Abstract This report reviews studies which provide evidence defining the mode of action and site of action of photosystem II (PS II) herbicides; the involvement of the secondary electron carrier on the reducing side of PS II (called B) is indicated as the target site for these compounds. These studies of the action of PS II-inhibitors were performed in chloroplasts of various weed species in order to define the mechanism which is responsible for herbicide tolerance at the level of chloroplast membranes in newly discovered triazine-resistant weed biotypes. Many species of triazine-resistant weed biotypes have been collected in North America and Europe. Where data is available, these plants have been found to share the following common features: a) they were discovered in areas where triazine herbicides had been used repeatedly, b) resistance to the triazines is extreme; it is not due to a minor shift in herbicidal response, c) no changes in herbicide uptake, translocation or metabolism - as compared to susceptible biotypes - can be detected, d) resistance is selective for only certain classes of photosynthetic herbicides, and, e) chloroplasts isolated from triazine-resistant weeds display high preferential resistance to the triazines in assays of photosystem II partial reactions. To focus on the mechanism which regulates preferential herbicide activity, we have characterized susceptible and resistant chloroplasts in the presence and absence of herbicides. Properties of the PS II complex of chloroplasts from several different triazine-resistant weed biotypes share the following traits: a) the herbicide binding site (as measured by direct binding of radiolabeled herbicides or by inhibition experiments) is modified such that the affinity for triazines is dramatically reduced. b) alterations in response to many PS II-herbicides occur such that the triazine-resistant chloroplasts are very strongly resistant to all symmetrical triazines, strongly resistant to assymmetrical triazinones, partially resistant to pyridazones and uracils, only slightly resistant to ureas or amides, and increasingly susceptible to nitrophenols, phenols and the herbicide bentazon (all as compared to susceptible chloroplasts), c) there is a change in the reaction kinetics of the electron transport step between the primary and secondary electron acceptors (referred to as Q and B ), and d) in two examples, specific small changes in a membranepolypeptide can be detected in the resistant thylakoids. We suggest that certain amino acids or segments of the apoprotein of B (the bound quinone which acts as the secondary electron carrier) are modified or deleted in these chloroplasts. Such a polypeptide change could affect both the redox poising of the Q-/B reaction pair, and the specific binding of herbicides.