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Photosystem two

J Barber1

  • 1Wolfson Laboratories, Biochemistry Department, Imperial College of Science, Technology and Medicine, London, UK. j.barber@ic.ac.uk

Biochimica Et Biophysica Acta
|August 7, 1998
PubMed
Summary
This summary is machine-generated.

Photosystem II (PSII) oxidizes water but is vulnerable to damage from singlet oxygen. This damage necessitates rapid degradation and replacement of the D1 protein in the PSII reaction center.

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Area of Science:

  • Biochemistry
  • Photosynthesis research
  • Plant science

Background:

  • Photosystem II (PSII) possesses a unique high redox potential for water oxidation.
  • This high potential makes PSII susceptible to damage from singlet oxygen generated by chlorophyll triplets.
  • The D1 and D2 proteins form the PSII reaction center and are prone to light-induced oxidation.

Purpose of the Study:

  • To investigate the light-induced damage to D1 and D2 proteins in Photosystem II.
  • To understand the implications of this damage on D1 protein turnover.
  • To correlate structural findings with known disassembly/reassembly processes.

Main Methods:

  • Mass spectrometry was employed to analyze protein oxidation.
  • Electron microscopy was used for structural studies of isolated PSII.
  • Analysis focused on the relative positioning of major PSII proteins.

Main Results:

  • Mass spectrometry confirmed light-induced oxidation of D1 and D2 proteins.
  • Structural studies revealed a pseudo-twofold symmetry between D1/CP43 and D2/CP47.
  • These findings support the high rate of D1 protein degradation and replacement.

Conclusions:

  • Detrimental side reactions, including protein oxidation, underlie the rapid turnover of the D1 protein.
  • Structural data is consistent with current models of D1 protein turnover.
  • The structural relationship between PSII and photosystem I is further elucidated.