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Literature summary for 1.15.1.2 extracted from

  • Mathe, C.; Niviere, V.; Mattioli, T.A.
    Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes (2005), J. Am. Chem. Soc., 127, 16436-16441.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E47A the electronic absorption band corresponding to the oxidized active site exhibits a pH-dependent alkaline transition changing from ca. 644 to 560 nm as the pH increases and with an apparent pKa of 9.0 in wild-type. In mutant E47A, this pKa shifts to 6.7 Desulfarculus baarsii
K48I the electronic absorption band corresponding to the oxidized active site exhibits a pH-dependent alkaline transition changing from ca. 644 to 560 nm as the pH increases and with an apparent pKa of 9.0 in wild-type. In mutant K48I, this pKa shifts to 7.6 Desulfarculus baarsii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron non-heme iron in square-pyramidal [His4Cys] coordination. At basic pH a high-spin Fe3+-OH species is formed at the active site, which upon protonation results in a water molecule in the active site Desulfarculus baarsii

Organism

Organism UniProt Comment Textmining
Desulfarculus baarsii
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