Studies on Herbicide Binding in Photosystem II Membrane Fragments from Spinach

R. Fromme, G. Renger

Research output: Contribution to journalArticle

5 Scopus citations

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+ removal from a site that is characterized by a high affinity as reflected by KDvalues of the order of 10-7 m. 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.

Original languageEnglish (US)
Pages (from-to)373-378
Number of pages6
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume45
Issue number5
DOIs
StatePublished - May 1990
Externally publishedYes

Keywords

  • Atrazine Binding
  • Ca Effects
  • Mild Proteolysis
  • Photosystem II
  • Temperature Dependence

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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