Application of exciton coupling theory to the structure of mitochondrial cytochrome b

Biochemistry. 1994 Jan 11;33(1):176-85. doi: 10.1021/bi00167a023.

Abstract

The circular dichroism of the reduced bis-heme mitochondrial cytochrome b in the Soret region has been analyzed using exciton theory. The theory was applied to a geometric model that reflects the current consensus of the structure of this membrane protein [Degli Esposti, M., De Vries, S., Crimi, M., Ghelli, A., Patarnello, T., & Meyer, A. (1993) Biochim. Biophys. Acta 1143, 243-271]. The analysis suggests that the iron-iron distance is about 19.5 A, with a possible range of 17-23 A; the two hemes appear to be canted at 45 degrees with respect to one another. It appears that the two hemes undergo a relative angular displacement upon reduction, suggesting some flexibility in the protein structure. Some applications of this analysis to other bis-heme proteins are considered.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Circular Dichroism
  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / isolation & purification
  • Electron Transport Complex III / chemistry
  • Electron Transport Complex III / isolation & purification
  • Mathematics
  • Mitochondria, Heart / metabolism
  • Models, Structural
  • Models, Theoretical
  • Oxidation-Reduction
  • Protein Conformation*
  • Protein Structure, Secondary*
  • Spectrophotometry

Substances

  • Cytochrome b Group
  • Electron Transport Complex III