Covalent modification of chloroplast Photosystem II polypeptides by p-nitrothiophenol

J. E. Mullet, C. J. Arntzen, Y. Kobayashi, Y. Inoue

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Illumination of the chlorophyll a b light-harvesting complex in the presence of p-nitrothio[14C]phenol caused quenching of fluorescence emission at 685 nm (77 K) relative to 695 nm and covalent modification of light-harvesting complex polypeptides. Fluorescence quenching saturated with one p-nitrothiophenol bound per light-harvesting complex polypeptide (10-13 chlorophylls); 1 2 maximal quenching occurred with one p-nitrothiophenol bound per light-harvesting complex polypeptides (190-247 chlorophylls). This result provides direct evidence for excitation energy transfer between light-harvesting complex subunits which contain 4-6 polypeptides plus 40-78 chlorophylls per complex. Illumination of chloroplasts or Photosystem II (PS II) particles in the presence of p-nitrothio[14C]phenol caused inhibition of PS II activity and labeling of several polypeptides including those of 42-48 kilodaltons previously identified as PS II reaction center polypeptides. In chloroplasts, inhibition of oxygen evolution accelerated p-nitrothiophenol modification reactions; DCMU or donors to PS II decreased p-nitrothiophenol modification. These results are consistent with the hypothesis that accumulation of oxidizing equivalents on the donor side of PS II creates a 'reactive state' in which polypeptides of PS II are susceptible to p-nitrothiophenol modification.

Original languageEnglish (US)
Pages (from-to)215-224
Number of pages10
JournalBBA - Bioenergetics
Volume635
Issue number2
DOIs
StatePublished - Apr 13 1981
Externally publishedYes

Fingerprint

Photosystem II Protein Complex
Chloroplasts
Peptides
Light
Chlorophyll
Quenching
Phenol
Lighting
Fluorescence
Diuron
Excitation energy
Energy Transfer
Energy transfer
Labeling
Oxygen

Keywords

  • Fluorescence quenching
  • Light-harvesting complex
  • p-Nitrothiophenol
  • Photosystem II
  • Protein modification
  • Reaction center

ASJC Scopus subject areas

  • Biophysics
  • Medicine(all)

Cite this

Covalent modification of chloroplast Photosystem II polypeptides by p-nitrothiophenol. / Mullet, J. E.; Arntzen, C. J.; Kobayashi, Y.; Inoue, Y.

In: BBA - Bioenergetics, Vol. 635, No. 2, 13.04.1981, p. 215-224.

Research output: Contribution to journalArticle

Mullet, J. E. ; Arntzen, C. J. ; Kobayashi, Y. ; Inoue, Y. / Covalent modification of chloroplast Photosystem II polypeptides by p-nitrothiophenol. In: BBA - Bioenergetics. 1981 ; Vol. 635, No. 2. pp. 215-224.
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N2 - Illumination of the chlorophyll a b light-harvesting complex in the presence of p-nitrothio[14C]phenol caused quenching of fluorescence emission at 685 nm (77 K) relative to 695 nm and covalent modification of light-harvesting complex polypeptides. Fluorescence quenching saturated with one p-nitrothiophenol bound per light-harvesting complex polypeptide (10-13 chlorophylls); 1 2 maximal quenching occurred with one p-nitrothiophenol bound per light-harvesting complex polypeptides (190-247 chlorophylls). This result provides direct evidence for excitation energy transfer between light-harvesting complex subunits which contain 4-6 polypeptides plus 40-78 chlorophylls per complex. Illumination of chloroplasts or Photosystem II (PS II) particles in the presence of p-nitrothio[14C]phenol caused inhibition of PS II activity and labeling of several polypeptides including those of 42-48 kilodaltons previously identified as PS II reaction center polypeptides. In chloroplasts, inhibition of oxygen evolution accelerated p-nitrothiophenol modification reactions; DCMU or donors to PS II decreased p-nitrothiophenol modification. These results are consistent with the hypothesis that accumulation of oxidizing equivalents on the donor side of PS II creates a 'reactive state' in which polypeptides of PS II are susceptible to p-nitrothiophenol modification.

AB - Illumination of the chlorophyll a b light-harvesting complex in the presence of p-nitrothio[14C]phenol caused quenching of fluorescence emission at 685 nm (77 K) relative to 695 nm and covalent modification of light-harvesting complex polypeptides. Fluorescence quenching saturated with one p-nitrothiophenol bound per light-harvesting complex polypeptide (10-13 chlorophylls); 1 2 maximal quenching occurred with one p-nitrothiophenol bound per light-harvesting complex polypeptides (190-247 chlorophylls). This result provides direct evidence for excitation energy transfer between light-harvesting complex subunits which contain 4-6 polypeptides plus 40-78 chlorophylls per complex. Illumination of chloroplasts or Photosystem II (PS II) particles in the presence of p-nitrothio[14C]phenol caused inhibition of PS II activity and labeling of several polypeptides including those of 42-48 kilodaltons previously identified as PS II reaction center polypeptides. In chloroplasts, inhibition of oxygen evolution accelerated p-nitrothiophenol modification reactions; DCMU or donors to PS II decreased p-nitrothiophenol modification. These results are consistent with the hypothesis that accumulation of oxidizing equivalents on the donor side of PS II creates a 'reactive state' in which polypeptides of PS II are susceptible to p-nitrothiophenol modification.

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