The thermal blockage of 3c e oxidation was analysed in PS II membrane fragments by monitoring flash-induced changes of the relative fluorescence quantum yield as a function of temperature. The results obtained reveal: (a) in dark-adapted samples the fraction of 3c e that is not reoxidised within a time domain of 10 s after the actinic flash increases with lowering the temperature (half-maximum effect at 250^260 K), (b) at low temperatures where 3c e generated in dark-adapted samples remains almost completely reduced, a significant extent of 3c e reoxidation arises when samples are used that were preilluminated at room temperature by one saturating flash followed by rapid freezing before performing the experiment, and (c) the extent of 3c e that is reoxidised at 258 K exhibits a characteristic binary oscillation as a function of the number of preillumination flashes given at room temperature. Based on these data it is inferred that Q f and 3c f are located at different equilibrium positions in the Q f site. As a consequence the formation of 3c f is coupled with significant structural changes that require sufficient flexibility of the protein matrix. This general feature corresponds with a recently proposed model for the acceptor side reactions of anoxygenic bacteria [Stowell, M.H