| EC |
1.20.9.1 |
| Accepted name: |
arsenate reductase (azurin) |
| Reaction: |
arsenite + H2O + 2 oxidized azurin = arsenate + 2 reduced azurin + 2 H+ |
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For diagram of arsenate catabolism, click here |
| Glossary: |
Azurin is a blue copper protein found in many bacteria, which undergoes oxidation-reduction between Cu(I) and Cu(II), and transfers single electrons between enzymes. |
| Other name(s): |
arsenite oxidase (ambiguous) |
| Systematic name: |
arsenite:azurin oxidoreductase |
| Comments: |
Contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Isolated from β-proteobacteria. Also uses a c-type cytochrome or O2 as acceptors. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 146907-46-2 |
| References: |
| 1. |
Anderson, G.L., Williams, J. and Hille, R. The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase. J. Biol. Chem. 267 (1992) 23674–23682. [PMID: 1331097] |
| 2. |
Ellis, P.J., Conrads, T., Hille, R. and Kuhn, P. Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å. Structure 9 (2001) 125–132. [DOI] [PMID: 11250197] |
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| [EC 1.20.9.1 created 2001 as EC 1.20.98.1, transferred 2011 to EC 1.20.9.1] |
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