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Literature summary for 1.1.98.6 extracted from

  • Mulliez, E.; Ollagnier-de Choudens, S.; Meier, C.; Cremonini, M.; Luchinat, C.; Trautwein, A.X.; Fontecave, M.
    Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli (1999), J. Biol. Inorg. Chem., 4, 614-620.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P28903
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-

Synonyms

Synonyms Comment Organism
anaerobic ribonucleoside-triphosphate reductase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center the [4Fe-4S]+ form is extremely sensitive to oxygen and converted to [4Fe-4S]2+, [3Fe-4S]+/0, and to the stable [2Fe-2S]2+ form. The oxidized protein retains full activity. The [2Fe-2S] form of the protein can be converted into a [3Fe-4S] form during chromatography on dATP-Sepharose Escherichia coli