Arsenate reductase (cytochrome c)

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 (cytochrome c)
Identifiers
EC no.1.20.2.1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

References

  1. vanden Hoven RN, Santini JM (June 2004). "Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1656 (2–3): 148–55. doi:10.1016/j.bbabio.2004.03.001. PMID 15178476.
  2. Santini JM, Kappler U, Ward SA, Honeychurch MJ, vanden Hoven RN, Bernhardt PV (February 2007). "The NT-26 cytochrome c552 and its role in arsenite oxidation". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1767 (2): 189–96. doi:10.1016/j.bbabio.2007.01.009. PMID 17306216.
  3. Branco R, Francisco R, Chung AP, Morais PV (August 2009). "Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24". Applied and Environmental Microbiology. 75 (15): 5141–7. 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 ML, Lett MC, Nitschke W, Schoepp-Cothenet B (July 2010). "Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes". The Journal of Biological Chemistry. 285 (27): 20433–41. doi:10.1074/jbc.m110.113761. PMC 2898339. PMID 20421652.
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