: J
authors: J
authors: Green
authors: H
authors: H
authors: Dalton
mesh_terms: D000473:Alkanes / Q000378:metabolism; D019605:Euryarchaeota / Q000201:enzymology*; D008401:Gas Chromatography-Mass Spectrometry; D007700:Kinetics; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000473:Alkanes; D010105:Oxygenases; C021555:methane monooxygenase