Degradation of the D1 protein of photosystem-II reaction centre by ultraviolet-B radiation requires the presence of functional manganese on the donor side.

The in vivo effects of ultraviolet-B radiation (280-320 nm) on photosystem-II activity and degradation of the D1 protein are investigated and compared with the in vitro results on isolated thylakoids and other detergent-extracted photosystem-II preparations. A cleavage site in the second transmembrane segment of the D1 protein, giving rise to a 20-kDa C-terminal and a 13-kDa N-terminal fragment pair, is detected after irradiation of entire leaves as well as in all photosystem-II preparations, irrespective of their actual ability to evolve oxygen but depending on the presence of Mn ions associated with the water-splitting system. Damage to the plastoquinone moiety, observed by other authors, is confirmed and is proposed to be responsible for the impairment of electron-transport activity, but not for the observed cleavage of the D1 protein.