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Combined Dynamic Model for the Kinetics of Electron Transfer from Cytochrome to a Bacteriochlorophill Dimer in Reaction Centers of Rps. Sulfoviridis

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Abstract

The electron transfer from the heme of cytochrome c to the bacteriochlorophill dimer in reaction centers of photosynthetic purple bacteria Rps. sulfoviridis is studied by laser flash photolysis at 40–296 K in conditions where one, two, or three cytochrome hemes are chemically reduced. In the model used for the electron transfer kinetics, the protein relaxation is described with a temperature-independent oscillatory coordinate and a temperature-dependent diffusion coordinate, with the protein dielectric relaxation times widely distributed along the diffusion coordinate. It is found that all the protein complexes can be divided into proteins with fast (k et = 107 to 10–4 s–1) and slow (k et ≪ 100 s–1) electron transfer. These populations presumably differ by the protonation state of the functional group. The contribution of the oscillatory and diffusion coordinates alters, which severely affects k et. Parameters V ab, ΔG, λ, τ0, and β for these reactions are determined.

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Authors and Affiliations

  1. Russian Academy of Sciences, Institute of Problems of Chemical Physics, Chernogolovka, Moscow oblast, 142432, Russia

    A. I. Kotel'nikov, E. S. Medvedev & B. L. Psikha

  2. Instituto de Bioquimica Vegetal y Fotosintesis, Universidad de Sevilla-CSIC, E-41092, Sevilla, Spain

    J. M. Ortega

  3. DEVM, CEA/Cadarache, B.P. No 1, 13115, St Paul les Durance Cedex, France

    D. Garcia

  4. DBCM-SBE, Bát, 532, CEA/Saclay, 91191, Gif-sur-Yvette Cedex, France

    P. Mathis

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  1. A. I. Kotel'nikov
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Kotel'nikov, A.I., Ortega, J.M., Medvedev, E.S. et al. Combined Dynamic Model for the Kinetics of Electron Transfer from Cytochrome to a Bacteriochlorophill Dimer in Reaction Centers of Rps. Sulfoviridis. Russian Journal of Electrochemistry 38, 77–87 (2002). https://doi.org/10.1023/A:1013742513054

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