BRENDA - Enzyme Database

Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552

Kalimuthu, P.; Heath, M.D.; Santini, J.M.; Kappler, U.; Bernhardt, P.V.; Biochim. Biophys. Acta 1837, 112-120 (2014) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
1.20.2.1
expression in Escherichia coli
Rhizobium sp.
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.20.2.1
periplasm
-
Rhizobium sp.
-
-
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.20.2.1
Rhizobium sp.
-
-
-
1.20.2.1
Rhizobium sp. NT-26
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.20.2.1
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
727089
Rhizobium sp.
?
-
-
-
?
1.20.2.1
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
727089
Rhizobium sp. NT-26
?
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.20.2.1
cytochrome c552
native electron transfer partner
Rhizobium sp.
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.20.2.1
expression in Escherichia coli
Rhizobium sp.
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.20.2.1
cytochrome c552
native electron transfer partner
Rhizobium sp.
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.20.2.1
periplasm
-
Rhizobium sp.
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.20.2.1
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
727089
Rhizobium sp.
?
-
-
-
?
1.20.2.1
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
727089
Rhizobium sp. NT-26
?
-
-
-
?