EC Number   |
Reaction |
Reference |
|---|
    1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
a ferric hydroperoxide species must be an active intermediate in the first oxygenation step |
438268 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
a three-step mechanism, mechanism of the the third step, heme oxygenase enzymatic ring-opening mechanism of verdoheme, a process which maintains iron homeostasis, overview. Reaction mechanism for the FeOOH pathway and the FeHOOH pathway, and complete triplet-state mechanism, overview |
715262 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
binding of heme stabilizes the solvent H-bonded network in the active site required for proper catalysis |
659302 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
determination of single turnover rate constants and reaction intermediates for heme oxygenase-1 |
438272 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
docking model of heme and ferredoxin, indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron |
658647 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
electrophilic oxidation mechanism, stereochemical control of the reaction regiospecificity |
659395 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of alpha-verdoheme to alpha-biliverdin, overview |
726967 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of verdoheme. Only alpha-verdoheme with the O atom in its alpha position, and not beta-, gamma-, or delta-verdoheme, is converted to biliverdin. The third step, like the first, shows regiospecificity, the distal Asp plays an important role in this step, similar to the first. The substrate heme is sandwiched between two helices, termed the proximal and distal helices. Reaction mechanism, overview |
728081 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
hydroperoxoferri-heme oxygenase-1 is the reactive species directly forming the alpha-meso-hydroxyheme product by attack of the distal OH of the hydroperoxo moiety at the heme alpha-carbon |
438278 |
| 1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O |
mechanism |
438249 |
