Single Crystals of the Photochemical Reaction Center from Rhodobacter sphaeroides Wild Type Strain 2.4.1 Analyzed by Polarized Light

  • Harry A. Frank
  • Shahriar S. Taremi
  • James R. Knox
  • Werner Mäntele
Chapter
Part of the NATO ASI Series book series (NSSA, volume 149)

Abstract

The crystal structures of the reaction centers from the carotenoidless mutant Rb. sphaeroides R26 and from Rps. viridis, have provided the means to explore the relationships between the structures of the chromophores and their spectroscopic properties (Deisenhofer et al., 1985; Allen et al., 1986; Chang et al., 1986). Prompted by the fact that one specific relationship, that between the carotenoid molecule and its various spectroscopic properties has not been fully elucidated by the existing structures, we set out to crystallize and study the reaction center protein from Rb. sphaeroides 2.4.1. The abundance of biochemical, spectroscopic and dynamics information previously obtained (Cogdell et al., 1976; Parson & Monger, 1976; Lutz et al., 1978; Vermeglio et al., 1978; McGann & Frank, 1985; Chadwick & Frank, 1986; Gagliano et al., 1986) for this particular bacterial strain and its associated carotenoid, spheroidene, makes the elucidation of the structure of this reaction center complex of particular importance.

Keywords

Reaction Center Wild Type Strain Primary Donor Transition Moment Crystal Axis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Allen, J. P., Feher, G., Yeates, T. O., Rees, D. C, Deisenhofer, J., Michel, H. & Huber, R. (1986) Proc. Nat. Acad. Sci. USA. 83, 8589–8593.PubMedCrossRefGoogle Scholar
  2. Chadwick, B. & Frank, H. A. (1986) Biochim. Biophys. Acta 851, 257–266.CrossRefGoogle Scholar
  3. Chang, C.-H., Tiede, G., Tang, J., Smith, U., Norris, J. & Schiffer, M. (1986) FEBS Letters 205, 82–86.PubMedCrossRefGoogle Scholar
  4. Cogdell, R. J., Parson, W. W. & Kerr, M. A. (1976) Biochim. Biophys. Acta 430, 83–93.PubMedCrossRefGoogle Scholar
  5. Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1985) Nature 318, 618–624.PubMedCrossRefGoogle Scholar
  6. Ditson, S. L., Davis, R. C. & Pearlstein, R. M. (1984) Biochim. Biophys. Acta 766, 623–629.CrossRefGoogle Scholar
  7. Frank, H. A., Taremi, S. S. & Knox, J. R. (1987) J. Mol. Biol. 197, in press.Google Scholar
  8. Gagliano, A. G., Breton, J. & Geacintov, N. E. (1986) Photobiochem. Photobiophys. 10, 213–221.Google Scholar
  9. Krinsky, N.I. (1971) In Carotenoids (Isler, O., Gutmann, H. & Solms, U., eds), pp. 48-51, Birkhauser, Basel.Google Scholar
  10. Lutz, M., Agalidis, I., Hervo, G., Cogdell, R. J. & Reiss-Husson, F. (1978) Biochim. Biophys. Acta 503, 287–303.PubMedCrossRefGoogle Scholar
  11. Maroti, P., Kirmaier, C., Wraight, C., Holten, D. & Pearlstein, R. M. (1985) Biochim. Biophys. Acta 810, 132–139.CrossRefGoogle Scholar
  12. McGann, W. J. & Frank, H. A. (1985) Biochim. Biophys. Acta 807, 101–109.CrossRefGoogle Scholar
  13. Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 5, 2445–2451.PubMedGoogle Scholar
  14. Parson, W.W. & Monger, T.G. (1976) Brookhaven Symp. Biol 28, 196–212.Google Scholar
  15. Vermeglio, A., Breton, J., Paillotin, G. & Cogdell, R. (1978) Biochim. Biophys. Acta 501, 514–530.PubMedCrossRefGoogle Scholar
  16. Vermeglio, A. & Clayton, R. K. (1976) Biochim. Biophys. Acta 449, 500–515.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Harry A. Frank
    • 1
  • Shahriar S. Taremi
    • 1
  • James R. Knox
    • 2
  • Werner Mäntele
    • 3
  1. 1.Departments of ChemistryUniversity of ConnecticutStorrsUSA
  2. 2.Molecular and Cell BiologyUniversity of ConnecticutStorrsUSA
  3. 3.Institut für Biophysik und StrahlenbiologieFreiburgGermany

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