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
. 1990 Aug;87(15):5930–5934. doi: 10.1073/pnas.87.15.5930

Photoreduction of NADP+ by isolated reaction centers of photosystem II: requirement for plastocyanin.

D I Arnon 1, J Barber 1
PMCID: PMC54443  PMID: 2198573

Abstract

The carrier of photosynthetically generated reducing power is the iron-sulfur protein ferredoxin, which provides directly, or via NADP+, reducing equivalents needed for CO2 assimilation and other metabolic reactions in the cell. It is now widely held that, in oxygenic photosynthesis, the generation of reduced ferredoxin-NADP+ requires the collaboration in series of two photosystems: photosystem II (PSII), which energizes electrons to an intermediate reducing potential and transfers them to photosystem I (PSI), which in turn is solely competent to energize electrons to the strong reducing potential required for the reduction of ferredoxin-NADP+ (the Z scheme). This investigation tested the premise of an alternative scheme, which envisions that PSII, without the involvement of PSI, is also capable of photoreducing ferredoxin-NADP+. We report here unexpected findings consistent with the alternative scheme. Isolated PSII reaction centers (completely free of PSI components), when supplemented with ferredoxin, ferredoxin-NADP+ oxidoreductase, and a PSII electron donor,1,5-diphenylcarbazide, gave a significant photoreduction of NADP+. A striking feature of this electron transfer from a PSII donor to the perceived terminal acceptor of PSI was its total dependence on catalytic quantities of plastocyanin, a copper-containing electron-transport protein hitherto known only as an electron donor to PSI.

Full text

PDF
5930

Images in this article

Selected References

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

  1. ARNON D. I., ALLEN M. B., WHATLEY F. R. Photosynthesis by isolated chloroplasts. Nature. 1954 Aug 28;174(4426):394–396. doi: 10.1038/174394a0. [DOI] [PubMed] [Google Scholar]
  2. Albertsson P. A., Hsu B. D., Tang G. M., Arnon D. I. Photosynthetic electron transport from water to NADP driven by photosystem II in inside-out chloroplast vesicles. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3971–3975. doi: 10.1073/pnas.80.13.3971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Arnon D. I., Tang G. M. Cytochrome b-559 and proton conductance in oxygenic photosynthesis. Proc Natl Acad Sci U S A. 1988 Dec;85(24):9524–9528. doi: 10.1073/pnas.85.24.9524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Arnon D. I. The discovery of ferredoxin: the photosynthetic path. Trends Biochem Sci. 1988 Jan;13(1):30–33. doi: 10.1016/0968-0004(88)90016-3. [DOI] [PubMed] [Google Scholar]
  5. Arnon D. I., Tsujimoto H. Y., Tang G. M. Proton transport in photooxidation of water: A new perspective on photosynthesis. Proc Natl Acad Sci U S A. 1981 May;78(5):2942–2946. doi: 10.1073/pnas.78.5.2942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bassi R., Simpson D. Chlorophyll-protein complexes of barley photosystem I. Eur J Biochem. 1987 Mar 2;163(2):221–230. doi: 10.1111/j.1432-1033.1987.tb10791.x. [DOI] [PubMed] [Google Scholar]
  7. Buchanan B. B., Arnon D. I. A reverse KREBS cycle in photosynthesis: consensus at last. Photosynth Res. 1990;24:47–53. [PubMed] [Google Scholar]
  8. Klimov V. V., Klevanik A. V., Shuvalov V. A., Kransnovsky A. A. Reduction of pheophytin in the primary light reaction of photosystem II. FEBS Lett. 1977 Oct 15;82(2):183–186. doi: 10.1016/0014-5793(77)80580-2. [DOI] [PubMed] [Google Scholar]
  9. Mitchell P. Keilin's respiratory chain concept and its chemiosmotic consequences. Science. 1979 Dec 7;206(4423):1148–1159. doi: 10.1126/science.388618. [DOI] [PubMed] [Google Scholar]
  10. Nanba O., Satoh K. Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559. Proc Natl Acad Sci U S A. 1987 Jan;84(1):109–112. doi: 10.1073/pnas.84.1.109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ramírez J. M., Campo F. F., Arnon D. I. Photosynthetic phosphorylation as energy source for protein synthesis and carbon dioxide assimilation by chloroplasts. Proc Natl Acad Sci U S A. 1968 Feb;59(2):606–612. doi: 10.1073/pnas.59.2.606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ramírez J. M., Del Campo F. F., Paneque A., Losada M. Ferredoxin-nitrite reductase from spinach. Biochim Biophys Acta. 1966 Apr 12;118(1):58–71. doi: 10.1016/s0926-6593(66)80144-3. [DOI] [PubMed] [Google Scholar]
  13. SHIN M., ARNON D. I. ENZYMIC MECHANISMS OF PYRIDINE NUCLEOTIDE REDUCTION IN CHLOROPLASTS. J Biol Chem. 1965 Mar;240:1405–1411. [PubMed] [Google Scholar]
  14. Schmidt A., Trebst A. The mechanism of photosynthetic sulfate reduction by isolated chloroplasts. Biochim Biophys Acta. 1969 Aug 5;180(3):529–535. doi: 10.1016/0005-2728(69)90031-0. [DOI] [PubMed] [Google Scholar]
  15. Schürmann P., Buchanan B. B., Arnon D. I. Role of cyclic photophosphorylation in photosynthetic carbon dioxide assimilation by isolated chloroplasts. Biochim Biophys Acta. 1972 Apr 20;267(1):111–124. doi: 10.1016/0005-2728(72)90143-0. [DOI] [PubMed] [Google Scholar]
  16. TAGAWA K., ARNON D. I. Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature. 1962 Aug 11;195:537–543. doi: 10.1038/195537a0. [DOI] [PubMed] [Google Scholar]
  17. TAGAWA K., TSUJIMOTO H. Y., ARNON D. I. Role of chloroplast ferredoxin in the energy conversion process of photosynthesis. Proc Natl Acad Sci U S A. 1963 Apr;49:567–572. doi: 10.1073/pnas.49.4.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Vernon L. P., Shaw E. R. Photoreduction of 2,6-dichlorophenolindophenol by diphenylcarbazide: a photosystem 2 reaction catalyzed by tris-washed chloroplasts and subchloroplast fragments. Plant Physiol. 1969 Nov;44(11):1645–1649. doi: 10.1104/pp.44.11.1645. [DOI] [PMC free article] [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