BRENDA - Enzyme Database
show all sequences of 1.8.2.3

The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553

Kusai, K.; Yamanaka, T.; Biochim. Biophys. Acta 325, 304-314 (1973)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
neither FAD nor FMN activate sulfide-cytochrome c reduction catalysed by cytochrome c-553
Chlorobium vibrioforme f. thiosulfatophilum
Inhibitors
Inhibitors
Commentary
Organism
Structure
Atebrin
60% inhibition at 0.1 mM
Chlorobium vibrioforme f. thiosulfatophilum
cyanide
80% inhibition at 0.001 mM
Chlorobium vibrioforme f. thiosulfatophilum
additional information
not inhibited by EDTA, o-phenanthroline, and CO
Chlorobium vibrioforme f. thiosulfatophilum
NaN3
7% inhibition at 10 mM
Chlorobium vibrioforme f. thiosulfatophilum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobium vibrioforme f. thiosulfatophilum
-
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation and DEAE-cellulose column chromatography
Chlorobium vibrioforme f. thiosulfatophilum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + ferricytochrome c 555
-
714361
Chlorobium vibrioforme f. thiosulfatophilum
sulfur + ferrocytochrome c 555 + H+
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
the enzyme is completely inactive after 2 min at 80°C
Chlorobium vibrioforme f. thiosulfatophilum
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
covalently-bound
Chlorobium vibrioforme f. thiosulfatophilum
heme
-
Chlorobium vibrioforme f. thiosulfatophilum
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0001
-
in 0.1 M Tris-HCl buffer, pH 7.4, at 20°C
Chlorobium vibrioforme f. thiosulfatophilum
cyanide
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
neither FAD nor FMN activate sulfide-cytochrome c reduction catalysed by cytochrome c-553
Chlorobium vibrioforme f. thiosulfatophilum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
covalently-bound
Chlorobium vibrioforme f. thiosulfatophilum
heme
-
Chlorobium vibrioforme f. thiosulfatophilum
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0001
-
in 0.1 M Tris-HCl buffer, pH 7.4, at 20°C
Chlorobium vibrioforme f. thiosulfatophilum
cyanide
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Atebrin
60% inhibition at 0.1 mM
Chlorobium vibrioforme f. thiosulfatophilum
cyanide
80% inhibition at 0.001 mM
Chlorobium vibrioforme f. thiosulfatophilum
additional information
not inhibited by EDTA, o-phenanthroline, and CO
Chlorobium vibrioforme f. thiosulfatophilum
NaN3
7% inhibition at 10 mM
Chlorobium vibrioforme f. thiosulfatophilum
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation and DEAE-cellulose column chromatography
Chlorobium vibrioforme f. thiosulfatophilum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + ferricytochrome c 555
-
714361
Chlorobium vibrioforme f. thiosulfatophilum
sulfur + ferrocytochrome c 555 + H+
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
the enzyme is completely inactive after 2 min at 80°C
Chlorobium vibrioforme f. thiosulfatophilum
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
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4
2
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1
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2
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1
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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
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1
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6
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1
1
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2
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2
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713981
Visser
A novel membrane-bound flavocy ...
Thiobacillus sp., Thiobacillus sp. W5
Arch. Microbiol.
167
295-301
1997
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1
2
1
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7
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1
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716866
Van Driessche
Covalent structure of the flav ...
Allochromatium vinosum
Protein Sci.
5
1753-1764
1996
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1
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716105
Yamanaka
-
Sulfide-cytochrome c reductase ...
Allochromatium vinosum, Chlorobaculum thiosulfatiphilum
Methods Enzymol.
243
463-472
1994
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2
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6
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2
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2
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4
2
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4
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6
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4
2
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2
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716916
Chen
The structure of flavocytochro ...
Allochromatium vinosum
Science
266
430-432
1994
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1
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1
1
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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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4
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1
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1
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715409
Fukumori
Flavocytochrome c of Chromatiu ...
Allochromatium vinosum
J. Biochem.
85
1405-1414
1979
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2
1
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5
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1
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5
1
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1
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1
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714361
Kusai
The oxidation mechanisms of th ...
Chlorobium vibrioforme f. thiosulfatophilum
Biochim. Biophys. Acta
325
304-314
1973
1
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