Effect of protein relaxation on electron transfer from the cytochrome subunit to the bacteriochlorophyll dimer in Rps. sulfoviridis reaction centers within mixed adiabatic/nonadiabatic model

Bioelectrochemistry. 2002 May 15;56(1-2):3-8. doi: 10.1016/s1567-5394(02)00036-1.

Abstract

The broad set of nonexponential electron transfer (ET) kinetics in reaction centers (RC) from Rhodopseudomonas sulfoviridis in temperature range 297-40 K are described within a mixed adiabatic/nonadiabatic model. The key point of the model is the combination of Sumi-Marcus and Rips-Jortner approaches which can be represented by the separate contributions of temperature-independent vibrational (v) and temperature-dependent diffusive (d) coordinates to the preexponential factor, to the free energy of reaction DeltaG=DeltaG(v)+DeltaG(d)(T) and to the reorganization energy lambda=lambda(v)+lambda(d)(T). The broad distribution of protein dielectric relaxation times along the diffusive coordinate is considered within the Davidson-Cole formalism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacteriochlorophylls / chemistry*
  • Cytochromes / chemistry*
  • Dimerization
  • Kinetics
  • Models, Chemical*
  • Rhodopseudomonas / chemistry*
  • Thermodynamics

Substances

  • Bacterial Proteins
  • Bacteriochlorophylls
  • Cytochromes