 | This article contains
close paraphrasing of a non-free copyrighted source,
https://www.brenda-enzymes.org/enzyme.php?ecno=1.8.99.5 (
Copyvios report). (April 2020) |
| dissimilatory sulfite reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.99.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Dissimilatory sulfite reductase ( EC 1.8.99.5) is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction. [1]
The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2). [2] The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. [3] During the process an intramolecular trisulfide is formed between two L-cysteine residues of DsrC and the sulfur atom from sulfite. [4] This trisulfide can be reduced by a number of proteins including DsrK and TcmB. [5]
Reaction in organisms performing dissimilatory sulfate reduction:
- (1) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O (overall reaction)
- (1a) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O
- (1b) a [DsrC protein]-S-sulfanyl-L-cysteine = hydrogen sulfide + a [DsrC protein]-disulfide
Reaction in organisms performing sulfur oxidation:
- (2) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+ (overall reaction)
- (2a) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+
- (2b) a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
The systematic name of this enzyme class is hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase.
This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation.
References
- ^ Parey K, Warkentin E, Kroneck PM, Ermler U (October 2010). "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry. 49 (41): 8912–21. doi: 10.1021/bi100781f. PMID 20822098.
- ^ Schedel M, Vanselow M, Trüper HG (1979). "Siroheme sulfite reductase isolated from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties". Archives of Microbiology. 121 (1): 29–36. Bibcode: 1979ArMic.121...29S. doi: 10.1007/BF00409202. S2CID 22126920.
- ^ Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M (December 2008). "The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration". The Journal of Biological Chemistry. 283 (49): 34141–9. doi: 10.1074/jbc.M805643200. PMC 2662231. PMID 18829451.
- ^ Santos AA, Venceslau SS, Grein F, Leavitt WD, Dahl C, Johnston DT, Pereira IA (December 2015). "A protein trisulfide couples dissimilatory sulfate reduction to energy conservation". Science. 350 (6267): 1541–5. Bibcode: 2015Sci...350.1541S. doi: 10.1126/science.aad3558. PMID 26680199. S2CID 206643054.
- ^ Venceslau SS, Stockdreher Y, Dahl C, Pereira IA (July 2014). "The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837 (7): 1148–64. doi: 10.1016/j.bbabio.2014.03.007. PMID 24662917.
| This article contains
close paraphrasing of a non-free copyrighted source,
https://www.brenda-enzymes.org/enzyme.php?ecno=1.8.99.5 (
Copyvios report). (April 2020) |
| dissimilatory sulfite reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.99.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Dissimilatory sulfite reductase ( EC 1.8.99.5) is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction. [1]
The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2). [2] The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. [3] During the process an intramolecular trisulfide is formed between two L-cysteine residues of DsrC and the sulfur atom from sulfite. [4] This trisulfide can be reduced by a number of proteins including DsrK and TcmB. [5]
Reaction in organisms performing dissimilatory sulfate reduction:
- (1) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O (overall reaction)
- (1a) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O
- (1b) a [DsrC protein]-S-sulfanyl-L-cysteine = hydrogen sulfide + a [DsrC protein]-disulfide
Reaction in organisms performing sulfur oxidation:
- (2) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+ (overall reaction)
- (2a) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+
- (2b) a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide
The systematic name of this enzyme class is hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase.
This enzyme is different from EC 1.8.1.2, assimilatory sulfite reductase (NADPH), and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin), which are involved in sulfate assimilation.
References
- ^ Parey K, Warkentin E, Kroneck PM, Ermler U (October 2010). "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry. 49 (41): 8912–21. doi: 10.1021/bi100781f. PMID 20822098.
- ^ Schedel M, Vanselow M, Trüper HG (1979). "Siroheme sulfite reductase isolated from Chromatium vinosum. Purification and investigation of some of its molecular and catalytic properties". Archives of Microbiology. 121 (1): 29–36. Bibcode: 1979ArMic.121...29S. doi: 10.1007/BF00409202. S2CID 22126920.
- ^ Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M (December 2008). "The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration". The Journal of Biological Chemistry. 283 (49): 34141–9. doi: 10.1074/jbc.M805643200. PMC 2662231. PMID 18829451.
- ^ Santos AA, Venceslau SS, Grein F, Leavitt WD, Dahl C, Johnston DT, Pereira IA (December 2015). "A protein trisulfide couples dissimilatory sulfate reduction to energy conservation". Science. 350 (6267): 1541–5. Bibcode: 2015Sci...350.1541S. doi: 10.1126/science.aad3558. PMID 26680199. S2CID 206643054.
- ^ Venceslau SS, Stockdreher Y, Dahl C, Pereira IA (July 2014). "The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837 (7): 1148–64. doi: 10.1016/j.bbabio.2014.03.007. PMID 24662917.