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. 1990 Dec;87(23):9295–9299. doi: 10.1073/pnas.87.23.9295

Evidence for a biological role in photosynthesis for cytochrome b-559--a component of photosystem II reaction center.

O Canaani 1, M Havaux 1
PMCID: PMC55151  PMID: 11607120

Abstract

Absorbance changes in untreated intact leaf discs, produced upon excitation with high-intensity red light, were shown to be due to the photooxidation of cytochrome b-559. At low intensities (<100 W/m2), photooxidation was almost undetectable. Photooxidation occurred with a half-time of 4.3 sec and an extent of 0.64 mol of cytochrome per 320 mol of chlorophyll. Upon transition to darkness, an additional oxidation occurred that exhibited faster kinetics (t/12 < 100 msec) and 0.32 mol of cytochrome was oxidized per 320 mol of chlorophyll. Photooxidation was inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea and was specifically induced by red light since far-red light did not cause any absorbance decrease. These results suggest that the redox changes of cytochrome b-559 are driven by photosystem II. Photooxidation was increased by 67% and its initial rate was doubled upon incubation of the leaf in carbonylcyanide p-trifluoromethoxy-phenylhydrazone. Exposure of the leaf to mild water stress or mild heat stress resulted in an increase in the extent of photooxidation and in a 6-fold decrease in the rate constant. Mild heat stress also induced a large increase of the rate constant for the dark reduction of the cytochrome. The dependence of photooxidation on high-intensity red light, its inhibition criteria, the fast transient dark oxidation, and enhancement of both photooxidation and dark transient oxidation by treatments that affect Z, the primary donor to P680, indicate that cytochrome b-559 in vivo is involved in cyclic electron flow around photosystem II. Its primary role in photosynthesis is to divert excess photons from a linear to a cyclic electron flow at high light intensities for protection of the D1 and D2 proteins against photodamage. Dark oxidation of the cytochrome is suggested to reflect a second role, that of deactivation of the powerful oxidant Z+ in the dark.

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Selected References

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

  1. Anderson J. M., Nyunt T., Boardman N. K. Light-induced redox changes of cytochrome b-559. Arch Biochem Biophys. 1973 Apr;155(2):436–444. doi: 10.1016/0003-9861(73)90134-3. [DOI] [PubMed] [Google Scholar]
  2. Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [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. Ben-Hayyim G. Light-induced absorbance changes of the high-potential cytochrome b559 in chloroplasts. Eur J Biochem. 1974 Jan 3;41(1):191–196. doi: 10.1111/j.1432-1033.1974.tb03259.x. [DOI] [PubMed] [Google Scholar]
  5. Briantais J. M., Vernotte C., Picaud M., Krause G. H. A quantitative study of the slow decline of chlorophyll a fluorescence in isolated chloroplasts. Biochim Biophys Acta. 1979 Oct 10;548(1):128–138. doi: 10.1016/0005-2728(79)90193-2. [DOI] [PubMed] [Google Scholar]
  6. Canaani O., Malkin S., Mauzerall D. Pulsed photoacoustic detection of flash-induced oxygen evolution from intact leaves and its oscillations. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4725–4729. doi: 10.1073/pnas.85.13.4725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Falkowski P. G., Fujita Y., Ley A., Mauzerall D. Evidence for Cyclic Electron Flow around Photosystem II in Chlorella pyrenoidosa. Plant Physiol. 1986 May;81(1):310–312. doi: 10.1104/pp.81.1.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Havaux M., Canaani O., Malkin S. Photosynthetic responses of leaves to water stress, expressed by photoacoustics and related methods : I. Probing the photoacoustic method as an indicator for water stress in vivo. Plant Physiol. 1986 Nov;82(3):827–833. doi: 10.1104/pp.82.3.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Heber U., Boardman N. K., Anderson J. M. Cytochrome b-563 redox changes in intact CO-fixing spinach chloroplasts and in developing pea chloroplasts. Biochim Biophys Acta. 1976 Feb 16;423(2):275–292. doi: 10.1016/0005-2728(76)90185-7. [DOI] [PubMed] [Google Scholar]
  10. Heber U., Kirk M. R., Boardman N. K. Photoreactions of Cytochrome b-559 and cyclic electron flow in photosystem II of intact chloroplasts. Biochim Biophys Acta. 1979 May 9;546(2):292–306. doi: 10.1016/0005-2728(79)90047-1. [DOI] [PubMed] [Google Scholar]
  11. Hiller R. G., Anderson J. M., Boardman N. K. Photooxidation of cytochrome b-559 in leaves and chloroplasts at room temperature. Biochim Biophys Acta. 1971 Sep 7;245(2):439–452. doi: 10.1016/0005-2728(71)90161-7. [DOI] [PubMed] [Google Scholar]
  12. Knaff D. B., Arnon D. I. LIGHT-INDUCED OXIDATION OF A CHLOROPLAST B-TYPE CYTOCHROME AT -189 degrees C. Proc Natl Acad Sci U S A. 1969 Jul;63(3):956–962. doi: 10.1073/pnas.63.3.956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Pakrasi H. B., Diner B. A., Williams JGK., Arntzen C. J. Deletion Mutagenesis of the Cytochrome b559 Protein Inactivates the Reaction Center of Photosystem II. Plant Cell. 1989 Jun;1(6):591–597. doi: 10.1105/tpc.1.6.591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tae G. S., Black M. T., Cramer W. A., Vallon O., Bogorad L. Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product. Biochemistry. 1988 Dec 27;27(26):9075–9080. doi: 10.1021/bi00426a002. [DOI] [PubMed] [Google Scholar]
  16. Thompson L. K., Brudvig G. W. Cytochrome b-559 may function to protect photosystem II from photoinhibition. Biochemistry. 1988 Sep 6;27(18):6653–6658. doi: 10.1021/bi00418a002. [DOI] [PubMed] [Google Scholar]
  17. Whitmarsh J., Cramer W. A. A pathway for the reduction of cytochrome b-559 by photosystem II in chloroplasts. Biochim Biophys Acta. 1978 Jan 11;501(1):83–93. doi: 10.1016/0005-2728(78)90097-x. [DOI] [PubMed] [Google Scholar]

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