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

Ho1

6 entries

Ho2

Biosynthesis of secondary metabolites, Porphyrin and chlorophyll metabolism

-

isoform

Ho3

-

HO4

-

HY1

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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KEGG

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Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of secondary metabolites

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.

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

-

-

?

protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+

biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O

P72849

-

658647

-

?

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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737588

-

?

protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+

biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O

6 entries

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

P72849

-

658647

-

?

protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+

biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O

-

737588

-

?

protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+

biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O

6 entries

heme

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the enzyme forms a 1:1 complex with heme

Sn-protoporphyrin IX

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25% inhibition at 0.02 mM

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

dehydroascorbate

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desferrioxamine

HClO4

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134% activity at 5% (v/v) HClO4

isoascorbate

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L-ascorbate

o-phenanthroline

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Tiron

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almost as effective as desferrioxamine

Trolox

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additional information

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not activated by EDTA, dehydroascorbate, and phenyledediamine

-

0.0013

hemin

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at pH 7.2 and 25°C

0.0013 - 0.0057

protoheme

3 entries

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

7

Agrobacterium tumefaciens

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isoform HO3

7.2

-

7.3

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isoforms HO4 and HY1

50

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10 - 45

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the relative enzyme activity increases between 10°C and 45°C

702147

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Anabaena sp.

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Anabaena sp. PCC 7120

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-

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702147, 739342

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Cereibacter sphaeroides

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-

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737548, 738561

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Deinococcus radiodurans

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Magnetospirillum magnetotacticum

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673571, 737588

-

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no activity in Cytophaga hutchinsonii

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Nostoc punctiforme

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Prochlorococcus marinus subsp. pastoris str. CCMP1986

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-

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Prochlorococcus sp. MIT9319

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Pseudomonas aeruginosa

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Pseudomonas fluorescens

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Pseudomonas putida

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Pseudomonas putida KT 2240

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-

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Pseudomonas putida PRS1

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Pseudomonas syringae

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Rhodopseudomonas palustris

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-

-

-

-

-

-

-

-

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isoforms HY1, HO3 and HO4

metabolism

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initial step in the biosynthesis of functional open-chain tetrapyrroles

739250

26000

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x * 26000, SDS-PAGE

26100

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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

31000

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53000

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gel filtration

?

monomer

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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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673571

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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702147

expressed in Escherichia coli and in an Arabidopsis thaliana hy1 mutant

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739326

expressed in Escherichia coli BL21 cells

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expressed in Escherichia coli BL21(DE3) cells

3 entries

expressed in Nicotiana benthamiana and Escherichia coli BL21 (DE3) cells

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702147

enzyme expression increases about 7fold during incubation of cells for 72 h in iron-deficient medium

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