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Photosystem II: evolutionary perspectives.

A W Rutherford1, P Faller

  • 1Service de Bioénergétique, URA CNRS 2096, Bat 532, CEA Saclay, 91191 Gif-sur-Yvette, France. rutherford@dsvidf.cea.fr

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|February 22, 2003
PubMed
Summary
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Photosystem II (PSII) likely evolved from a homodimeric ancestor. A mutation splitting the special chlorophyll pair increased oxidation potential, enabling oxygen evolution and driving the shift to today's heterodimeric PSII structure.

Area of Science:

  • Biochemistry
  • Photosynthesis Research
  • Evolutionary Biology

Background:

  • Photosystem II (PSII) is crucial for oxygenic photosynthesis.
  • Its structure and function are modeled based on current understanding.
  • PSII is proposed to have evolved from a homodimeric ancestor.

Purpose of the Study:

  • To propose a key evolutionary event in Photosystem II (PSII) development.
  • To explain the transition from a homodimeric to a heterodimeric reaction center.
  • To elucidate the role of pigment evolution in enabling oxygen evolution.

Main Methods:

  • Theoretical modeling of Photosystem II evolution.
  • Analysis of cofactor properties within reaction center proteins.
  • Hypothesizing selective pressures driving structural changes.

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Main Results:

  • A mutation separating the ancestral special chlorophyll pair is proposed as a key evolutionary event.
  • This separation significantly increased the oxidation potential of chlorophylls.
  • The increased oxidation potential facilitated the development of oxygen evolution.
  • The inefficient and damaging nature of a homodimeric system created selective pressure for the current heterodimeric PSII.

Conclusions:

  • The evolution of PSII involved a critical mutation that separated paired chlorophylls, enabling oxygen evolution.
  • The current heterodimeric structure of PSII, with the D1 protein, is an adaptation for managing oxidative stress.
  • The role of TyrD on the D2 side may involve electrostatic confinement of positive charges to the D1 protein.