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Information on EC 1.8.2.3 - sulfide-cytochrome-c reductase (flavocytochrome c)
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EC Tree
1.8.2.3 sulfide-cytochrome-c reductase (flavocytochrome c)IUBMB Comments
The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.
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Word Map
- 1.8.2.3
- sulfur
- vinosum
- sulfite
- flavin
- thiosulfate
- heme
- chromatium
-
phototrophic
- flavoprotein
-
purple
-
sulfide:quinone
- persulfide
- chlorobium
-
sulfur-oxidizing
- polysulfide
- limicola
-
allochromatium
- paradoxus
-
chemolithoautotrophic
-
haloalkaliphilic
-
cupriavidus
-
ectothiorhodospira
-
flavin-binding
-
biogeochemical
- thioalkalivibrio
- thiosulfatophilum
- thiocyanate
- hemoprotein
- vacuolata
- tepidum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
flavocytochrome c sulfide dehydrogenase, sulfide:cytochrome c oxidoreductase, flavocytochrome c-sulfide dehydrogenase, sulfide-cytochrome c reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FCC
FCSD
flavocytochrome c sulfide dehydrogenase
flavocytochrome c-sulfide dehydrogenase
FSDH
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 SOURCE
PATHWAYS
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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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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
-
-
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
WP_010812125.1; WP_011616200.1
-
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
WP_010812125.1; WP_011616200.1
without sulfide:quinone oxidoreductase (SQR) Cupriavidus necator H16 uses flavocytochrome c sulfide dehydrogenase (FCSD) to oxidize self-produced sulfide
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
the enzyme does not catalyze oxidation of thiosulfate, sulfite, tetrathionate, and sulfur
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
the enzyme does not catalyze oxidation of thiosulfate, sulfite, tetrathionate, and sulfur
-
-
?
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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NATURAL SUBSTRATE
NATURAL 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 + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
WP_010812125.1; WP_011616200.1
without sulfide:quinone oxidoreductase (SQR) Cupriavidus necator H16 uses flavocytochrome c sulfide dehydrogenase (FCSD) to oxidize self-produced sulfide
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
-
-
?
hydrogen sulfide + 2 ferricytochrome c
sulfur + 2 ferrocytochrome c + 2 H+
W0DP88; W0DKT4
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
-
-
?
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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 one molecule of heme c per molecule
heme
-
covalently bound heme c, the enzyme contains two molecules of heme c per molecule
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INHIBITOR
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
Prosthecochloris vibrioformis 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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
WP_010812125.1: FccA, WP_011616200.1: FccB
WP_010812125.1; WP_011616200.1
GenBank
brenda
W0DP88: flavin-binding subunit, W0DKT4: heme-binding subunit
W0DP88; W0DKT4
UniProt
brenda
W0DP88: flavin-binding subunit, W0DKT4: heme-binding subunit
W0DP88; W0DKT4
UniProt
brenda
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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
W0DP88; W0DKT4
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
metabolism
WP_010812125.1; WP_011616200.1
without sulfide:quinone oxidoreductase (SQR) Cupriavidus necator H16 uses flavocytochrome c sulfide dehydrogenase (FCSD) to oxidize self-produced sulfide and FCSD couples with persulfide dioxygenase (PDO) to oxidize sulfide to sulfite and thiosulfate, via a pathway similar to the SQR-PDO pathway
metabolism
-
one of the central enzymes of the respiratory chain in sulfur-oxidizing bacteria
-
physiological function
flavocytochrome c sulfide dehydrogenase enhances thiosulfate oxidation by the sulfur-oxidizing (Sox) system but couples with the Sox system for sulfide oxidation to sulfate in the absence of sulfide:quinone oxidoreductase
physiological function
WP_010812125.1; WP_011616200.1
the enzyme plays a detoxification role in Cupriavidus necator H16. With the fccA and fccB genes encoding flavocytochrome c sulfide dehydrogenases Cupriavidus necator H16 oxidizes self-produced H2S
physiological function
Cupriavidus pinatubonensis JMP 134
-
flavocytochrome c sulfide dehydrogenase enhances thiosulfate oxidation by the sulfur-oxidizing (Sox) system but couples with the Sox system for sulfide oxidation to sulfate in the absence of sulfide:quinone oxidoreductase
-
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
101000
-
gel filtration column is reequilibrated with low ionic strength buffer
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
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
monomer
heterodimer
-
1 * 43568 + 1 * ?, native flavoprotein subunit, calculated from amino acid sequence (without disulfide bridges but with FAD)
heterodimer
-
1 * 43652 + 1 * ?, native flavoprotein subunit, MALDI-TOF mass spectrometry
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 * 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
heterodimer
W0DP88; W0DKT4
1 * 42000 (FAD-binding subunit) + 1 * 7300 (heme-binding subunit), SDS-PAGE
heterodimer
-
1 * 42000 (FAD-binding subunit) + 1 * 7300 (heme-binding subunit), SDS-PAGE
-
monomer
-
1 * 42832, electrospray mass spectrometry of SoxF as isolated yields masses of 42797 Da and 42832 Da
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Visser, J.; De Jong, G.; Robertson, L.; Kuenen, J.
