Abstract

Based on different lines of experimental evidence a special protein matrix containing at least two polypeptides (referred to as D-1 and D-2) was inferred to play a key role for the electron transport at the PS II acceptor side and its blockage by a number of herbicides. The lysine free polypeptide D-1 which exhibits remarkable structural homologies and functional analogies with the L-subunit of the reaction center complex of purple bacteria very likely contains the binding site for the secondary plastoquinone Qb and many PS II herbicides (for recent review see ref. 1) . Experiments with a lysine-specific protease led to the conclusion that allosteric modifications affect electron transport and herbicide binding (2). Recently lipids were shown to be of functional relevance for PS II electron transport (3). Accordingly detergent treatment of thylakoids for preChapaution of PS II particles might also give rise to changes of the structural and functional pattern of PS II. Here this problem is attacked by comChapautive studies of electron transport and the modifications of atrazine binding by specific proteases and K3 [Fe(CN)6] in thylakoids and PS II particles, respectively.

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