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IUBMB Comments The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
FCSD, flavocytochrome c sulfide dehydrogenase, flavocytochrome c-522, flavocytochrome c-sulfide dehydrogenase, flavocytochrome c: sulfide dehydrogenase, FSDH, SoxF, sulfide-cytochrome c reductase, sulfide-cytochrome c reductase (flavocytochrome c), sulfide:cytochrome c oxidoreductase,
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flavocytochrome c sulfide dehydrogenase
flavocytochrome c-522
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flavocytochrome c-sulfide dehydrogenase
flavocytochrome c: sulfide dehydrogenase
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sulfide-cytochrome c reductase
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sulfide-cytochrome c reductase (flavocytochrome c)
sulfide:cytochrome c oxidoreductase
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sulphide-cytochrome c reductase
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FCSD
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flavocytochrome c sulfide dehydrogenase
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flavocytochrome c sulfide dehydrogenase
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flavocytochrome c sulfide dehydrogenase
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flavocytochrome c-sulfide dehydrogenase
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flavocytochrome c-sulfide dehydrogenase
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FSDH
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sulfide-cytochrome c reductase (flavocytochrome c)
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sulfide-cytochrome c reductase (flavocytochrome c)
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hydrogen sulfide + 2 ferricytochrome c = sulfur + 2 ferrocytochrome c + 2 H+
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hydrogen-sulfide:flavocytochrome c oxidoreductase
The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.
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hydrogen sulfide + ferricytochrome c 555
sulfur + ferrocytochrome c 555 + H+
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-
-
?
hydrogen sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
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-
-
-
?
sulfide + oxidized benzyl viologen
sulfur + reduced benzyl viologen + H+
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
sulfide + oxidized heart cytochrome c
sulfur + reduced heart cytochrome c + H+
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sulfur or polysulfide as product
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?
sulfide + oxidized horse cytochrome c
sulfur + reduced horse cytochrome c + H+
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?
sulfide + oxidized Nitrosomonas europaea cytochrome c552
sulfur + reduced Nitrosomonas europaea cytochrome c552 + H+
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?
sulfide + oxidized Rhodospirillum rubrum cytochrome c2
sulfur + reduced Rhodospirillum rubrum cytochrome c2
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?
sulfur + reduced benzyl viologen + H+
sulfide + oxidized benzyl viologen
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?
additional information
?
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sulfide + oxidized benzyl viologen
sulfur + reduced benzyl viologen + H+
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?
sulfide + oxidized benzyl viologen
sulfur + reduced benzyl viologen + H+
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?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
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?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
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?
sulfide + oxidized cytochrome c
sulfur + reduced cytochrome c + H+
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?
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
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?
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
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r
sulfide + oxidized flavocytochrome c
sulfur + reduced flavocytochrome c + H+
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?
additional information
?
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cytochrome c554 from Pseudomonas aeruginosa and cytochrome c555 from Chlorobium limicola f. thiosulfatophilum are not reduced by the enzyme
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?
additional information
?
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trifluoroacetylated cytochrome c is not reduced in the presence of cytochrome c-552 and sulfide
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?
additional information
?
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SoxF does not catalyze thiosulfate- or sulfite-dependent cytochrome c reduction
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?
