1.8.5.4: bacterial sulfide:quinone reductase
This is an abbreviated version!
For detailed information about bacterial sulfide:quinone reductase, go to the full flat file.
Word Map on EC 1.8.5.4
-
1.8.5.4
-
sulfur
-
h2s
-
thiosulfate
-
persulfide
-
polysulfide
-
acidithiobacillus
-
sulfurtransferase
-
sulfide-oxidizing
-
rhodanese
-
sulfane
-
ferrooxidans
-
3-mercaptopyruvate
-
anoxygenic
-
sulfur-oxidizing
-
chemolithotrophic
-
sulfide-dependent
-
echiuran
-
unicinctus
-
limnetica
-
urechis
-
monotopic
-
oscillatoria
-
tepidum
-
chlorobaculum
-
sulfide-rich
-
medicine
- 1.8.5.4
- sulfur
- h2s
- thiosulfate
- persulfide
- polysulfide
- acidithiobacillus
- sulfurtransferase
-
sulfide-oxidizing
- rhodanese
-
sulfane
- ferrooxidans
- 3-mercaptopyruvate
-
anoxygenic
-
sulfur-oxidizing
-
chemolithotrophic
-
sulfide-dependent
-
echiuran
- unicinctus
- limnetica
-
urechis
-
monotopic
- oscillatoria
- tepidum
- chlorobaculum
-
sulfide-rich
- medicine
Reaction
n HS-
+
n quinone
=
Synonyms
CmSQR, CpSQR, CT1087, HMT2, III SQR, membrane-bound sulfide:quinone oxidoreductases, SQOR, SQR, Sqrdl, sqrF, Suden_1879, Suden_2082, Suden_619, sulfide quinone oxidoreductase, sulfide quinone reductase, sulfide-quinone oxidoreductase, sulfide-quinone reductase, sulfide: quinone oxidoreductase, sulfide:decylubiquinone oxidoreductase, sulfide:quinone oxidoreductase, sulfidequinone reductase-like protein, TrSqrF, type I SQR, type III sulfide:quinone oxidoreductase, type VI sulfide:quinone oxidoreductase
ECTree
1.8.5.4 bacterial sulfide:quinone reductaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.8.5.4 - bacterial sulfide:quinone reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
NaHS
the growth of the DELTAsqr mutant is fully inhibited while the wild-type and the complementation strain are partly inhibited after treatment with 4-5 mM NaHS
2n-nonyl-4-hydroxyquinoline-N-oxide
complete inhibition at 0.001 mM
2n-nonyl-4-hydroxyquinoline-N-oxide
-
complete inhibition at 0.001 mM
antimycin A
-
at 0.01 mM antimycin, residual sulfide:quinone oxidoreductase activity amounts to 53.4%
iodoacetamide
can irreversibly inactivate TrSqrF but only if substrates are present and the enzyme is actively catalyzing its reaction. When the enzyme is inhibited by iodoacetamide, the FAD cofactor is released. The inhibition studies support a mechanism that entails opening and reforming of the heterodisulfide bridge during the catalytic cycle of TrSqrF
additional information
-
insentitive towards nonylhydroxyquinoline-N-oxide
-
additional information
-
not inhibited by 5n-undecyl-6-hydroxy-4,7-dioxobenzothiazole, 2-iodo-6-isopropyl-3-methyl-2'-4,4'-trinitrodiphenyl ether, and 3-(3',4'-dichlorophenyl)-1,1-dimelhylurea
-
additional information
-
insensitive to 3-(3'-4'-dichlorophenyl)-1,1-dimethylurea and 2-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenyl ether
-
additional information
detailed structure-function analysis of the type VI SQR enzyme which enables the proposal of a distinct mechanism of sulfide oxidation for this class. For catalysis of sulfide oxidation, all SQRs require FAD cofactor and a redox-active centre in the active site, usually formed between conserved essential cysteines. SQRs of different types have variation in the number and position of cysteines, highlighting the potential for diverse catalytic mechanisms. The photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina contains a type VI SQR enzyme (TrSqrF) having unusual catalytic parameters and four cysteines likely involved in the catalysis. TrSqrF homology structure modeling, the A chains of three structures of SqrE and SqrA enzymes of Acidianus ambivalens and Aquifex aeolicus, respectively, are selected for model building (PDB IDs 3H8L, 3HYW and 3HYV). The TrSqrF has four cysteines in the primary sequence: Cys332 is ubiquitous, while Cys121 is identified in type I, IV, V and VI SQRs and they correspond to the highly conserved Cys347 and Cys124 of Aquifex aeolicus SQR, respectively. There is no matching residue to the Cys156 of Aquifex aeolicus enzyme in the Thiocapsa roseopersicina and all other type VI SQR proteins. The Cys272 is a unique, characteristic conserved cysteine of the type VI SQRs. Based on the available SQR structures, the corresponding amino acids of this cysteine in type I and type V SQR proteins are localized in a surface loop. The TrSqrF also contains a cysteine residue (Cys49) which is not conserved within any SQR type
-
additional information
-
detailed structure-function analysis of the type VI SQR enzyme which enables the proposal of a distinct mechanism of sulfide oxidation for this class. For catalysis of sulfide oxidation, all SQRs require FAD cofactor and a redox-active centre in the active site, usually formed between conserved essential cysteines. SQRs of different types have variation in the number and position of cysteines, highlighting the potential for diverse catalytic mechanisms. The photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina contains a type VI SQR enzyme (TrSqrF) having unusual catalytic parameters and four cysteines likely involved in the catalysis. TrSqrF homology structure modeling, the A chains of three structures of SqrE and SqrA enzymes of Acidianus ambivalens and Aquifex aeolicus, respectively, are selected for model building (PDB IDs 3H8L, 3HYW and 3HYV). The TrSqrF has four cysteines in the primary sequence: Cys332 is ubiquitous, while Cys121 is identified in type I, IV, V and VI SQRs and they correspond to the highly conserved Cys347 and Cys124 of Aquifex aeolicus SQR, respectively. There is no matching residue to the Cys156 of Aquifex aeolicus enzyme in the Thiocapsa roseopersicina and all other type VI SQR proteins. The Cys272 is a unique, characteristic conserved cysteine of the type VI SQRs. Based on the available SQR structures, the corresponding amino acids of this cysteine in type I and type V SQR proteins are localized in a surface loop. The TrSqrF also contains a cysteine residue (Cys49) which is not conserved within any SQR type
-
