Transmembrane electric potential difference in the protein-pigment complex of photosystem 2

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

Research output: Contribution to journalReview articlepeer-review

Abstract

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 (δ φ). The major contribution to δ φ of the PS2 reaction center is due to charge separation between the primary chlorophyll donor P680 and the quinone acceptor QA, accompanied by re-reduction of P+ 680 by the redox-active tyrosine residue YZ. The processes associated with the uptake and release of protons on the acceptor and donor sides of the enzyme, respectively, are also coupled with δ φ generation. The objective of this work was to describe the mechanisms of δ φ 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.

Original languageEnglish (US)
Pages (from-to)947-955
Number of pages9
JournalBiochemistry (Moscow)
Volume77
Issue number9
DOIs
StatePublished - Sep 1 2012

All Science Journal Classification (ASJC) codes

  • Biochemistry

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