REVIEW: Electron Transfer in Photosystem I Containing Native and Modified Quinone Acceptors

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A. Yu. Semenov^1,2*, A. A. Petrova¹, M. D. Mamedov¹, and V. A. Nadtochenko²

¹A.N. Belozersky Institute of Physical-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: +7 (495) 939-3181; E-mail: semenov@genebee.msu.ru

²N.N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia; fax: +7 (499) 137-8357

^* To whom correspondence should be addressed.

Received January 27, 2015; Revision received March 8, 2015

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The pigment–protein complex of photosystem I (PS I) catalyzes light-driven oxidation of plastocyanin or cytochrome c₆ and reduction of ferredoxin or flavodoxin in oxygenic photosynthetic organisms. In this review, we describe the current state of knowledge of the processes of excitation energy transfer and formation of the primary and secondary ion-radical pairs within PS I. The electron transfer reaction involving quinone cofactor in the A₁ site and its role in providing asymmetry of electron transport as well as interaction with oxygen and ascorbate in PS I are discussed.

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KEY WORDS: photosystem I, reaction center, electron transfer, asymmetry, primary reactions, quinone acceptors, interaction with oxygen and ascorbate

DOI: 10.1134/S0006297915060024

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