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Literature summary for 1.20.2.1 extracted from

  • Santini, J.; Kappler, U.; Ward, S.; Honeychurch, M.; vanden Hoven, R.; Bernhardt, P.
    The NT-26 cytochrome c552 and its role in arsenite oxidation (2007), Biochim. Biophys. Acta, 1767, 189-196.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arsenite + cytochrome c552 + H2O arsenite-oxidising bacterium physiological electron acceptor arsenate + reduced cytochrome c552
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?
arsenite + cytochrome c552 + H2O arsenite-oxidising bacterium NT-26 physiological electron acceptor arsenate + reduced cytochrome c552
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?

Organism

Organism UniProt Comment Textmining
arsenite-oxidising bacterium Q6VAL9 subunit aroB
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arsenite-oxidising bacterium NT-26 Q6VAL9 subunit aroB
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arsenite + cytochrome c + H2O horse heart cytochrome c serves as an in vitro elelctron acceptor arsenite-oxidising bacterium arsenate + reduced cytochrome c
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?
arsenite + cytochrome c + H2O horse heart cytochrome c serves as an in vitro elelctron acceptor arsenite-oxidising bacterium NT-26 arsenate + reduced cytochrome c
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?
arsenite + cytochrome c552 + H2O physiological electron acceptor arsenite-oxidising bacterium arsenate + reduced cytochrome c552
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?
arsenite + cytochrome c552 + H2O physiological electron acceptor arsenite-oxidising bacterium NT-26 arsenate + reduced cytochrome c552
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?

Cofactor

Cofactor Comment Organism Structure
cytochrome c552 physiological electron acceptor to the arsenite oxidase, the gene that encodes this protein is located downstream of the arsenite oxidase genes aroBA. Characterisation reveals the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes arsenite-oxidising bacterium