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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Saraiva LM,Thomson AJ,Le Brun NE,Liu MY,Payne WJ,LeGall J,Moura Idoi
10.1006/bbrc.1994.2434subject
Has Abstractpub_date
1994-10-14 00:00:00pages
120-8issue
1eissn
0006-291Xissn
1090-2104pii
S0006291X8472434Xjournal_volume
204pub_type
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