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

\rightleftharpoons

arsenate + 2 reduced cytochrome c + 2 H⁺

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

References

↑ vanden Hoven, R.N.; Santini, J.M. (2004). "Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor". Biochim. Biophys. Acta. 1656: 148–155. doi:10.1016/j.bbabio.2004.03.001. PMID 15178476.
↑ Santini, J.M.; Kappler, U.; Ward, S.A.; Honeychurch, M.J.; vanden Hoven, R.N.; Bernhardt, P.V. (2007). "The NT-26 cytochrome c₅₅₂ and its role in arsenite oxidation". Biochim. Biophys. Acta. 1767: 189–196. doi:10.1016/j.bbabio.2007.01.009. PMID 17306216.
↑ Branco, R.; Francisco, R.; Chung, A.P.; Morais, P.V. (2009). "Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24". Appl. Environ. Microbiol. 75: 5141–5147. doi:10.1128/aem.02798-08. PMID 19525272.
↑ Lieutaud, A.; van Lis, R.; Duval, S.; Capowiez, L.; Muller, D.; Lebrun, R.; Lignon, S.; Fardeau, M.L.; Lett, M.C.; Nitschke, W.; Schoepp-Cothenet, B. (2010). "Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes". J. Biol. Chem. 285: 20433–20441. doi:10.1074/jbc.m110.113761. PMID 20421652.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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