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Literature summary for 1.20.2.1 extracted from

  • Kalimuthu, P.; Heath, M.D.; Santini, J.M.; Kappler, U.; Bernhardt, P.V.
    Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552 (2014), Biochim. Biophys. Acta, 1837, 112-120.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhizobium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Rhizobium sp.
-
-

Organism

Organism UniProt Comment Textmining
Rhizobium sp.
-
-
-
Rhizobium sp. NT-26
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mediated electrocatalytic voltammetry study. In the absence of arsenite, or the enzyme, cytochrome c552 cofactor exhibits a well-defined single electron reversible response at a Au electrode modified with the long chain mercaptoundecanoic acid, which presents a self-assembled monolayer of negatively charged functional groups to the protein surface. In the presence of arsenite and enzyme a variety of CV waveforms are observed depending on sweep rate and substrate concentration. Arsenite binding is very fast Rhizobium sp. ?
-
 ?
additional information mediated electrocatalytic voltammetry study. In the absence of arsenite, or the enzyme, cytochrome c552 cofactor exhibits a well-defined single electron reversible response at a Au electrode modified with the long chain mercaptoundecanoic acid, which presents a self-assembled monolayer of negatively charged functional groups to the protein surface. In the presence of arsenite and enzyme a variety of CV waveforms are observed depending on sweep rate and substrate concentration. Arsenite binding is very fast Rhizobium sp. NT-26 ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
cytochrome c552 native electron transfer partner Rhizobium sp.