Arsenate reductase (cytochrome c)

Arsenate reductase (cytochrome c)
Identifiers
EC number 1.20.2.1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Arsenate reductase (cytochrome c) (EC 1.20.2.1, arsenite oxidase) is an enzyme with systematic name arsenite:cytochrome c oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction

arsenite + H2O + 2 oxidized cytochrome c arsenate + 2 reduced cytochrome c + 2 H+

Arsenate reductase is a molybdoprotein isolated from alpha-proteobacteria that contains iron-sulfur clusters.

References

  1. ↑ vanden Hoven, R.N.; Santini, J.M. (2004). "Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor". Biochim. Biophys. Acta. 1656: 148–155. doi:10.1016/j.bbabio.2004.03.001. PMID 15178476.
  2. ↑ Santini, J.M.; Kappler, U.; Ward, S.A.; Honeychurch, M.J.; vanden Hoven, R.N.; Bernhardt, P.V. (2007). "The NT-26 cytochrome c552 and its role in arsenite oxidation". Biochim. Biophys. Acta. 1767: 189–196. doi:10.1016/j.bbabio.2007.01.009. PMID 17306216.
  3. ↑ Branco, R.; Francisco, R.; Chung, A.P.; Morais, P.V. (2009). "Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24". Appl. Environ. Microbiol. 75: 5141–5147. doi:10.1128/aem.02798-08. PMC 2725503. PMID 19525272.
  4. ↑ Lieutaud, A.; van Lis, R.; Duval, S.; Capowiez, L.; Muller, D.; Lebrun, R.; Lignon, S.; Fardeau, M.L.; Lett, M.C.; Nitschke, W.; Schoepp-Cothenet, B. (2010). "Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes". J. Biol. Chem. 285: 20433–20441. doi:10.1074/jbc.m110.113761. PMC 2898339. PMID 20421652.
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