Browse by author
Lookup NU author(s): Dr Elisabeth Lowe, Dr Clive Butler
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Cytochrome c′, a c-type cytochrome with unique spectroscopic and magnetic properties, has been characterized in a variety of denitrifying and photosynthetic bacteria. Cytochrome c′ has a role in defence and/or removal of NO but the mechanism of action is not clear. To examine the function of cytochrome c′ from Neisseria meningitidis, the protein was purified after heterologous overexpression in Escherichia coli. The electronic spectra of the oxidized c′ demonstrated a pH-dependent transition (over the pH range of 6-10) typical of known c′-type cytochromes. Interestingly, the form in which NO is supplied determines the redox state of the resultant haem-nitrosyl complex, Fe(III)-NO complexes were formed when Fe(II) or Fe(III) cytochrome c′ was sparged with NO gas, whereas an Fe(II)-NO complex was generated when NO was supplied using DEA NONOate (diazeniumdiolate). © 2005 Biochemical Society.
Author(s): Huston WM, Lowe EC, Butler CS, Moir JWB
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: Biochemical Society Transactions
Year of Conference: 2004
Pages: 187-189
ISSN: 0300-5127
Publisher: Portland Press
URL: http://dx.doi.org/10.1042/BST0330187
DOI: 10.1042/BST0330187
PubMed id: 15667302
Notes: 10th Nitrogen Cycle Meeting 2004
Library holdings: Search Newcastle University Library for this item
ISBN: 14708752
