1.14.15.20: heme oxygenase (biliverdin-producing, ferredoxin)
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For detailed information about heme oxygenase (biliverdin-producing, ferredoxin), go to the full flat file.
Reaction
+ 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = + + + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
Synonyms
ferredoxin-dependent heme oxygenase, ferredoxin-dependent soluble heme oxygenase, haem oxygenase, heme oxygenase, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HY1
ECTree
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Systematic Name
Systematic Name on EC 1.14.15.20 - heme oxygenase (biliverdin-producing, ferredoxin)
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protoheme,reduced ferredoxin:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4, NADPH---hemoprotein reductase.