|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Composite Reactions → Electron-Transfer-Reactions|
|Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
|arsenite-oxidizing bacterium NT-14 :||arsenite oxidoreductase
In Pathway: arsenite oxidation I (respiratory)
Reaction Locations: inner membrane (sensu Gram-negative Bacteria)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: arsenate reductase (cytochrome c)
Enzyme Commission Synonyms: arsenite oxidase (ambiguous)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -0.25228882 [Latendresse13]
Enzyme Commission Summary:
A molybdoprotein containing iron-sulfur clusters. Isolated from α-proteobacteria. Unlike EC 184.108.40.206, arsenate reductase (azurin), it does not use azurin as acceptor.
Branco09: Branco R, Francisco R, Chung AP, Morais PV (2009). "Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24." Appl Environ Microbiol 75(15);5141-7. PMID: 19525272
Lieutaud10: Lieutaud A, van Lis R, Duval S, Capowiez L, Muller D, Lebrun R, Lignon S, Fardeau ML, Lett MC, 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(27);20433-41. PMID: 20421652
Santini07: Santini JM, Kappler U, Ward SA, Honeychurch MJ, vanden Hoven RN, Bernhardt PV (2007). "The NT-26 cytochrome c552 and its role in arsenite oxidation." Biochim Biophys Acta 1767(2);189-96. PMID: 17306216
vandenHoven04: vanden Hoven RN, Santini JM (2004). "Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor." Biochim Biophys Acta 1656(2-3);148-55. PMID: 15178476
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