Abstract
Methane monooxygenase (MMO, E.C. 1.14.13.25) was purified from membranes of the methane-oxidizing bacterium Methylococcus capsulatus (strain M) and separated into two components: monooxygenase and NADH-oxidoreductase. The individual components did not oxidize methane. Oxidation of the substrate was observed in the presence of two components. MMO specific activity was 3600 nmol CH4/min/mg of the protein. The degree of purification was 170. The criterion of purity was sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which showed that the monooxygenase and NADH-reductase consist of subunits with a molecular weight of 35 ± 3 kDa and 45 ± 3 kDa, respectively. From gel chromatography on Sephadex G-200, a molecular weight of 180 kDa was found for the native NADH-reductase, suggesting a tetrameric structure for this enzyme. The quaternary structure of the NADH-reductase and monooxygenase were investigated by electron microscopy. NADH-reductase is constructed from four identical subunits with molecular w...
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