The Enzyme Database

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EC 1.20.2.1     
Accepted name: arsenate reductase (cytochrome c)
Reaction: arsenite + H2O + 2 oxidized cytochrome c = arsenate + 2 reduced cytochrome c + 2 H+
Other name(s): arsenite oxidase (ambiguous)
Systematic name: arsenite:cytochrome c oxidoreductase
Comments: A molybdoprotein containing iron-sulfur clusters. Isolated from α-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  vanden Hoven, R.N. and Santini, J.M. Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor. Biochim. Biophys. Acta 1656 (2004) 148–155. [DOI] [PMID: 15178476]
2.  Santini, J.M., Kappler, U., Ward, S.A., Honeychurch, M.J., vanden Hoven, R.N. and Bernhardt, P.V. The NT-26 cytochrome c552 and its role in arsenite oxidation. Biochim. Biophys. Acta 1767 (2007) 189–196. [DOI] [PMID: 17306216]
3.  Branco, R., Francisco, R., Chung, A.P. and Morais, P.V. Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24. Appl. Environ. Microbiol. 75 (2009) 5141–5147. [DOI] [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. and Schoepp-Cothenet, B. Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes. J. Biol. Chem. 285 (2010) 20433–20441. [DOI] [PMID: 20421652]
[EC 1.20.2.1 created 2011]
 
 


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