The sensitivity of Photosystem II to damage by UV-B radiation depends on the oxidation state of the water-splitting complex.
The water-oxidizing complex of Photosystem II is an important target of ultraviolet-B (280-320 nm) radiation, but the mechanistic background of the UV-B induced damage is not well understood. Here we studied the UV-B sensitivity of Photosystem II in different oxidation states, called S-states of the water-oxidizing complex. Photosystem II centers of isolated spinach thylakoids were synchronized to different distributions of the S(0), S(1), S(2) and S(3) states by using packages of visible light flashes and were exposed to UV-B flashes from an excimer laser (lambda=308 nm). The loss of oxygen evolving activity showed that the extent of UV-B damage is S-state-dependent. Analysis of the data obtained from different synchronizing flash protocols indicated that the UV-sensitivity of Photosystem II is significantly higher in the S(3) and S(2) states than in the S(1) and S(0) states. The data are discussed in terms of a model where UV-B-induced inhibition of water oxidation is caused either by direct absorption within the catalytic manganese cluster or by damaging intermediates of the water oxidation process.
Szilárd
András
A
Institute of Plant Biology, Biological Research Center of the Hungarian Academy of Sciences, P.O. Box 521, H-6701 Szeged, Hungary.
Sass
László
L
Deák
Zsuzsanna
Z
Vass
Imre
I
D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism / Q000528:radiation effects*; D045332:Photosystem II Protein Complex / Q000378:metabolism / Q000528:radiation effects*; D018724:Spinacia oleracea / Q000737:chemistry; D020524:Thylakoids / Q000737:chemistry; D014466:Ultraviolet Rays; D014867:Water / Q000378:metabolism*
D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D014867:Water