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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Conference Article|
February 01 2005
Purification and characterization of cytochrome c′ from Neisseria meningitidis
W.M. Huston;
W.M. Huston
*Department of Biology (Area 10), University of York, Heslington, York YO10 5YW, U.K.
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E.C. Lowe;
E.C. Lowe
*Department of Biology (Area 10), University of York, Heslington, York YO10 5YW, U.K.
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C.S. Butler;
C.S. Butler
†Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, U.K.
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J.W.B. Moir
J.W.B. Moir
1
*Department of Biology (Area 10), University of York, Heslington, York YO10 5YW, U.K.
1To whom correspondence should be addressed (email jm46@york.ac.uk).
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Publisher: Portland Press Ltd
Received:
September 29 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (1): 187–189.
Article history
Received:
September 29 2004
Citation
W.M. Huston, E.C. Lowe, C.S. Butler, J.W.B. Moir; Purification and characterization of cytochrome c′ from Neisseria meningitidis. Biochem Soc Trans 1 February 2005; 33 (1): 187–189. doi: https://doi.org/10.1042/BST0330187
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