Arsenate reductase (cytochrome c)

Arsenate reductase (cytochrome c)
Arsenate reductase (cytochrome c)
Identifiers
EC no.	1.20.2.1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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 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.
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.
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.
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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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 (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a 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 Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)