Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-7647
Main Title: Studies on Herbicide Binding in Photosystem II Membrane Fragments from Spinach
Author(s): Fromme, R.
Renger, G.
Type: Article
Language Code: en
Abstract: The 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.
URI: https://depositonce.tu-berlin.de//handle/11303/8501
http://dx.doi.org/10.14279/depositonce-7647
Issue Date: 1990
Date Available: 10-Nov-2018
DDC Class: 570 Biowissenschaften; Biologie
Subject(s): atrazine binding
Photosystem II
Ca2+ effects
temperature dependence
mild proteolysis
License: https://creativecommons.org/licenses/by-nc-nd/3.0/
Journal Title: Zeitschrift für Naturforschung C
Publisher: De Gruyter
Publisher Place: Berlin
Volume: 45
Issue: 5
Publisher DOI: 10.1515/znc-1990-0511
Page Start: 373
Page End: 378
EISSN: 1865-7125
ISSN: 0939-5075
Appears in Collections:Inst. Chemie » Publications

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