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EC 1.14.15.20 Details
show Brenda entryEC number
1.14.15.20
Accepted name
heme oxygenase (biliverdin-producing, ferredoxin)
Reaction
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
Other name(s)
HO1 (gene name),
HY1 (gene name),
HO3 (gene name),
HO4 (gene name),
pbsA1 (gene name)
Systematic name
protoheme,reduced ferredoxin:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating)
Comment
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 α-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.
History
created 2016
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.6.7.1 created 1972, deleted 1978 1.6.7.2 created 1972, deleted 1978 1.6.7.3 created 1978, deleted 1978 1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000 1.14.99.6 created 1972, modified 2000, deleted 2000 1.14.99.8 created 1972, deleted 1984 1.14.99.13 created 1972, deleted 1984 1.14.99.16 created 1972, deleted 2002 1.14.99.17 created 1972, deleted 1976 1.14.99.18 created 1976, modified 1999, deleted 2003 1.14.99.25 created 1986, deleted 2000
