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Electron transfer in photosystem I containing native and modified quinone acceptors

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Abstract

The pigment-protein complex of photosystem I (PS I) catalyzes light-driven oxidation of plastocyanin or cytochrome c 6 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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Abbreviations

A0A and A0B :

primary electron acceptor chlorophylls in A and B branches

A1A and A1B :

quinone molecules — secondary electron acceptors in A and B branches

Chl:

chlorophyll

Chl1A/Chl1B:

Chl2A/Chl2B, and Chl3A/Chl3B are the first, second, and third molecules of chlorophyll in symmetrical branches of redox cofactors A and B in PS I

Cl2NQ:

2,3-dichloro-1,4-naphthoquinone

P700:

dimer of chlorophyll — primary electron donor

PhQ:

phylloquinone

PQ:

plastoquinone

PS I:

photosystem I

RC:

reaction center

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Correspondence to A. Yu. Semenov.

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Published in Russian in Biokhimiya, 2015, Vol. 80, No. 6, pp. 775–784.

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Semenov, A.Y., Petrova, A.A., Mamedov, M.D. et al. Electron transfer in photosystem I containing native and modified quinone acceptors. Biochemistry Moscow 80, 654–661 (2015). https://doi.org/10.1134/S0006297915060024

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  • DOI: https://doi.org/10.1134/S0006297915060024

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