Replacement of Methionine as the Axial Ligand of Achromobacter cycloclastes Cytochrome C554 at High pH Values Revealed by Absorption, EPR and MCD Spectroscopy

Lígia M. Saraiva, A. J. Thomson, Nick E. Lebrun, Ming Y. Liu, William J. Payne, Jean Legall, Isabel Moura

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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.

Original languageEnglish
Pages (from-to)120-128
Number of pages9
JournalBiochemical And Biophysical Research Communications
Volume204
Issue number1
DOIs
Publication statusPublished - 1 Jan 1994

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