Quantitative Analysis of Genetically Altered Reaction Centers Using an In Vitro Cytochrome Oxidation Assay

  • Edward J. Bylina
  • Raffael Jovine
  • Douglas C. Youvan
Part of the NATO ASI Series book series (NSSA, volume 149)


In the analysis of complex phenomena such as the biogenesis or photochemical function of reaction center proteins, the approach of a geneticist is to generate and characterize a large number of mutants affecting specific steps in the process. In some analyses, spontaneous mutants which possess selectable characteristics may be informative. For example, the role of specific amino acid residues in herbicide and quinone binding can be deduced from the analysis of spontaneous herbicide resistant mutants. However, the analysis of spontaneous mutations as a general approach to study structure-function relationships has serious limitations. Many mutations have phenotypes which possess unselectable characteristics. With the determination of the structure of the reaction center1, this class of mutations can be generated by replacing important amino acid residues adjacent to chromophores throughout the protein by site-directed mutagenesis.


Reaction Center Reaction Center Protein Flash Intensity Relative Light Intensity Multiple Photon 
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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  1. 1.
    J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel, Nature 318, 618–624 (1985).PubMedCrossRefGoogle Scholar
  2. H. Michel, O. Epp, and J. Deisenhofer, EMBO J. 5, 2445–2451 (1986).PubMedGoogle Scholar
  3. 2 E.J. Bylina and D.C. Youvan, Z. Naturforsch. 42c, 769-774 (1987).Google Scholar
  4. 3. E.J. Bylina and D.C Youvan, in preparation.Google Scholar
  5. 4. for reviews, see M.E. Michel-Beyerle, Ed., Antennas and Reaction Centers of Photosynthetic Bacteria-Structure, Interaction and Dynamics, Springer, Berlin, 1985.; W.W. Parson and B. Ke, in Photosynthesis (Govindjee, Ed.), Vol. I, 331-385, Academic Press, New York, 1982.Google Scholar
  6. 5.
    M.Y. Okamura, R.J. Debus, D. Kleinfeld, and G. Feher, in Function of Quinones in Energy Conserving Systems (B.L. Trumpower, Ed.), 299–317, Academic Press, New York, 1982.Google Scholar
  7. 6.
    M.L. Paddock, J.C. Williams, S.H. Rongey, E.C. Abresch, G. Feher, and M.Y. Okamura, in Progress in Photosynthesis Research (J. Biggins, Ed.), Vol III, 775–778, Martinus Nijhoff, Dordrecht 1987.Google Scholar
  8. 7.
    R.C. Prince and D.C. Youvan, Biochim. Biophys. Acta 890, 286–291 (1987).CrossRefGoogle Scholar
  9. 8.
    D.C Youvan, S. Ismail, and E.J. Bylina, Gene 38, 19–30 (1985).PubMedCrossRefGoogle Scholar
  10. 9.
    H.-C. Yen and B. Marrs, Arch. Biochem. and Biophys. 181, 411–418 (1977).CrossRefGoogle Scholar
  11. 10.
    D.C. Youvan, E.D. Lickerman, and M.M. Yang, Photonics Spectra 21, 109–110 (1987).Google Scholar
  12. 11.
    D.F. Bocian, N.J. Boldt, B.W. Chadwick, and H.A. Frank, FEBS Lett. 214, 92–96 (1987).PubMedCrossRefGoogle Scholar
  13. 12. R. Jovine and D.C. Youvan, in preparation.Google Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Edward J. Bylina
    • 1
  • Raffael Jovine
    • 1
  • Douglas C. Youvan
    • 1
  1. 1.Department of Applied Biological SciencesMassachusetts Institute of TechnologyCambridgeUSA

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