ExplorEnz: EC 1.20.2.1

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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]