Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Rhizobium sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Rhizobium sp. | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhizobium sp. | - |
- |
- |
Rhizobium sp. NT-26 | - |
- |
- |
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 | Comment | Organism | Structure |
---|---|---|---|
cytochrome c552 | native electron transfer partner | Rhizobium sp. |