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

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
Search
PMCarticles
PubMedarticles
NCBIproteins
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

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  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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