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Limited Proteolysis and Its Influence on Thermal Stability of the Photosynthetic Reaction Center from Chloroflexus aurantiacus

  • Michail A. Kutuzov
  • Nellie B. Levina
  • Najmoutin G. Abdulaev
  • Alexander S. Zolotarev
Part of the FEMS Symposium book series (FEMSS)

Summary

Limited proteolysis with proteases of different specificity has been used to obtain a number of preparations of the reaction center (RC) from the thermophilic green bacterium Chloroflexus aurantiacus. The absorption spectrum of the native RC are preserved in these preparations, even after the shortening of the N-termini of both RC subunits to different extent. Considerable part of the hydrophilic N-terminus of the L-subunit has been shown to be unaccessible to the proteases. AlaL3-ArgL25 region contribute to the thermal stability of the Chloroflexus RC.

Keywords

Purple Bacterium Limited Proteolysis Phototrophic Bacterium Photosynthetic Reaction Center Primary Charge Separation 
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. 1.
    C. R. Woese, Bacterial evolution, Microbiol. rev. 5I: 22 I (1987)Google Scholar
  2. 2.
    B. K. Pierson, J. P. Thornber, and R. E. B. Seftor, Partial purification, subunit structure and thermal stability of the photochemical reaction center of the thermophilic green bacterium Chloroflaxus aurantiacus, Biochim. Biophys. Acta 723: 322 (1983)CrossRefGoogle Scholar
  3. 3.
    Yu. A. Ovchinnikov, N. G. Abdulaev, A. S. Zolotarev, B. E. Shmukler, A. A. Zargarov, M. A. Kutuzov, I. N. Telezhinskaya, and N. B. Levina, Photosynthetic reaction centre of ChZoroflexus aurantiacus. I. Primary structure of L-subunit, FEBS Lett. 231: 237 (1988)PubMedCrossRefGoogle Scholar
  4. 4.
    Yu. A. Ovchinnikov, N. G. Abdulaev, B. E. Shmuckler, A. A. Zargarov, M. A. Kutuzov, I. N. Telezhinskaya, N. B. Levine, and A. S. Zolotarev, Photosynthetic reaction centre of ChZoroflexus aurantiacus. Primary structure of M-subunit, FEBS Lett. 232: 364 (1988)PubMedCrossRefGoogle Scholar
  5. 5.
    J. A. Shiozawa, F. Lottspeich, D. Oesterhelt, and R. Feick, The primary structure of the Chioroflexus aurantiacus reaction-center polypeptides, Eur. J. Biochem. Ï80: 75 (1989)Google Scholar
  6. 6.
    M. D. Mamedov, N. I. Zacharova, A. A. Kondrashin, and A. Yu. Semenov, The effect of o-phenanthroline on electrogenesis under primary charge separation in the reaction center of Rhodopseudomonas sphaeroides, Biol. Membrany (Russ) 3: 513 (1986)Google Scholar
  7. 7.
    B. Schobert, J. K. Lanyi, and D. Oesterhelt, Structure and orientation of halorhodopsin in the membrane: a proteolytic fragmentation study, EMBO J. 7: 905 (1988)PubMedGoogle Scholar
  8. 8.
    D. J. Merkler, C. K. Farrington, and F. C. Wedler, Protein thermostability, Int. J. Pept. Protein Res. 18: 430 (1981)PubMedCrossRefGoogle Scholar
  9. 9.
    F. S. Qaw and J. M. Brewer, Arginyl residues and thermal stability of proteins, Mol. Cell. Biochem. 71: 121 (1986)CrossRefGoogle Scholar
  10. 10.
    M. F. Perutz and H. Ridt, Stereochemical bases of heat stability in bacterial ferredoxins and hemoglobin A2, Nature 255: 256 (1975).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Michail A. Kutuzov
    • 1
  • Nellie B. Levina
    • 1
  • Najmoutin G. Abdulaev
    • 1
  • Alexander S. Zolotarev
    • 1
  1. 1.Shemyakin Institute of Bioorganic ChemistryUSSR Academy of SciencesMoscowUSSR

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