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The susceptibility of the P ‐benzoquinone‐mediated electron transport and atrazine binding to trypsin and its modification by CaCl 2 in thylakoids and PS II membrane fragments
Author(s) -
Renger G.,
Hagemann R.,
Fromme R.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80744-x
Subject(s) - thylakoid , chemistry , atrazine , membrane , electron transport chain , trypsin , benzoquinone , biophysics , binding site , biochemistry , chloroplast , enzyme , biology , pesticide , agronomy , gene
Comparative studies in thylakoids and oxygen‐evolving Triton X‐100 PS II membrane fragments reveal: (i) There exists one high‐affinity atrazine binding site per PS II in both preparations. The affinity is reduced in PS II membrane fragments, (ii) The susceptibility to tryptic attack on atrazine binding and p‐BQ‐mediated electron transport is markedly reduced by CaCl 2 in PS II membrane fragments, but no protection is observed in thylakoids. NH 2 OH and K 3 [Fe(CN) 6 ] both reduce the binding affinity in PS II membrane fragments. The action of NH 2 OH is invariant to CaCl 2 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed.