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Based on the functional organization scheme of system-II-electron transport and its modification by different procedures a proteinaceous component enwrapping the redox components (plastoquinone molecules) of the acceptor side (thereby acting as regulatory element) is inferred to be the unique target for herbicidal interaction with system II. This proteinaceous component, which is attacked by trypsin, provides the receptor sites for the herbicides. Studies of the release kinetics in trypsinated chloroplasts of the inhibition of oxygen evolution with K 3  [Fe (CN) 6 ] as electron acceptor indicates, that there exists a binding area with different specific subreceptor sites rather than a unique binding site for the various types of inhibitors. Furthermore, trypsination of the proteinaceous component enhances the efficiency of the plastoquinone pool to act as a non-photochemical quencher for excitation energy.

Studies about the Mechanism of Herbicidal Interaction with Photosystem II in Isolated Chloroplasts