EC Number   |
Cofactor |
Reference |
|---|
    1.14.14.18 | ascorbate |
- |
726864, 726996 |
| 1.14.14.18 | heme |
- |
658647, 673571, 674200, 675302, 701661, 702147, 702346, 702640, 703420, 704821, 704854, 704976 |
| 1.14.14.18 | heme |
1:1 complex with enzyme |
657694 |
| 1.14.14.18 | heme |
heme iron is coordinated by a water molecule in ferric form |
658117 |
| 1.14.14.18 | heme |
hemoprotein, heme is both substrate and cofactor, heme oxygenase-2 binds heme at heme regulatory motifs with a conserved Cys-Pro pair |
438270 |
| 1.14.14.18 | heme |
high-spin heme oxygenase-2,4-dimethyldeuterohemin-H2O complex dominates at low pH, low-spin heme oxygenase-2,4-dimethyldeuterohemin-OH complex dominates at alkaline pH |
702262 |
| 1.14.14.18 | heme |
sprectrum shows a Soret band at 407 nm |
742894 |
| 1.14.14.18 | heme |
the heme is located at the intermonomer interface and is bound by both monomers. The heme iron is coordinated by the side chain of His245 and an azide molecule when it is present in crystallization conditions |
715594 |
| 1.14.14.18 | more |
CO as a ferrous heme ligand or ferricyanide as an oxidant have no effect |
702346 |
| 1.14.14.18 | NADH |
NADPH is more effective than NADH |
438243 |
