Purification and characterization of cytochrome c ' from Neisseria meningitidis

W M Huston, E C Lowe, C S Butler, J W B Moir

Research output: Contribution to journalArticlepeer-review


Cytochrome c', a c-type cytochrome with unique spectroscopic and magnetic properties, has been characterized in a variety of denitrifying and photosynthetic bacteria. Cytochrome cl 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 cl-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).

Original languageEnglish
Pages (from-to)187-189
Number of pages3
JournalBiochemical Society transactions
Publication statusPublished - Feb 2005


  • cytochrome c '
  • Neisseria meningitidis
  • nitrosyl complex
  • nitric oxide
  • purification
  • spectroscopy

Cite this