Two DCMU-resistant strains of the cyanobacterium Synechocystis 6714 were used to analyse the binding sites of DCMU, atrazine and QB. DCMUr-IIA was DCMU and atrazine resistant; it presented an impaired electron flow and its 33-kDa protein was weakly attached to the membrane. DCMUr-IIB, derived from the former, simultaneously regained atrazine sensitivity, normal electron flow and a tight linkage of the 33-kDa protein to the membrane. This mutant shows that loss of DCMU binding does not necessarily affect the binding of either atrazine or QB. The role of the 33-kDa protein is discussed.