Replacement of methionine as the axial ligand of Achromobacter cycloclastes cytochrome c554 at high pH values revealed by absorption, EPR and MCD spectroscopy.

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.

authors

Saraiva LM,Thomson AJ,Le Brun NE,Liu MY,Payne WJ,LeGall J,Moura I

doi

10.1006/bbrc.1994.2434

subject

Has Abstract

pub_date

1994-10-14 00:00:00

pages

120-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X8472434X

journal_volume

204

pub_type

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