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

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15.20 heme oxygenase (biliverdin-producing, ferredoxin)

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Results	in table
15	Activating Compound
2	AA Sequence
6	Cloned(Commentary)
1	Cofactor
1	Expression
1	General Information
1	Inhibitors
4	KM Value [mM]
5	Localization
7	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
87	Organism
10	Pathway
3	pH Optimum
6	Purification (Commentary)
1	Reaction
30	Reference
2	Specific Activity [micromol/min/mg]
1	Storage Stability
13	Substrates and Products (Substrate)
9	Subunits
25	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]

Systematic Name

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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.