heme oxygenase (biliverdin-producing, ferredoxin) EC#: 1.14.15.20; ChemWhat Code: 1375710

Product Name heme oxygenase (biliverdin-producing, ferredoxin)
Example Structure Example Structure of heme oxygenase (biliverdin-producing, ferredoxin) EC#: 1.14.15.20
Synonyms ferredoxin-dependent heme oxygenase, ferredoxin-dependent soluble heme oxygenase, haem oxygenase, heme oxygenase, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HY1
EC Number 1.14.15.20
CAS Registry Number
Comments 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 ¦Á-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.
Cofactor
History
Reactions Protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O(2) + 6 H(+) = biliverdin + Fe(2+) + Co + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H(2)O.

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