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RAS BiologyБиохимия Biochemistry

  • ISSN (Print) 0320-9725
  • ISSN (Online) 3034-5294

STUDY OF ELECTRON TRANSFER IN PHOTOSYSTEM I USING HIGH-FREQUENCY EPR SPECTROSCOPY. IN MEMORY OF PROFESSOR KLAUS MÖBIUS (1936–2024)

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PII
S30345294S0320972525070023-1
DOI
10.7868/S3034529425070023
Publication type
Review
Status
Published
Authors
V.V. Ptushenko
  • Affiliation: Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology
A.Yu. Semenov
  • Affiliation: Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology
Volume/ Edition
Volume 90 / Issue number 7
Pages
903-914
Abstract
Klaus Möbius, Professor at the Free University of Berlin, was an outstanding physical chemist and biophysicist. He was a pioneer of the development of high field/high-frequency EPR spectroscopy methods and their application in the study of photosynthesis. Among the most essential are applications in studying the charge transfer kinetics and properties of the ion-radical pairs in photosynthetic reaction centers (RC). Under his leadership and with his direct participation a unique setup allowing registration of the kinetics of the electron transfer between (bacteriochlorophyll dimer and quinone in the bacterial photosynthetic RC and plant photosystem I (PSI) was created. This setup also allowed the precise determining the distance between separated charges based on measuring the frequencies of the Electron Spin Echo Envelope Modulation (ESEEM). This setup made it possible to prove that electron transfer in PSI occurs mainly along the branch A of redox cofactors. The kinetics of reverse reaction (reoxidation of the phyllosemiquinone-anion A1– and reduction of the photo-oxidized chlorophyll dimer P700+) in the PSI were measured under the same conditions. The essential data on the bioprotective effect of the disaccharide trehalose on the kinetics of forward and backward electron transfer in PSI complexes were obtained. A significant slowdown in the kinetics of electron transfer due to the restriction of the protein conformational mobility, as well as the long-term maintaining of PSI functional activity dried in a vitreous trehalose matrix at room temperature (i.e. subjected to a reversible anhydrobiosis) was demonstrated. These results obtained in collaboration with Prof. Möbius and Prof. Venturoli (Bologna) allowed elucidating the role of the hydrogen bond network in conformational mobility of the protein subunits in ensuring electron transfer in the photosynthetic RC.
Keywords
высокочастотная ЭПР-спектроскопия ион-радикальная пара мультирезонансные методы первичный донор электрона семихнион железосерные кластеры трегалоза
Date of publication
04.02.2026
Year of publication
2026
Number of purchasers
0
Views
83

References

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