Dynamics in Photo system II Structure and Function
15
level. A primary event in the effect of excess light on the PS II will lead to
the modification of the Dl protein followed by its cleavage, and then
to complete degradation of the Dl protein. This light-dependent process
appears to be enhanced under stress conditions like in forest decline. When
the light-dependent repair system that specifically synthesizes the Dl protein
is no longer compensating the light degradation, photosystem II is quickly
fully inactivated. Phosphorylation of the reaction center polypeptides of PS
II may play an important role in regulation of PS II turnover.
Acknowledgment. Work at Bochum was supported by the Deutsche Forschungsgemeinschaft.
References
Allen JF (1992) Protein phosphorylation in regulation of photosynthesis. Biochim Biophys
Acta 1098: 275-335
Allen JP, Feher G, Yeates TO, Komiya H, Rees DC (1987) Structure of the reaction
center from Rhodobacter sphaeroides R-26: The cofactors. Proc Natl Acad Sci USA 84:
5730-5734
Aro EM, Kettunen R, Tyystjarvi E (1992) ATP and light regulate Dl protein
modification and degradation. FEBS Letters 297: 29-33
Barber J (1987) Photosynthetic reaction centres: a common link. Trends Biochem Sci 12:
321-236
Barber J (ed) (1992) The photosystems: structure, function and molecular biology. Topics
in photosynthesis, vol 11. Elsevier, Amsterdam
Barber J, Andersson B (1992) Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci 17: 61-66
Blankenship RE (1992) Origin and early evolution of photosynthesis. Photosynth Res 33:
91-111
Debus RJ, Barry BA, Babcock GT, McIntosh L (1988) Directed mutagenesis indicates
that the donor to P+ 680 in photosystem II is tyrosine-161 of the Dl polypeptide.
Biochemistry 27: 9071-9074
Deisenhofer J, Michel H (1989) Das photosynthetische Reaktionszentrum des Pupurbakteriums Rhodopseudomonas viridis. Angew Chern 101: 872-892
Deisenhofer J, Epp 0, Miki K, Huber R, Michel H (1985) Structure of the protein
subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A
resolution. Nature 318: 618-624
Demmig-Adams B, Adams WW (1992) Photoprotection and other responses of plants to
high light stress. Annu Rev Physiol Plant Mol Bioi 43: 599-626
Draber W, Kluth JF, Tietjen K, Trebst A (1991) Herbicides in photosynthesis research.
Angew Chern Int Ed Engl 30: 1621-1633
Draber W, Hilp U, Likusa K, Trebst A (1993) Inhibition of photosynthesis by 4-nitro-6alkylphenols: structure-activity studies in wildtype and five mutants of Chlamydomonas
reinhardtii thylakoids. Z Naturforsch 48c: 308-318
Elich TO, Edelman M, Mattoo AK (1992) Identification, characterization, and resolution
of the in vivo phosphorylated form of the Dl photosystem II reaction center protein. J
Bioi Chern 267: 3523-3529
Gal A, Hauska G, Herrmann R, Ohad I (1990) Interaction between light harvesting
chlorophyll-alb protein (LHC II) kinase and cytochrome b6/f complex. J Bioi Chern
265: 19749-19749
15
level. A primary event in the effect of excess light on the PS II will lead to
the modification of the Dl protein followed by its cleavage, and then
to complete degradation of the Dl protein. This light-dependent process
appears to be enhanced under stress conditions like in forest decline. When
the light-dependent repair system that specifically synthesizes the Dl protein
is no longer compensating the light degradation, photosystem II is quickly
fully inactivated. Phosphorylation of the reaction center polypeptides of PS
II may play an important role in regulation of PS II turnover.
Acknowledgment. Work at Bochum was supported by the Deutsche Forschungsgemeinschaft.
References
Allen JF (1992) Protein phosphorylation in regulation of photosynthesis. Biochim Biophys
Acta 1098: 275-335
Allen JP, Feher G, Yeates TO, Komiya H, Rees DC (1987) Structure of the reaction
center from Rhodobacter sphaeroides R-26: The cofactors. Proc Natl Acad Sci USA 84:
5730-5734
Aro EM, Kettunen R, Tyystjarvi E (1992) ATP and light regulate Dl protein
modification and degradation. FEBS Letters 297: 29-33
Barber J (1987) Photosynthetic reaction centres: a common link. Trends Biochem Sci 12:
321-236
Barber J (ed) (1992) The photosystems: structure, function and molecular biology. Topics
in photosynthesis, vol 11. Elsevier, Amsterdam
Barber J, Andersson B (1992) Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci 17: 61-66
Blankenship RE (1992) Origin and early evolution of photosynthesis. Photosynth Res 33:
91-111
Debus RJ, Barry BA, Babcock GT, McIntosh L (1988) Directed mutagenesis indicates
that the donor to P+ 680 in photosystem II is tyrosine-161 of the Dl polypeptide.
Biochemistry 27: 9071-9074
Deisenhofer J, Michel H (1989) Das photosynthetische Reaktionszentrum des Pupurbakteriums Rhodopseudomonas viridis. Angew Chern 101: 872-892
Deisenhofer J, Epp 0, Miki K, Huber R, Michel H (1985) Structure of the protein
subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A
resolution. Nature 318: 618-624
Demmig-Adams B, Adams WW (1992) Photoprotection and other responses of plants to
high light stress. Annu Rev Physiol Plant Mol Bioi 43: 599-626
Draber W, Kluth JF, Tietjen K, Trebst A (1991) Herbicides in photosynthesis research.
Angew Chern Int Ed Engl 30: 1621-1633
Draber W, Hilp U, Likusa K, Trebst A (1993) Inhibition of photosynthesis by 4-nitro-6alkylphenols: structure-activity studies in wildtype and five mutants of Chlamydomonas
reinhardtii thylakoids. Z Naturforsch 48c: 308-318
Elich TO, Edelman M, Mattoo AK (1992) Identification, characterization, and resolution
of the in vivo phosphorylated form of the Dl photosystem II reaction center protein. J
Bioi Chern 267: 3523-3529
Gal A, Hauska G, Herrmann R, Ohad I (1990) Interaction between light harvesting
chlorophyll-alb protein (LHC II) kinase and cytochrome b6/f complex. J Bioi Chern
265: 19749-19749