JBIC Journal of Biological Inorganic Chemistry

, Volume 4, Issue 6, pp 824–837 | Cite as

Mitochondrial cytochromes c: a comparative analysis

  • L. Banci
  • I. Bertini
  • A. Rosato
  • G. Varani
ORIGINAL ARTICLE

c

proteins of known sequence have been modeled in the oxidized state based on the existing crystallographic and NMR structures. The secondary structural elements and the overall three-dimensional structure were found to be maintained throughout the superfamily, despite variability in the sequence of individual proteins. The iron axial ligands and their reciprocal orientation were found to be nearly universally conserved. Residues constituting the hydrophobic core of the protein are also very highly conserved or conservatively substituted. Certain surface-exposed charged as well as hydrophobic groups have also been found to be conserved to the same degree as core residues. Patterns of conservation of exposed residues identify regions of the protein that are likely to be critical for its function in electron transfer.

Cytochrome c Electron transfer Structure 

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Copyright information

© Society of Biological Inorganic Chemistry 1999

Authors and Affiliations

  • L. Banci
    • 1
  • I. Bertini
    • 1
  • A. Rosato
    • 1
  • G. Varani
    • 2
  1. 1.Department of Chemistry and Centro Risonanze Magnetiche University of Florence, Via Luigi Sacconi 6 I-50019 Sesto Fiorentino, Italy e-mail: bertini@cerm.unifi.it Tel.: +39-055-4209272 Fax: +39-055-4209271IT
  2. 2.Medical Research Council, Laboratory of Molecular Biology MRC Centre, Hills Road, Cambridge CB2 2QH, UKGB

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