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