A general exit strategy of monoheme cytochromes c and c2 in electron transfer complexes?

IUBMB Life. 2015 Sep;67(9):694-700. doi: 10.1002/iub.1410. Epub 2015 Aug 26.

Abstract

Using our previously reported maps of the electrostatic surface of horse heart ferri- and ferro-cyt c, comparisons were made between the complementary electrostatic surfaces of three cyt c peroxidase-cyt c complexes and the photosynthetic reaction center-cyt c complex, considering both iron oxidation states. The results obtained were consistent with a sliding mechanism for the electron shuttle on the surface of the protein complexes, promoted by the change in iron oxidation state. This mechanism was found to be in agreement with theoretical and NMR studies reported in the literature. Importantly, the analysis also provided a rationale for recognition of nonproductive associations. As we have previously reported the same conclusion on examination of redox partners of cyt c in the mitochondrial respiratory pathway, our hypothesis is that the proposed mechanism could represent a general exit strategy of monoheme cyts c and c2 in electron transfer complexes.

Keywords: cytochrome c; cytochrome c2; electron transfer complexes; electrostatic surface; exit strategy; redox protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacteria / metabolism
  • Cell Respiration / physiology*
  • Cytochromes c / chemistry*
  • Cytochromes c / metabolism*
  • Electron Transport
  • Horses
  • Kinetics
  • Models, Molecular
  • Oxidation-Reduction
  • Peroxidase
  • Photosynthetic Reaction Center Complex Proteins / metabolism*
  • Protein Conformation
  • Saccharomyces cerevisiae / metabolism

Substances

  • Photosynthetic Reaction Center Complex Proteins
  • Cytochromes c
  • Peroxidase