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Information on EC 1.14.15.20 - heme oxygenase (biliverdin-producing, ferredoxin)

for references in articles please use BRENDA:EC1.14.15.20

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IUBMB 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 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.

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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protoheme
+
6
reduced ferredoxin [iron-sulfur] cluster
+
3
O2
+
6
H+
=
biliverdin
+
Fe2+
+
CO
+
6
oxidized ferredoxin [iron-sulfur] cluster
+
3
H2O
+
6
reduced ferredoxin [iron-sulfur] cluster
+
3
+
6
=
+
+
+
6
oxidized ferredoxin [iron-sulfur] cluster
+
3

Synonyms
ferredoxin-dependent heme oxygenase, ferredoxin-dependent soluble heme oxygenase, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
-
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
heme degradation II, phycocyanobilin biosynthesis, phycoerythrobilin biosynthesis I, phycoerythrobilin biosynthesis II, phycourobilin biosynthesis, phycoviolobilin biosynthesis, phytochromobilin biosynthesis
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