Photosynthesis Research

, Volume 9, Issue 1–2, pp 3–12 | Cite as

Molecular arrangement of pigment-protein complex of photosystem 1

  • V. V. Shubin
  • N. V. Karapetyan
  • A. A. Krasnovsky


The circular dichroism (CD) method was applied to study the molecular organization of P700, antenna chlorophyll and protein of photosystem 1 complexes (CP1), isolated from chloroplasts under mild treatment with Triton X-100. Analysis of CD spectra and protein: chlorophyll: P700 ratios for CP1 complexes that were different in their chlorophyll content indicate that CP1 preparations can be considered as a mixture of CP1-RC, containing P700 (10–20%), and CP1-LH without P700 (80–90%). Both types of complexes contain approximately 25 chlorophyll molecules, and the destruction of their spatial organization with detergents represents a cooperative transition. The rate of chlorophyll destruction in CP1-LH is much higher than that in CP1-RC. In both complexes a 65 kDa polypeptide predominates, whose secondary structure (typical for α/β proteins) is stable to Triton X-100 and does not depends on the chlorophyll content. Chlorophyll seems to be grouped in clusters (5–7 molecules) in the hydrophobic cores of 2–3 parallel α/β domains of the 65 kDa protein. Only one of the clusters in CP1-RC includes P700; on P700 photooxidation the change of its interaction with the nearest pigment environment results in a complicated shape of the light-induced CD spectra.

Key words

light-harvesting complex (pea) cPII optical absorption linear dichroism chroism protein secondary structure 



photosystem 1


pigment-protein complex of PS1


chlorophyll a


CP1 with ratio Ch1:P700 140


reaction center


light-harvesting pigment


CP1, containing P700


CP1 without P700 (containing LH)


circular dichroism


sodium dodecyl sulfate


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Anderson JM (1980) Biochim Biophys Acta 591:113–126Google Scholar
  2. 2.
    Bengis C and Nelson N (1977) J Biol Chem 252:4564–4569Google Scholar
  3. 3.
    Bolotina IA, Chekhov VO, Lugauskas VYu and Ptitsyn OB (1980) Mol Biol (USSR) 14:902–909Google Scholar
  4. 4.
    Bolotina IA, Chekhov VO, Lugauskas VYu and Ptitsyn OB (1981) Mol Biol (USSR) 15:167–175Google Scholar
  5. 5.
    Duysens LNM (1952) Doctoral thesis, University of UtrechtGoogle Scholar
  6. 6.
    Hiyama T and Ke B (1972) Biochim Biophys Acta 261:160–172Google Scholar
  7. 7.
    Ikegami I and Ke B (1984) Biochim Biophys Acta 764:70–79Google Scholar
  8. 8.
    Karapetyan NV, Litvin FF and Krasnovsky AA (1963) Biofizika (USSR) 8:191–200Google Scholar
  9. 9.
    Karapetyan NV, Shubin VV, Rakhimberdieva MG, Vashchenko RG and Bolychevtseva YuV (1984) FEBS Lett 173:209–212Google Scholar
  10. 10.
    Krasnovksy AA, Kosobutskaya LM and Voinovskaya KK (1953) DAN USSR 92: 1201–1204Google Scholar
  11. 11.
    Mullet JR, Burke JJ and Arntzen CJ (1980) Plant Physiol 65:814–822Google Scholar
  12. 12.
    Nabedryk E, Biaudet P, Darr S, Arntzen CJ and Breton J (1984) Biochim Biophys Acta 767:640–647Google Scholar
  13. 13.
    Philipson KD, Sato VL and Sauer K (1972) Biochemistry 11:4591–4595Google Scholar
  14. 14.
    Richardson JS (1981) In: Anfinsen CB, Edsall JT and Richards PM (eds) Advances in protein chemistry, pp. 167–337. New York: Academic PressGoogle Scholar
  15. 15.
    Scops RK (1974) Anal Biochem 59:277–282Google Scholar
  16. 16.
    Shiozawa JA, Alberte RS and Thornber JF (1974) Arch Biochem Biophys 165: 388–397Google Scholar
  17. 17.
    Shubin VV, Efimovskaya TV and Karapetyan NV (1981) J Phys Chem (USSR) 55: 2916–2921Google Scholar
  18. 18.
    Shubin VV, Vaschenko RG and Karapetyan NV (1985) Mol Biol (USSR) 19: 841–850Google Scholar
  19. 19.
    Thornber JP (1975) Annu Rev Plant Physiol 26:127–158Google Scholar
  20. 20.
    Vierling E and Alberte RS (1983) Plant Physiol 72:625–633Google Scholar

Copyright information

© Martinus Nijhoff/Dr. W. Junk Publishers 1986

Authors and Affiliations

  • V. V. Shubin
    • 1
  • N. V. Karapetyan
    • 1
  • A. A. Krasnovsky
    • 1
  1. 1.A.N. Bakh Institute of BiochemistryUSSR Academy of SciencesMoscowUSSR

Personalised recommendations