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  • Title: Replacement of methionine as the axial ligand of Achromobacter cycloclastes cytochrome c554 at high pH values revealed by absorption, EPR and MCD spectroscopy.
    Author: Saraiva LM, Thomson AJ, Le Brun NE, Liu MY, Payne WJ, LeGall J, Moura I.
    Journal: Biochem Biophys Res Commun; 1994 Oct 14; 204(1):120-8. PubMed ID: 7945350.
    Abstract:
    Cytochrome c554 from the denitrifying bacterium Achromobacter cycloclastes is a monoheme class II c-type cytochrome with a His-Met axial coordination at neutral pH. The amino acid composition and the N-terminal sequence of the cytochrome have been determined. Subsequent determination of the pH-dependence of the redox potential and examination of the EPR and MCD spectra of ferricytochrome c554 revealed a new form at high pH values made apparent with both spectroscopies. These observations are consistent with the presence of lysine as the axial ligand for which methionine substitutes at high pH values.
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