EC Number   |
Cofactor  |
Reference |
|---|
   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 |
