REVIEW: Transmembrane Electric Potential Difference in the Protein–Pigment Complex of Photosystem 2

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M. D. Mamedov^*, V. N. Kurashov, I. O. Petrova, and A. Yu. Semenov

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-3181; E-mail: mamedov@genebee.msu.ru

^* To whom correspondence should be addressed.

Received April 12, 2012

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The protein–pigment complex of photosystem 2 (PS2) localized in the thylakoid membranes of higher plants, algae, and cyanobacteria is the main source of oxygen on Earth. The light-induced functioning of PS2 is directly linked to electron and proton transfer across the membrane, which results in the formation of transmembrane electric potential difference (ΔΨ). The major contribution to ΔΨ of the PS2 reaction center is due to charge separation between the primary chlorophyll donor P₆₈₀ and the quinone acceptor Q_A, accompanied by re-reduction of P₆₈₀⁺ by the redox-active tyrosine residue Y_Z. The processes associated with the uptake and release of protons on the acceptor and donor sides of the enzyme, respectively, are also coupled with ΔΨ generation. The objective of this work was to describe the mechanisms of ΔΨ generation associated with the S-state transitions of the water-oxidizing complex in intact PS2 complex and in PS2 preparation depleted of Mn₄Ca cluster in the presence of artificial electron donors. The findings elucidate the mechanisms of electrogenic reactions on the PS2 donor side and may be a basis for development of an effective solar energy conversion system.

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KEY WORDS: photosystem 2, reaction center, S-state transitions, proteoliposomes, electron donors, direct electrometric method, photoelectric response, electrogenicity, channels

DOI: 10.1134/S0006297912090015

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