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Covalent modification of chloroplast Photosystem II polypeptides by p-nitrothiophenol

Authors
  • Mullet, J.E.
  • Arntzen, C.J.
  • Kobayashi, Y.
  • Inoue, Y.
Type
Published Article
Journal
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher
Elsevier
Publication Date
Jan 01, 1981
Volume
635
Issue
2
Pages
215–224
Identifiers
DOI: 10.1016/0005-2728(81)90021-9
Source
Elsevier
Keywords
License
Unknown

Abstract

Illumination of the chlorophyll a b light-harvesting complex in the presence of p- nitrothio[ 14 C]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[ 14 C]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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