Biology:Arsenate reductase (cytochrome c)

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Short description: Enzyme
Arsenate reductase (cytochrome c)
Identifiers
EC number1.20.2.1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] arsenate + 2 reduced cytochrome c + 2 H+

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

References

  1. "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. June 2004. doi:10.1016/j.bbabio.2004.03.001. PMID 15178476. 
  2. "The NT-26 cytochrome c552 and its role in arsenite oxidation". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1767 (2): 189–96. February 2007. doi:10.1016/j.bbabio.2007.01.009. PMID 17306216. 
  3. "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. August 2009. doi:10.1128/aem.02798-08. PMID 19525272. 
  4. "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. July 2010. doi:10.1074/jbc.m110.113761. PMID 20421652. 

External links