1.14.13.25 cytochrome c one of three protein components is a soluble CO-binding cytochrome c 438921 1.14.13.25 FAD - 674158, 685272, 746420, 764175, 764188, 764309, 764329, 764976, 764980, 765765 1.14.13.25 FAD binds to the enzyme reductase protein MMOR 675455 1.14.13.25 FAD bound to the MMOR enzyme component 672130 1.14.13.25 FAD characterization of FAD redox centre of component C 438928 1.14.13.25 FAD in the 2Fe-2S cluster-containing reductase (MMOR) 764181 1.14.13.25 FAD protein C, reductase component: contains 1 mol FAD per mol protein 438923, 438924, 438925, 438932, 438938, 438939, 438941, 438943 1.14.13.25 FAD soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation 746420 1.14.13.25 FAD the FAD-containing domain MMOR-FAD consits of MMOR residues 97-343 764425 1.14.13.25 FAD the specific activity of MmoC is increased significantly by 20% in presence of 25 microM FAD, whereas addition of FMN does not improve activity confirming FAD as the prosthetic group 764485 1.14.13.25 Ferredoxin - 764329 1.14.13.25 Ferredoxin several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview 674158 1.14.13.25 additional information - 438932 1.14.13.25 additional information cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode 658632 1.14.13.25 additional information component B has no prosthetic group 438932, 438950 1.14.13.25 additional information component D contains no metal ions or organic cofactors 438943 1.14.13.25 additional information presence of a FAD and a [2Fe2S] cluster as its prosthetic group at the reductase MmoC component of the soluble methane monooxygenase complex. The MmMmoC prefers NADH instead of NADPH. No NADPH oxidation activity can be determined at 1 mM 764485 1.14.13.25 additional information the overall picture of the sMMO reductase reveals an electron pathway as NADH -> FAD -> [2Fe-2S] -> methane monohydroxylase (MMOH) 746420 1.14.13.25 NAD(P)H - 672690, 764175, 764181, 764188, 764309 1.14.13.25 NADH - 438920, 438921, 438922, 438924, 438925, 438926, 438928, 438929, 438930, 438931, 438932, 438933, 438934, 438935, 438936, 438937, 438938, 438939, 438941, 438943, 438945, 438946, 438948, 438949, 657998, 658051, 671721, 671722, 672049, 672102, 672130, 673999, 674145, 674158, 674170, 675083, 676844, 684566, 685262, 685272, 701759, 701836, 703761, 704758, 711260, 728376, 744100, 745389, 745730, 746420, 764976, 764980, 765765 1.14.13.25 NADH binds to the enzyme hydroxylase protein MMOH 675455 1.14.13.25 NADH in vivo only NADH can be the electron donor 438947 1.14.13.25 NADH NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands 764425 1.14.13.25 NADH NADH is largely preferred over NAPDH 764329 1.14.13.25 NADH preferred 438923 1.14.13.25 NADH soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation 746420 1.14.13.25 NADH specific for 764485 1.14.13.25 NADH two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles 703211 1.14.13.25 NADPH - 438920, 438921, 438923, 438933, 438936, 438948, 684566, 685262, 685272, 701759, 701836, 703211, 703761, 704758, 764980 1.14.13.25 NADPH NADH is largely preferred over NAPDH 764329 1.14.13.25 NADPH only in vitro 438947 1.14.13.25 [2Fe-2S]-center - 746420, 764329 1.14.13.25 [2Fe-2S]-center in the 2Fe-2S cluster-containing reductase (MMOR) 764181