Purification and characterisation of cytochrome c' from Neisseria meningitidis

, Lowe, E, Butler, Clive, & Moir, James (2005) Purification and characterisation of cytochrome c' from Neisseria meningitidis. Biochemical Society Transactions, 33(1), pp. 187-189.

Description

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).

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4 citations in Web of Science®
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ID Code: 7160
Item Type: Contribution to Journal (Journal Article)
Refereed: Yes
Measurements or Duration: 3 pages
Keywords: Cytochrome c?, Neisseria Meningitidis, Nitric Oxide, Nitrosyl Complex, Purification, Spectroscopy
ISSN: 0300-5127
Pure ID: 34310696
Divisions: Past > QUT Faculties & Divisions > Faculty of Science and Technology
Past > Institutes > Institute of Health and Biomedical Innovation
Copyright Owner: Consult author(s) regarding copyright matters
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Deposited On: 27 Apr 2007 00:00
Last Modified: 03 Mar 2024 06:53