BRENDA - Enzyme Database
show all sequences of 1.8.2.3

The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium

Chen, Z.; Koh, M.; Van Driessche, G.; Van Beeumen, J.; Bartsch, R.; Meyer, T.; Cusanovich, M.; Mathews, F.; Science 266, 430-432 (1994)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
-
Allochromatium vinosum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
21000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
46000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
67000
-
-
Allochromatium vinosum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Allochromatium vinosum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + oxidized flavocytochrome c
-
716916
Allochromatium vinosum
sulfur + reduced flavocytochrome c + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
heterodimer
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
Cofactor
Cofactor
Commentary
Organism
Structure
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
Allochromatium vinosum
heme
the enzyme contains a diheme cytochrome subunit
Allochromatium vinosum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Allochromatium vinosum
heme
the enzyme contains a diheme cytochrome subunit
Allochromatium vinosum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Allochromatium vinosum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
21000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
46000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
67000
-
-
Allochromatium vinosum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + oxidized flavocytochrome c
-
716916
Allochromatium vinosum
sulfur + reduced flavocytochrome c + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit
Allochromatium vinosum
Other publictions for EC 1.8.2.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
714154
Quentmeier
Sulfide dehydrogenase activity ...
Paracoccus pantotrophus
Biochemistry
43
14696-14703
2004
-
-
-
-
-
-
4
2
-
-
3
-
-
1
-
-
1
-
-
-
-
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2
1
-
-
-
1
1
-
-
1
2
-
-
-
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-
1
-
-
-
-
4
2
2
-
-
3
-
-
-
-
1
-
-
-
-
2
1
-
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-
1
1
-
-
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-
-
-
-
-
-
715342
Kostanjevecki
A membrane-bound flavocytochro ...
Ectothiorhodospira shaposhnikovii
J. Bacteriol.
182
3097-3103
2000
-
-
-
-
-
-
-
-
1
-
2
-
-
6
-
-
1
-
-
-
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1
1
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-
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-
-
1
-
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-
1
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1
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2
-
-
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-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
2
-
-
713981
Visser
A novel membrane-bound flavocy ...
Thiobacillus sp., Thiobacillus sp. W5
Arch. Microbiol.
167
295-301
1997
-
-
-
-
-
-
1
2
1
-
2
-
-
7
-
-
1
-
-
-
-
-
2
1
-
-
-
-
1
-
-
2
-
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-
-
-
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2
-
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-
-
1
-
2
1
-
2
-
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-
-
1
-
-
-
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
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716866
Van Driessche
Covalent structure of the flav ...
Allochromatium vinosum
Protein Sci.
5
1753-1764
1996
-
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
716105
Yamanaka
-
Sulfide-cytochrome c reductase ...
Allochromatium vinosum, Chlorobaculum thiosulfatiphilum
Methods Enzymol.
243
463-472
1994
-
-
-
-
-
-
2
-
-
-
6
-
-
2
-
-
2
-
-
-
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-
4
2
-
-
-
-
-
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-
4
-
2
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-
-
4
-
-
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-
2
-
-
-
-
6
-
-
-
-
2
-
-
-
-
4
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
716916
Chen
The structure of flavocytochro ...
Allochromatium vinosum
Science
266
430-432
1994
-
-
-
1
-
-
-
-
-
-
3
-
-
4
-
-
-
-
-
-
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-
1
1
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-
-
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2
-
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-
2
1
-
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3
-
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-
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1
1
-
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-
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714363
Gray
-
The role of a cytochrome c-552 ...
Allochromatium vinosum
Biochim. Biophys. Acta
680
290-296
1982
-
-
-
-
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-
-
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-
4
-
-
1
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1
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2
1
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-
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4
-
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1
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2
1
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-
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-
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-
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-
-
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715409
Fukumori
Flavocytochrome c of Chromatiu ...
Allochromatium vinosum
J. Biochem.
85
1405-1414
1979
-
-
-
-
-
-
2
1
-
-
3
-
-
5
-
-
-
-
-
-
-
-
5
1
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-
1
-
1
-
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-
-
-
-
-
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-
-
-
-
-
-
2
-
1
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-
3
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-
-
-
-
-
-
5
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
714361
Kusai
The oxidation mechanisms of th ...
Chlorobium vibrioforme f. thiosulfatophilum
Biochim. Biophys. Acta
325
304-314
1973
1
-
-
-
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-
4
-
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1
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1
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-
1
-
-
-
1
-
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-
-
2
-
-
1
1
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2
-
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-
1
4
-
-
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1
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-
1
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1
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