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flavin
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the enzyme contains one molecule flavin
FAD
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FAD
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covalently bound, the enzyme contains one molecule of FAD per molecule
FAD
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covalently bound, the enzyme contains one molecule of FAD per molecule
FAD
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FAD is covalently bound to Cys42
FAD
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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
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heme
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covalently bound heme c, the enzyme contains one molecule of heme c per molecule
heme
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covalently bound heme c, the enzyme contains two molecules of heme c per molecule
heme
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the enzyme contains a diheme cytochrome subunit
heme
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the smaller subunit contains one molecule covalently bound heme c
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Atebrin
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60% inhibition at 0.1 mM
NaN3
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7% inhibition at 10 mM
reduced heart cytochrome c
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competitive product inhibition
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sulfite
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preincubation of SoxF with 1 mM sodium sulfite for 20 min inactivates SoxF (9.0% residual sulfide dehydrogenase activity)
cyanide
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strong inhibition at 0.67 mM
cyanide
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80% inhibition at 0.001 mM
cyanide
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1 mM cyanide inhibits SoxF activity at pH 6.0 by 25% and at pH 8.0 by 92%
additional information
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CO do not affect the catalytic activity of the cytochrome-552
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additional information
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not inhibited by EDTA, o-phenanthroline, and CO
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additional information
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neither FAD nor FMN activate sulfide-cytochrome c reduction catalysed by cytochrome c-553
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0.0038
oxidized cytochrome c
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pH and temperature not specified in the publication
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0.116
oxidized heart cytochrome c
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at pH 6.0 and 30°C
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0.0017
Sulfide
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pH and temperature not specified in the publication
0.0023
Sulfide
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at pH 6.0 and 30°C
0.0125
Sulfide
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in 10 mM Tris-HCl buffer, pH 8.5, at 20°C
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3.9
oxidized heart cytochrome c
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at pH 6.0 and 30°C
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0.0072
reduced heart cytochrome c
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at pH 6.0 and 30°C
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0.0013
sulfur
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at pH 6.0 and 30°C
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0.0001
cyanide
Chlorobium vibrioforme f. thiosulfatophilum
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in 0.1 M Tris-HCl buffer, pH 7.4, at 20°C
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5.1
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isoelectric focusing
6.7
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isoelectric focusing
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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10000
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1 * 46000 + 1 * 10000, SDS-PAGE
101000
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gel filtration column is reequilibrated with low ionic strength buffer
21300
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1 * 46600 + 1 * 21300, SDS-PAGE
40000
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1 * 40000 + 1 * 11000, SDS-PAGE
42010
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calculated from amino acid sequence
42797
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1 * 42797, electrospray mass spectrometry
42832
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1 * 42832, electrospray mass spectrometry of SoxF as isolated yields masses of 42797 Da and 42832 Da
43568
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1 * 43568 + 1 * ?, native flavoprotein subunit, calculated from amino acid sequence (without disulfide bridges but with FAD)
43652
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1 * 43652 + 1 * ?, native flavoprotein subunit, MALDI-TOF mass spectrometry
46600
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1 * 46600 + 1 * 21300, SDS-PAGE
47000
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1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
61800
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calculated from amino acid sequence
64000
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gel filtration column reequilibrated with either intermediate or high ionic strength buffer
11000
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1 * 40000 + 1 * 11000, SDS-PAGE
11000
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1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
21000
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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
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1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
21000
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1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
46000
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1 * 46000 + 1 * 10000, SDS-PAGE
46000
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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
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1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
46000
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1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
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heterodimer
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1 * 43568 + 1 * ?, native flavoprotein subunit, calculated from amino acid sequence (without disulfide bridges but with FAD)
heterodimer
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1 * 43652 + 1 * ?, native flavoprotein subunit, MALDI-TOF mass spectrometry
heterodimer
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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
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1 * 46000 + 1 * 21000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
heterodimer
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1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
heterodimer
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1 * 46600 + 1 * 21300, SDS-PAGE
heterodimer
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1 * 47000 + 1 * 11000, flavoprotein subunit and cytochrome subunit, SDS-PAGE
heterodimer
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1 * 46000 + 1 * 10000, SDS-PAGE
heterodimer
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1 * 40000 + 1 * 11000, SDS-PAGE
heterodimer
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1 * 40000 + 1 * 11000, SDS-PAGE
monomer
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1 * 42797, electrospray mass spectrometry
monomer
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1 * 42832, electrospray mass spectrometry of SoxF as isolated yields masses of 42797 Da and 42832 Da
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80
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when the cytochrome is heated at 80°C for 2 min, its catalytic activity greatly decreases
80
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the enzyme is completely inactive after 2 min at 80°C
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ammonium sulfate precipitation and DEAE-cellulose column chromatography
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ammonium sulfate precipitation and Q-Sepharose column chromatography
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
DEAE-Sepharose column chromatography and Sephadex G-50 gel filtration
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muRPC C2/C18 PC 3.2/3 or muRPC C8 PC 2.1/10 column chromatography and Superdex 30 PC gel filtration
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Amberlite CG-50 column chromatography
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in the absence of sulfide or thiosulfate, FCSD expression is significantly reduced
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the production of FCSD mRNA is upregulated by sulfide
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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
Chlorobium vibrioforme 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
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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
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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
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1.8.2.3 sulfide-cytochrome-c reductase (flavocytochrome c)
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