The susceptibility of the P-benzoquinone-mediated electron transport and atrazine binding to trypsin and its modification by CaCl2 in thylakoids and PS II membrane fragments

G. Renger, R. Hagemann, Raimund Fromme

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

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 CaCl2 in PS II membrane fragments, but no protection is observed in thylakoids. NH2OH and K3[Fe(CN)6] both reduce the binding affinity in PS II membrane fragments. The action of NH2OH is invariant to CaCl2 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed.

Original languageEnglish (US)
Pages (from-to)210-214
Number of pages5
JournalFEBS Letters
Volume203
Issue number2
DOIs
StatePublished - Jul 28 1986
Externally publishedYes

Fingerprint

Atrazine
Thylakoids
Electron Transport
Trypsin
Membranes
Octoxynol
Binding Sites
benzoquinone
Oxygen

Keywords

  • Atrazine binding
  • CaCl protection
  • Hydroxylamine effect
  • Photosystem II membrane fragment
  • Potassium ferricyanide effect
  • Trypsin effect

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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abstract = "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 CaCl2 in PS II membrane fragments, but no protection is observed in thylakoids. NH2OH and K3[Fe(CN)6] both reduce the binding affinity in PS II membrane fragments. The action of NH2OH is invariant to CaCl2 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed.",
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T1 - The susceptibility of the P-benzoquinone-mediated electron transport and atrazine binding to trypsin and its modification by CaCl2 in thylakoids and PS II membrane fragments

AU - Renger, G.

AU - Hagemann, R.

AU - Fromme, Raimund

PY - 1986/7/28

Y1 - 1986/7/28

N2 - 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 CaCl2 in PS II membrane fragments, but no protection is observed in thylakoids. NH2OH and K3[Fe(CN)6] both reduce the binding affinity in PS II membrane fragments. The action of NH2OH is invariant to CaCl2 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed.

AB - 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 CaCl2 in PS II membrane fragments, but no protection is observed in thylakoids. NH2OH and K3[Fe(CN)6] both reduce the binding affinity in PS II membrane fragments. The action of NH2OH is invariant to CaCl2 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed.

KW - Atrazine binding

KW - CaCl protection

KW - Hydroxylamine effect

KW - Photosystem II membrane fragment

KW - Potassium ferricyanide effect

KW - Trypsin effect

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