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Mitochondrial cytochromes c: a comparative analysis.

L Banci1, I Bertini, A Rosato

  • 1Department of Chemistry, University of Florence, Sesto Fiorentino, Italy.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|January 13, 2000
PubMed
Summary
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Eukaryotic cytochrome c protein structures are highly conserved, especially key iron ligands and hydrophobic cores. Surface residue conservation highlights critical regions for electron transfer function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Evolution

Background:

  • Cytochrome c is a vital protein in cellular respiration and electron transfer.
  • Understanding its structure-function relationship is crucial for various biological processes.

Purpose of the Study:

  • To model the three-dimensional structures of 113 eukaryotic cytochrome c proteins.
  • To identify conserved structural elements and residues critical for function.

Main Methods:

  • Comparative structural modeling of oxidized cytochrome c proteins.
  • Analysis of crystallographic and NMR data for known structures.
  • Sequence and structural conservation analysis.

Main Results:

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  • High conservation of secondary and overall 3D structures across the cytochrome c superfamily.
  • Near-universal conservation of iron axial ligands and their orientation.
  • Significant conservation of hydrophobic core residues and certain surface-exposed residues.
  • Identification of conserved surface regions potentially involved in electron transfer.

    • Conclusions:

    • Eukaryotic cytochrome c structure is remarkably conserved, indicating functional constraints.
    • Conserved surface residues likely play key roles in mediating electron transfer.
    • Structural modeling provides insights into conserved functional mechanisms across diverse species.