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Structure Information on the Bacterial Primary Donor P+ •, Acceptor QĀ •, and Radical Pair P+ •-QĀ • as Obtained from High-Field EPR/ENDOR and MO Studies

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The Reaction Center of Photosynthetic Bacteria

Abstract

Recent 3 mm (W-band, 95 GHz) high-field EPR and ENDOR studies are presented on the primary donor cation radicals P +•865 (bacteriochlorophyll dimer) in single crystals of reaction centers (RC’s) and on frozen solutions of acceptor anion radicals Q–• (quinones) and of the charge-separated radical pair P +•865 —QĀ• in photosynthetic bacteria Rb. sphaeroides R-26 and biomimetic model systems. Both the hyperfine tensors of various protons and the g-tensor of P +•865 have been determined and compared with tensor values calculated by INDO type MO methods that are based on recent X-ray structure data. The results consistently reveal a breaking of the local C2 symmetry of the electronic structure at the primary donor side of the reaction center. This might be relevant for the vectorial electron transfer along the protein complex. Among the quinone radical anions studied are frozen solutions of the electron acceptors of bacterial and plant reaction centers (ubiquinone and plastoquinone, respectively). The increased electron Zeeman interaction in high-field EPR leads to almost completely resolved g-tensor components, and single crystal-like hyperfine couplings could be measured even in disordered samples. The g-tensor values and component linewidths are sensitive probes for specific anisotropic interactions with the environment. Pulsed high-field EPR reveals anisotropic contributions to T2 relaxation by librational motion of the primary acceptor in its protein binding site. In the case of the transient correlated coupled radical pair P +•865 —QĀ• (Fe replaced by Zn) the spin-polarized high-field EPR spectra allow an unambiguous determination of the relative orientation of the g-tensors of the donor and acceptor parts. Thereby high-precision structure information is obtained on the electron transfer pigments after light-induced charge separation.

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Authors and Affiliations

  1. Dept. of Physics, Free University Berlin, Arnimallee 14, D-14195, Berlin, Germany

    K. Möbius & M. Plato

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  1. K. Möbius
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  2. M. Plato
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Editors and Affiliations

  1. Institut für Physikalische und Theoretische Chemie, Technische Universität München, Lichtenbergstraße 4, D - 85748, Garching, Germany

    Maria-Elisabeth Michel-Beyerle

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© 1996 Springer-Verlag Berlin Heidelberg

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Möbius, K., Plato, M. (1996). Structure Information on the Bacterial Primary Donor P+ •, Acceptor QĀ •, and Radical Pair P+ •-QĀ • as Obtained from High-Field EPR/ENDOR and MO Studies. In: Michel-Beyerle, ME. (eds) The Reaction Center of Photosynthetic Bacteria. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61157-5_6

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  • DOI: https://doi.org/10.1007/978-3-642-61157-5_6

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-64723-9

  • Online ISBN: 978-3-642-61157-5

  • eBook Packages: Springer Book Archive

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