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The Photosynthetic Bacterial Reaction Center II

Structure, Spectroscopy and Dynamics

  • Book
  • © 1992

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Editors:
  1. Jacques Breton

    1. CEN Saclay, Gif-sur-Yvette, France

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    You can also search for this editor in PubMed   Google Scholar

  2. André Verméglio

    1. CEN Cadarache, France

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    You can also search for this editor in PubMed   Google Scholar

Part of the book series: NATO Science Series A: (NSSA, volume 237)

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Table of contents (46 chapters)

  1. Front Matter

    Pages i-x
    Download chapter PDF

  2. The 3-D Structure of the Reaction Center from Rhodopseudomonas Viridis

    • Johann Deisenhofer, Hartmut Michel
    Pages 1-11

  3. Correlation Between the Polarized Light Absorption and the X-Ray Structure of Single Crystals of the Reaction Center from Rhodobacter Sphaeroides R-26

    • Harry A. Frank, Mila L. Aldema
    Pages 13-20

  4. Symmetrical Inter-Subunit Suppressors of the Bacterial Reaction Center cd-Helix Exchange Mutants

    • Steven J. Robles, Teresa Ranck, Douglas C. Youvan
    Pages 21-23

  5. Mutations that Affect the Donor Midpoint Potential in Reaction Centers from Rhodobacter Sphaeroides

    • J. C. Williams, N. W. Woodbury, A. K. W. Taguchi, J. M. Peloquin, H. A. Murchison, R. G. Alden et al.
    Pages 25-31

  6. Suggestions for Directed Engineering of Reaction Centers: Metal, Substituent and Charge Modifications

    • Jack Fajer, Louise Karle Hanson, Michael C. Zerner, Mark A. Thompson
    Pages 33-42

  7. Potential Energy Function for Photosynthetic Reaction Centre Chromophores: Energy Minimisations of a Crystalline Bacteriopheophytin a Analog

    • N. Foloppe, J. Breton, J. C. Smith
    Pages 43-48

  8. Bacterial Reaction Centers with Plant-Type Pheophytins

    • Hugo Scheer, Michaela Meyer, Ingrid Katheder
    Pages 49-57

  9. Trapping of a Stable Form of Reduced Bacteriopheophytin and Bacteriochlorophyll in Ectothiorhodospira SP. Photoreaction Center

    • Ted Mar, Gabriel Gingras
    Pages 59-65

  10. Triplet-Minus-Singlet Absorbance Difference Spectroscopy of Heliobacterium Chlorum Monitored with Absorbance-Detected Magnetic Resonance

    • J. Vrieze, E. J. van de Meent, A. J. Hoff
    Pages 67-77

  11. Mid- and Near-IR Electronic Transitions of P+: New Probes of Resonance Interactions and Structural Asymmetry in Reaction Centers

    • William W. Parson, Eliane Nabedryk, Jacques Breton
    Pages 79-88

  12. 15N Endor Experiments on the Primary Donor Cation Radical D+ in Bacterial Reaction Center Single Crystals of RB. Shaeroides R-26

    • F. Lendzian, B. Bönigk, M. Plato, K. Möbius, W. Lubitz
    Pages 89-97

  13. EPR and Endor Studies of the Primary Donor Cation Radical in Native and Genetically Modified Bacterial Reaction Centers

    • J. Rautter, Ch. Geßner, F. Lendzian, W. Lubitz, J. C. Williams, H. A. Murchison et al.
    Pages 99-108

  14. Molecular Orbital Study of Electronic Asymmetry in Primary Donors of Bacterial Reaction Centers

    • Martin Plato, Friedhelm Lendzian, Wolfgang Lubitz, Klaus Möbius
    Pages 109-118

  15. Near-Infrared-Excitation Resonance Raman Studies of Bacterial Reaction Centers

    • Vaithianathan Palaniappan, David F. Bocian
    Pages 119-126

  16. Asymmetric Structural Aspects of the Primary Donor in Several Photosynthetic Bacteria: the Near-IR Fourier Transform Raman Approach

    • T. A. Mattioli, B. Robert, M. Lutz
    Pages 127-132

  17. Rhodocyclus Gelatinosus Reaction Center: Characterization of the Quinones and Structure of the Primary Donor

    • Ileana Agalidis, Bruno Robert, Tony Mattioli, Françoise Reiss-Husson
    Pages 133-139

  18. FTIR Characterization of Leu M160→His, Leu L131→His and His L168→Phe Mutations Near the Primary Electron Donor in RB. Sphaeroides Reaction Centers

    • E. Nabedryk, J. Breton, J. Allen, H. Murchison, A. Taguchi, J. Williams et al.
    Pages 141-145

  19. FTIR Spectroscopy of The P+Q -A /PQA State in Met L248→Thr, Ser L244→Gly, Phe M197→Tyr, Tyr M210→Phe, Tyr M210→Leu, Phe L181—Tyr and Phe L181—Tyr M210→Tyr L181—Phe M210 Mutants of RB. Shaeroides

    • E. Nabedryk, J. Breton, J. Wachtveitl, K. A. Gray, D. Oesterhelt
    Pages 147-153

  20. Light-Induced Charge Separation in Photosynthetic Bacterial Reaction Centers Monitored by FTIR Difference Spectroscopy: the QA Vibrations

    • J. Breton, J.-R. Burie, C. Berthomieu, D. L. Thibodeau, S. Andrianambinintsoa, D. Dejonghe et al.
    Pages 155-162
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Keywords

About this book

The NATO Advanced Research Workshop entitled "The Photosynthetic Bacterial Reaction Center: Structure, Spectroscopy, and Dynamics" was held May 10-15, 1992, in the Maison d'H6tes of the Centre d'Etudes Nuc1eaires de Cadarache near Aix-en-Provence in the south of France. This workshop is the most recent of a string of meetings which started in Feldafing (Germany) in March 1985, soon after the three-dimensional structure of the bacterial reaction center had been elucidated by X-ray crystallography. This was followed, in September 1987, by a workshop in Cadarache and, in March 1990, by a second meeting in Feldafing. Although one of the most important processes on Earth, photosynthesis is still poorly understood. Stimulated by the breakthrough of solving the bacterial reaction center structure at atomic resolution, the field of relating this structure to the function of the reaction center, i. e. the remarkably efficient conversion and storage of solar energy, has been developing vigorously. Once the general organization of the cofactors and some details of the protein-cofactor interactions were known, it became possible to combine a variety of spectroscopic techniques with the powerful tool of site-directed mutagenesis in order to address increasingly incisive questions about the specific role of some amino acid residues in the electron transfer process. Still another promising tool is being developed, namely the exchange of a number of the native bacteriochlorophyll and bacteriopheophytin cofactors by chemically modified pigments.

Editors and Affiliations

  • CEN Saclay, Gif-sur-Yvette, France

    Jacques Breton

  • CEN Cadarache, France

    André Verméglio

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