Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Mar 1;90(5):1834–1838. doi: 10.1073/pnas.90.5.1834

Oxygen evolution in photosynthesis: from unicycle to bicycle.

V P Shinkarev 1, C A Wraight 1
PMCID: PMC45974  PMID: 11607372

Abstract

Flash-induced oxygen evolution in the thylakoids of plants and algae exhibits damped oscillations with period four. These are well described by the S-state model of Kok et al. [Kok, B., Forbush, B. & McGloin, M. (1970) Photochem. Photobiol. 11, 457-475], with damping provided by empirical misses and double hits in the reaction center of photosystem II. Here we apply a mechanistic interpretation of misses as mainly determined by reaction centers that are inactive at the time of the flash due to the presence of either P+ or QA, according to the electron transfer equilibria on the donor and acceptor sides of the reaction center. Calculation of misses on this basis, using known or estimated values of the equilibrium constants for electron transfer between the S states and tyrosine Yz, between Yz and P680, as well as between the acceptor plastoquinones, allows a natural description of the flash number dependence of oxygen evolution. The calculated misses are different for each flash-induced reaction center transition. Identification of this mechanism underlying the miss factor for each transition leads to the recognition of two different reaction sequence cycles of photosystem II, with different transition probabilities, producing an intrinsic heterogeneity of photosystem II activity.

Full text

PDF
1834

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bouges-Bocquet B. Kinetic models for the electron donors of photosystem II of photosynthesis. Biochim Biophys Acta. 1980 Dec;594(2-3):85–103. doi: 10.1016/0304-4173(80)90006-3. [DOI] [PubMed] [Google Scholar]
  2. Buser C. A., Thompson L. K., Diner B. A., Brudvig G. W. Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry. 1990 Sep 25;29(38):8977–8985. doi: 10.1021/bi00490a014. [DOI] [PubMed] [Google Scholar]
  3. Debus R. J., Barry B. A., Babcock G. T., McIntosh L. Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system. Proc Natl Acad Sci U S A. 1988 Jan;85(2):427–430. doi: 10.1073/pnas.85.2.427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Debus R. J., Barry B. A., Sithole I., Babcock G. T., McIntosh L. Directed mutagenesis indicates that the donor to P+680 in photosystem II is tyrosine-161 of the D1 polypeptide. Biochemistry. 1988 Dec 27;27(26):9071–9074. doi: 10.1021/bi00426a001. [DOI] [PubMed] [Google Scholar]
  5. Jursinic P. Investigation of double turnovers in photosystem II charge separation and oxygen evolution with excitation flashes of different duration. Biochim Biophys Acta. 1981 Mar 12;635(1):38–52. doi: 10.1016/0005-2728(81)90005-0. [DOI] [PubMed] [Google Scholar]
  6. Kok B., Forbush B., McGloin M. Cooperation of charges in photosynthetic O2 evolution-I. A linear four step mechanism. Photochem Photobiol. 1970 Jun;11(6):457–475. doi: 10.1111/j.1751-1097.1970.tb06017.x. [DOI] [PubMed] [Google Scholar]
  7. Metz J. G., Nixon P. J., Rögner M., Brudvig G. W., Diner B. A. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry. 1989 Aug 22;28(17):6960–6969. doi: 10.1021/bi00443a028. [DOI] [PubMed] [Google Scholar]
  8. Vermass W. F., Rutherford A. W., Hansson O. Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Donor D is a tyrosine residue in the D2 protein. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8477–8481. doi: 10.1073/pnas.85.22.8477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Zankel K. L. Rapid fluorescence changes observed in chloroplasts: their relationship to the O2 evolving system. Biochim Biophys Acta. 1973 Oct 19;325(1):138–148. doi: 10.1016/0005-2728(73)90159-x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES