Arsenate reductase (azurin)

arsenate reductase (azurin)
Identifiers
EC no.	1.20.9.1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Arsenate reductase (azurin) (EC 1.20.9.1) is an enzyme that catalyzes the chemical reaction

arsenite + H₂O + 2 azurin_ox${\displaystyle \rightleftharpoons }$ arsenate + 2 azurin_red + 2 H⁺

The 3 substrates of this enzyme are arsenite, water, and oxidised azurin, whereas its 3 products are arsenate, reduced azurin, and hydrogen ion.

Classification

This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with a copper protein as acceptor.

Nomenclature

The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase.

Structure and function

The enzyme contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Also uses a c-type cytochrome or O
_² as acceptors.

References

• Anderson GL, Williams J, Hille R (1992). "The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase". J. Biol. Chem. 267 (33): 23674–82. doi: 10.1016/S0021-9258(18)35891-5 . PMID   1331097.
• Ellis PJ, Conrads T, Hille R, Kuhn P (2001). "Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A". Structure. 9 (2): 125–32. doi: 10.1016/S0969-2126(01)00566-4 . PMID   11250197.