A novel membrane-bound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobacillus sp. W5
Arch. Microbiol.
167
295-301
1997
Thiobacillus sp., Thiobacillus sp. W5
brenda
Quentmeier, A.; Hellwig, P.; Bardischewsky, F.; Wichmann, R.; Friedrich, C.
Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus
Biochemistry
43
14696-14703
2004
Paracoccus pantotrophus
brenda
Kusai, K.; Yamanaka, T.
The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553
Biochim. Biophys. Acta
325
304-314
1973
Prosthecochloris vibrioformis f. thiosulfatophilum
brenda
Gray, G.; Knaff, D.
The role of a cytochrome c-552-cytochrome c complex in the oxidation of sulfide in Chromatium vinosum
Biochim. Biophys. Acta
680
290-296
1982
Allochromatium vinosum
-
brenda
Kostanjevecki, V.; Brige, A.; Meyer, T.; Cusanovich, M.; Guisez, Y.; Van Beeumen, J.
A membrane-bound flavocytochrome c-sulfide dehydrogenase from the purple phototrophic sulfur bacterium Ectothiorhodospira vacuolata
J. Bacteriol.
182
3097-3103
2000
Ectothiorhodospira shaposhnikovii
brenda
Fukumori, Y.; Yamanaka, T.
Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure
J. Biochem.
85
1405-1414
1979
Allochromatium vinosum
brenda
Yamanaka, T.
Sulfide-cytochrome c reductase (flavocytochrome c)
Methods Enzymol.
243
463-472
1994
Allochromatium vinosum, Chlorobaculum thiosulfatiphilum
-
brenda
Van Driessche, G.; Koh, M.; Chen, Z.; Mathews, F.; Meyer, T.; Bartsch, R.; Cusanovich, M.; Van Beeumen, J.
Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum
Protein Sci.
5
1753-1764
1996
Allochromatium vinosum
brenda
Chen, Z.; Koh, M.; Van Driessche, G.; Van Beeumen, J.; Bartsch, R.; Meyer, T.; Cusanovich, M.; Mathews, F.
The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium
Science
266
430-432
1994
Allochromatium vinosum
brenda
Lue, C.; Xia, Y.; Liu, D.; Zhao, R.; Gao, R.; Liu, H.; Xun, L.
Cupriavidus necator H16 uses flavocytochrome c sulfide dehydrogenase to oxidize self-produced and added sulfide
Appl. Environ. Microbiol.
83
e01610-17
2017
Cupriavidus necator (WP_010812125.1 AND WP_011616200.1), Cupriavidus necator
brenda
Xin, Y.; Gao, R.; Cui, F.; Lue, C.; Liu, H.; Liu, H.; Xia, Y.; Xun, L.
The heterotrophic bacterium Cupriavidus pinatubonensis JMP134 oxidizes sulfide to sulfate with thiosulfate as a key intermediate
Appl. Environ. Microbiol.
86
e01835-20
2020
Cupriavidus pinatubonensis (Q46W64), Cupriavidus pinatubonensis, Cupriavidus pinatubonensis JMP 134 (Q46W64)
brenda
Tikhonova, T.V.; Lilina, A.V.; Osipov, E.M.; Shipkov, N.S.; Dergousova, N.I.; Kulikova, O.G.; Popov, V.O.
Catalytic properties of flavocytochrome c sulfide dehydrogenase from haloalkaliphilic bacterium Thioalkalivibrio paradoxus
Biochemistry (Moscow)
86
361-369
2021
Thioalkalivibrio paradoxus (W0DP88 AND W0DKT4), Thioalkalivibrio paradoxus, Thioalkalivibrio paradoxus ARh1 (W0DP88 AND W0DKT4)
brenda
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