EC Number   |
Cofactor |
Reference |
|---|
   1.14.18.3 | ascorbate |
- |
438940 |
| 1.14.18.3 | duroquinol |
- |
745305 |
| 1.14.18.3 | duroquinol |
NADH passes electron to duroquinol |
745305 |
| 1.14.18.3 | more |
- |
438940 |
| 1.14.18.3 | more |
duroquinol as artificial reductant |
675831 |
| 1.14.18.3 | more |
succinate, particulate enzyme functions in vitro with either succinate or NADH as electron donor, soluble enzyme functions only with NADH |
438927 |
| 1.14.18.3 | more |
the pMMO electron donor is generally thought to be ubiquinol generated by a type 2 NADH:quinone oxidoreductase. The addition of cytochrome could facilitate electron transfer without the requirement for NADH |
744325 |
| 1.14.18.3 | NAD+ |
methane activation by particulate methane monooxygenase is NAD-dependent |
746420 |
| 1.14.18.3 | NAD+ |
methane activation by particulate methane monooxygenase is NAD-dependent. Docking simulations of NAD+ on the enzyme clearly show preferential binding of the cofactor in the vicinity of the Cu metal centers confirming its functional relationship with particulate methane monooxygenase |
746420 |
| 1.14.18.3 | NADH |
- |
438927, 438944, 438952, 672301, 673739, 674005, 675831, 684112, 686085, 687284, 689789, 702170, 703343, 726954, 727340, 727552, 728079 |
