1.14.13.25	formate + NAD(P)H + O2	assay with whole cells	
1.14.13.25	methane + duroquinol + O2	-	
1.14.13.25	methane + NAD(P)H + H+ + O2	-	
1.14.13.25	methane + NAD(P)H + H+ + O2	methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system	
1.14.13.25	methane + NAD(P)H + O2	-	
1.14.13.25	methane + NAD(P)H + O2	initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source	
1.14.13.25	methane + NADH + H+ + O2	-	
1.14.13.25	methane + NADH + O2	-	
1.14.13.25	methane + NADH + O2	methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2	
1.14.13.25	methane + NADH + O2	via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane	
1.14.13.25	methane + reduced acceptor + H* + O2	-	
1.14.13.25	additional information	access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview	
1.14.13.25	additional information	the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview	
1.14.13.25	additional information	the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane	
1.14.13.25	additional information	the sMMO enzyme has broad substrate specificity compared to pMMO