An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica.
Extracts of Methylomonas methanica catalyse the O2-and NAD(P)H-dependent disappearance of bromomethane. The activity is unstable at 2 degrees C but is stable at --70 degrees C for several weeks. Bromomethane mono-oxygenase is particulate and is inhibited by metal-binding reagents, by compounds SKF 525A and Lilly 53325, by some metal ions and by acetylene. Evidence is presented that indicates that bromomethane mono-oxygenase is the enzyme responsible for methane oxidation in vivo.
D006863:Hydrogen-Ion Concentration; D008697:Methane; D008772:Methylococcaceae / Q000201:enzymology*; D010105:Oxygenases / Q000032:analysis* / Q000037:antagonists & inhibitors; D011335:Proadifen; D013696:Temperature
D011335:Proadifen; D010105:Oxygenases; C019799:bromomethane mono-oxygenase; D008697:Methane