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Enzyme Nomenclature
Information on EC 1.8.2.3 - sulfide-cytochrome-c reductase (flavocytochrome c)
for references in articles please use BRENDA:EC1.8.2.3
Word Map on EC 1.8.2.3
- 1.8.2.3
- sulfur
- vinosum
- flavoprotein
- chromatium
-
phototrophic
- flavin
-
purple
- thiosulfate
- chlorobium
- limicola
-
allochromatium
-
periplasmic
- persulfide
-
chemolithoautotrophic
- thiosulfatophilum
-
diheme
-
c-type
-
autotroph
-
sulfur-oxidizing
-
ectothiorhodospira
- tepidum
- vacuolata
-
hemoprotein
-
sulfide:quinone
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.8.2.3
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RECOMMENDED NAME
GeneOntology No.
sulfide-cytochrome-c reductase (flavocytochrome c)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + 2 ferricytochrome c = sulfur + 2 ferrocytochrome c + 2 H+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:flavocytochrome c oxidoreductase
The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + ferricytochrome c 555
sulfur + ferrocytochrome c 555 + H+
-
-
-
-
?
hydrogen sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
-
-
-
-
?
sulfide + oxidized heart cytochrome c
sulfur + reduced heart cytochrome c + H+
-
-
sulfur or polysulfide as product
-
?
sulfide + oxidized horse cytochrome c
sulfur + reduced horse cytochrome c + H+
-
-
-
-
?
sulfide + oxidized Nitrosomonas europaea cytochrome c552
sulfur + reduced Nitrosomonas europaea cytochrome c552 + H+
-
-
-
-
?
sulfide + oxidized Rhodospirillum rubrum cytochrome c2
sulfur + reduced Rhodospirillum rubrum cytochrome c2
-
-
-
-
?
sulfur + reduced benzyl viologen + H+
sulfide + oxidized benzyl viologen
-
-
-
-
?
sulfide + oxidized benzyl viologen
sulfur + reduced benzyl viologen + H+
-
-
-
-
?
sulfide + oxidized benzyl viologen
sulfur + reduced benzyl viologen + H+
-
-
-
-
?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
-
-
-
-
?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
-
-
-
-
?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
-
-
-
-
?
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
-
-
-
-
?
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
-
-
-
-
r
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
-
-
-
-
?
additional information
?
-
-
cytochrome c554 from Pseudomonas aeruginosa and cytochrome c555 from Chlorobium limicola f. thiosulfatophilum are not reduced by the enzyme
-
-
-
additional information
?
-
-
trifluoroacetylated cytochrome c is not reduced in the presence of cytochrome c-552 and sulfide
-
-
-
additional information
?
-
-
SoxF does not catalyze thiosulfate- or sulfite-dependent cytochrome c reduction
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
covalently bound, the enzyme contains one molecule of FAD per molecule
FAD
-
covalently bound, the enzyme contains one molecule of FAD per molecule
FAD
-
the enzyme contains a glutathione reductase-like flavin-binding subunit. FAD is bound covalently to the flavoprotein subunit by an 8-alpha-methyl(S-cysteinyl) thioether linkage
heme
-
covalently bound heme c, the enzyme contains two molecules of heme c per molecule
heme
-
covalently bound heme c, the enzyme contains one molecule of heme c per molecule
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sulfite
-
preincubation of SoxF with 1 mM sodium sulfite for 20 min inactivates SoxF (9.0% residual sulfide dehydrogenase activity)
cyanide
-
1 mM cyanide inhibits SoxF activity at pH 6.0 by 25% and at pH 8.0 by 92%
additional information
-
CO do not affect the catalytic activity of the cytochrome-552
-
additional information
-
not inhibited by EDTA, o-phenanthroline, and CO
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
neither FAD nor FMN activate sulfide-cytochrome c reduction catalysed by cytochrome c-553
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0038
oxidized cytochrome c
-
pH and temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
cyanide
Chlorobium vibrioforme f. thiosulfatophilum;
-
in 0.1 M Tris-HCl buffer, pH 7.4, at 20°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
21000
42832
-
1 * 42832, electrospray mass spectrometry of SoxF as isolated yields masses of 42797 Da and 42832 Da
43568
-
1 * 43568 + 1 * ?, native flavoprotein subunit, calculated from amino acid sequence (without disulfide bridges but with FAD)
43652
-
1 * 43652 + 1 * ?, native flavoprotein subunit, MALDI-TOF mass spectrometry
46000
47000
-
1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
64000
-
gel filtration column reequilibrated with either intermediate or high ionic strength buffer
101000
-
gel filtration column is reequilibrated with low ionic strength buffer
11000
-
1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
21000
-
1 * 46000 + 1 * 21000, cytochrome c-552 is split by 6 M urea into cytochrome and flavoprotein moieties with molecular weights of 21000 and 46000 Da, respectively
21000
-
1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
21000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
46000
-
1 * 46000 + 1 * 21000, cytochrome c-552 is split by 6 M urea into cytochrome and flavoprotein moieties with molecular weights of 21000 and 46000 Da, respectively
46000
-
1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
46000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
monomer
-
1 * 42797, electrospray mass spectrometry; 1 * 42832, electrospray mass spectrometry of SoxF as isolated yields masses of 42797 Da and 42832 Da
heterodimer
-
1 * 46000 + 1 * 21000, cytochrome c-552 is split by 6 M urea into cytochrome and flavoprotein moieties with molecular weights of 21000 and 46000 Da, respectively
heterodimer
-
1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
heterodimer
-
1 * 43568 + 1 * ?, native flavoprotein subunit, calculated from amino acid sequence (without disulfide bridges but with FAD); 1 * 43652 + 1 * ?, native flavoprotein subunit, MALDI-TOF mass spectrometry
heterodimer
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
heterodimer
-
1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
80
-
when the cytochrome is heated at 80°C for 2 min, its catalytic activity greatly decreases
80
-
the enzyme is completely inactive after 2 min at 80°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
ammonium sulfate precipitation and Q-Sepharose column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
DEAE-Sepharose column chromatography and Sephadex G-50 gel filtration
-
muRPC C2/C18 PC 3.2/3 or muRPC C8 PC 2.1/10 column chromatography and Superdex 30 PC gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the absence of sulfide or thiosulfate, FCSD expression is significantly reduced
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.2.3)
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