Photosynthesis Research

, 98:121 | Cite as

Electrogenic reactions and dielectric properties of photosystem II

Review

Abstract

This review is focused on the mechanism of photovoltage generation involving the photosystem II turnover. This large integral membrane enzyme catalyzes the light-driven oxidation of water and reduction of plastoquinone. The data discussed in this work show that there are four main electrogenic steps in native complexes: (i) light-induced charge separation between special pair chlorophylls P680 and primary quinone acceptor QA; (ii) P 680 + reduction by the redox-active tyrosine YZ of polypeptide D1; (iii) oxidation of Mn cluster by Y Z ox followed by proton release, and (iv) protonation of double reduced secondary quinone acceptor QB. The electrogenicity related to (i) proton-coupled electron transfer between Q A and preoxidized non-heme iron (Fe3+) in native and (ii) electron transfer between protein–water boundary and Y Z ox in the presence of redox-dye(s) in Mn-depleted samples, respectively, were also considered. Evaluation of the dielectric properties using the electrometric data and the polarity profiles of reaction center from purple bacteria Blastochloris viridis and photosystem II are presented. The knowledge of the profile of dielectric permittivity along the photosynthetic reaction center is important for understanding of the mechanism of electron transfer between redox cofactors.

Keywords

Photosystem II Proteoliposomes Photovoltage Iron–quinone complex Oxygen-evolving complex Dielectric properties 

Abbreviations

PS II

Photosystem II

RC

Reaction center

P680

Special pair chlorophylls of PS II

QA (QB)

Primary (secondary) plastoquinone acceptor

Fe2+(Fe3+)

Non-heme iron in its reduced (oxidized) state

YZ

Redox-active tyrosine of polypeptide D1

ΔΨ

Photovoltage

ε

Effective dielectric constant

OEC

Oxygen-evolving complex

τ

Characteristic time constant

Notes

Acknowledgments

The authors appreciate the excellent technical assistance of Andrey Zaspa. Thanks are also due to Dr. Chamorovsky S.K. and Chamorovsky K.S. for critical reading of the manuscript. The work was supported by grants from the Russian Foundation for Basic Research (06-04-48672 and 07-04-01050) and from Russian Federal Agency for Science and Innovation (02.512.11.2085).

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© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.A.N. Belozersky Institute of Physical–Chemical BiologyMoscow State UniversityMoscowRussia
  2. 2.A.N. Frumkin Institute of Physical Chemistry and ElectrochemistryRussian Academy of SciencesMoscowRussia

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