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EC Tree
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 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
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,
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ferredoxin-dependent heme oxygenase
ferredoxin-dependent soluble heme oxygenase
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ferredoxin-dependent heme oxygenase
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ferredoxin-dependent heme oxygenase
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heme oxygenase
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Ho1
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HY1
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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
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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.
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hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
?
mesoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
mesobiliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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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
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + H2O2 + H+
verdoheme + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
?
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hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
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-
?
mesoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
mesobiliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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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
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-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
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?
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heme
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the enzyme forms a 1:1 complex with heme
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Sn-protoporphyrin IX
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25% inhibition at 0.02 mM
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4,5-dihydroxy-1,3-benzene disulfonic acid
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6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid
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significantly increases enzyme activity
D-ascorbate
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99% activity with D-ascorbate as compared to L-ascorbate
HClO4
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134% activity at 5% (v/v) HClO4
Tiron
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almost as effective as desferrioxamine
additional information
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not activated by EDTA, dehydroascorbate, and phenyledediamine
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desferrioxamine
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desferrioxamine
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6fold increase of activity in the presence of 2.5 mM desferrioxamine
L-ascorbate
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adding of a second electron donor, such as ascorbate, led to a 10fold increase in the heme conversion rate
L-ascorbate
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the enzyme requires an iron chelator and second reductant, such as L-ascorbate, for full activity
L-ascorbate
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required for activity
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0.0013
hemin
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at pH 7.2 and 25°C
0.0013 - 0.0057
protoheme
0.0013
protoheme
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isoform HY1, at pH 7.2 and 25°C
0.0027
protoheme
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isoform HO3, at pH 7.2 and 25°C
0.0057
protoheme
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isoform HO4, at pH 7.2 and 25°C
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0.00069
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unpurified enzyme, at pH 7.6 and 42°C
0.1403
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after 203fold purification, at pH 7.6 and 42°C
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7.3
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isoforms HO4 and HY1
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10 - 45
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the relative enzyme activity increases between 10°C and 45°C
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brenda
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brenda
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brenda
no activity in Cytophaga hutchinsonii
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brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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isoforms HY1, HO3 and HO4
brenda
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brenda
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brenda
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metabolism
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initial step in the biosynthesis of functional open-chain tetrapyrroles
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A0A5P9QE76_9MICO
221
0
23994
TrEMBL
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HO1_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
240
0
27051
Swiss-Prot
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26000
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x * 26000, SDS-PAGE
27000
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x * 27000, recombinant enzyme, SDS-PAGE
28500
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x * 28500, calculated from amino acid sequence
29000
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x * 29000, SDS-PAGE
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?
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x * 27000, recombinant enzyme, SDS-PAGE
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x * 53000, GST-tagged enzyme, SDS-PAGE
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x * 26100, calculated from amino acid sequence
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x * 28500, calculated from amino acid sequence
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x * 28540, isoform HO2, calculated from amino acid sequence
?
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x * 31000, isoform HO2, SDS-PAGE
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-30°C, in 50 mM HEPES-NaOH (pH 7.2) with 40% (v/v) glycerol, at least 3 months, no loss of activity
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ammonium sulfate precipitation, Blue 2-Sepharose column chromatography, DEAE column chromatography, ferredoxin-Sepharose column chromatography, and Sephadex G-75 gel filtration
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ammonium sulfate precipitation, DE-52 column chromatography, and Sephadex G-75 gel filtration
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ammonium sulfate precipitation, Sephadex G-75 gel filtration , DE-52 column chromatography, and hydroxyapatite column chromatography
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partial purification by nickel chelating column chromatography
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Q sepharose column chromatography
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Talon-cobalt-affinity column chromatography
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expressed in Escherichia coli and in an Arabidopsis thaliana hy1 mutant
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Nicotiana benthamiana and Escherichia coli BL21 (DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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enzyme expression increases about 7fold during incubation of cells for 72 h in iron-deficient medium
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Sugishima, M.; Migita, C.T.; Zhang, X.; Yoshida, T.; Fukuyama, K.
Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme
Eur. J. Biochem.
271
4517-4525
2004
Synechocystis sp. (P72849)
brenda
Gohya, T.; Zhang, X.; Yoshida, T.; Migita, C.T.
Spectroscopic characterization of a higher plant heme oxygenase isoform-1 from Glycine max (soybean)--coordination structure of the heme complex and catabolism of heme
FEBS J.
273
5384-5399
2006
Glycine max
brenda
Gisk, B.; Yasui, Y.; Kohchi, T.; Frankenberg-Dinkel, N.
Characterization of the heme oxygenase protein family in Arabidopsis thaliana reveals a diversity of functions
Biochem. J.
425
425-434
2010
Arabidopsis thaliana
brenda
Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.
Effects of modified phycobilin biosynthesis in the cyanobacterium Synechococcus sp. strain PCC 7002
J. Bacteriol.
193
1663-1671
2011
Synechococcus sp.
brenda
Rhie, G.; Beale, S.
Phycobilin biosynthesis: Reductant requirements and product identification for heme oxygenase from Cyanidium caldarium
Arch. Biochem. Biophys.
320
182-194
1995
Cyanidium caldarium
brenda
Gohya, T.; Sato, M.; Zhang, X.; Migita, C.
Variation of the oxidation state of verdoheme in the heme oxygenase reaction
Biochem. Biophys. Res. Commun.
376
293-298
2008
Glycine max
brenda
Zhang, X.; Migita, C.; Sato, M.; Sasahara, M.; Yoshida, T.
Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase: Properties of the heme and enzyme complex
FEBS J.
272
1012-1022
2005
Synechocystis sp.
brenda
Beale, S.; Cornejo, J.
Biosynthesis of phycobilins. Ferredoxin-mediated reduction of bilverdin catalyzed by extracts of Cyanidium caldarium
J. Biol. Chem.
266
22328-22332
1991
Cyanidium caldarium
brenda
Dammeyer, T.; Frankenberg-Dinkel, N.
Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms
Photochem. Photobiol. Sci.
7
1121-1130
2008
Synechocystis sp. PCC 6803
brenda
Cornejo, J.; Willows, R.; Beale, S.
Phytobilin biosynthesis: Cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803
Plant J.
15
99-107
1998
Synechocystis sp. PCC 6803
brenda
Willows, R.; Mayer, S.; Foulk, M.; DeLong, A.; Hanson, K.; Chory, J.; Beale, S.
Phytobilin biosynthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy1 mutant
Plant Mol. Biol.
43
113-120
2000
Synechocystis sp.
brenda
Muramoto, T.; Tsurui, N.; Terry, M.; Yokota, A.; Kohchi, T.
Expression and biochemical properties of a ferredoxin-dependent heme oxygenase required for phytochrome chromophore synthesis
Plant Physiol.
130
1958-1966
2002
Arabidopsis thaliana
brenda
Montgomery, B.L.; Lagarias, J.C.
Phytochrome ancestry: sensors of bilins and light
Trends Plant Sci.
7
357-366
2002
Agrobacterium tumefaciens, Anabaena sp., Synechocystis sp., Deinococcus radiodurans, Magnetospirillum magnetotacticum, Nostoc punctiforme, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas syringae, Rhodobacter sphaeroides, Rhodopseudomonas palustris, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. MIT9319, no activity in Cytophaga hutchinsonii, Anabaena sp. PCC 7120, Pseudomonas putida KT 2240, Pseudomonas putida PRS1
brenda
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1.14.15.20 heme oxygenase (biliverdin-producing, ferredoxin)
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