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Literature summary for 1.15.1.2 extracted from

  • Mathe, C.; Niviere, V.; Houee-Levin, C.; Mattioli, T.A.
    Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii (2006), Biophys. Chem., 119, 38-48.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron EPR analysis of wild-type and mutant E48A. Rapid treatment with H2O2 results in the stabilization of a side-on high spin Fe3+-(eta2-OO) peroxo species. Comparison between Treponema pallidum and Desulfoarctus baarsii enzyme Desulfarculus baarsii
Iron EPR analysis of wild-type and mutant E48A. Rapid treatment with H2O2 results in the stabilization of a side-on high spin Fe3+-(eta2-OO) peroxo species. Comparison between Treponema pallidum and Desulfoarctus baarsii enzyme. Above pH 8.5, the iron centre of Treponema pallidum becomes unstable and no spectra can be obtained Treponema pallidum

Organism

Organism UniProt Comment Textmining
Desulfarculus baarsii
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-
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Treponema pallidum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining