Fromme, R.Renger, G.2018-11-102018-11-1019900939-5075https://depositonce.tu-berlin.de/handle/11303/8501http://dx.doi.org/10.14279/depositonce-7647The mechanism of atrazine binding and its modification by Chelex-100-induced Ca2+ depletion and proteolytic degradation by trypsin, was analyzed in PS II membrane fragments from spinach. It was found: 1) Chelex-100 treatment leads in a comparatively slow process (t1/2 = 5 - 10 min) to Ca2+ re moval from a site that is characterized by a high affinity as reflected by KD values of the order of 10-7M. The number of these binding sites was found to be almost one per PS II in samples washed twice with Ca2+ -free buffer. 2) Chelex-100 treatment does not affect the affinity of atrazine binding but increases the susceptibility to proteolytic attack by trypsin. 3) The electron transport activity is only slightly affected by Chelex-100 treatment. 4) The atrazine binding exhibits a rather small T-dependence within the physiological range of 7 °C to 27 °C. The implications of these findings for herbicide binding are discussed.en570 Biowissenschaften; Biologieatrazine bindingPhotosystem IICa2+ effectstemperature dependencemild proteolysisArticle1865-7125