Dissimilatory sulfite reductase

Dissimilatory sulfite reductase (EC 1.8.99.5) is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction.[1]

dissimilatory sulfite reductase
Identifiers
EC no.1.8.99.5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

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

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  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.