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Purification and characterization of cytochrome c′ from Neisseria meningitidis

Lookup NU author(s): Dr Elisabeth Lowe, Dr Clive Butler


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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.

Publication metadata

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


DOI: 10.1042/BST0330187

PubMed id: 15667302

Notes: 10th Nitrogen Cycle Meeting 2004

Library holdings: Search Newcastle University Library for this item

ISBN: 14708752