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New Insights into Photosystem I (Second Edition)

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Plant Sciences".

Deadline for manuscript submissions: 20 December 2025 | Viewed by 1014

Special Issue Editors


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Guest Editor
Photosynthesis Research Unit, National Research Council of Italy (CNR-IBBA), Via Corti 12, 20133 Milan, Italy
Interests: biophysics; biochemistry; plant physiology; plant biology; plant biotechnology; plant environmental; stress physiology; fluorescence; abiotic stress tolerance; spectroscopy; absorption
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Guest Editor
Department of Physics and Astronomy, Georgia State University, Atlanta, GA, USA
Interests: photosynthesis; absorption; Raman spectroscopy; electronic structure; spectrometry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Photosystem I is a large protein cofactor supercomplex fundamental component of the electron transport chain of oxygen-evolving photosynthetic organisms, and it can operate either in series with Photosystem II in the linear electron transport chain, or independently from Photosystem II in a cyclic transport. Photosystem I is known to operate with a photochemical quantum conversion yield close to the unit, which makes it an attractive system for the development of biological mimicking of artificial molecules and devices. In Photosystem I, two structurally symmetric electron transfer chains operate in electron transfer through the so-called bidirectional mechanism, which distinguishes it from both PSII and its homologue, the purple bacteria reaction centre. However, despite intense research over several decades, some of the key mechanisms concerning the primary photochemical conversion reactions, the energy of the successive electron transfer cascade, and the mechanisms controlling the functionality of the two active electron transfer branches are yet to be fully elucidated. Furthermore, the partners and mechanisms of cyclic electron transfer in the thylakoid membranes, and the physiological role of this transport mechanism, are yet to be fully established.

This Special Issue for IJMS aims to gather contributions aimed at improving the understanding of the molecular mechanism of light harvesting, photochemical energy conversion, electron transfer, and electron transport reaction involving Photosystem I.

Dr. Stefano Santabarbara
Prof. Dr. Gary Hastings
Guest Editors

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Keywords

  • photosystem I
  • photochemisty
  • electron transfer
  • protein–cofactor interaction
  • reaction kinetics
  • reaction mechanism
  • redox tuning
  • light harvesting
  • low-energy (red) forms
  • bioenergetics
  • cyclic electron transfer

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Published Papers (1 paper)

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Research

13 pages, 3554 KiB  
Article
The Quenching of Long-Wavelength Fluorescence by the Closed Reaction Center in Photosystem I in Thermostichus vulcanus at 77 K
by Parveen Akhtar, Ivo H. M. van Stokkum and Petar H. Lambrev
Int. J. Mol. Sci. 2024, 25(22), 12430; https://doi.org/10.3390/ijms252212430 - 19 Nov 2024
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Abstract
Photosystem I in most organisms contains long-wavelength or “Red” chlorophylls (Chls) absorbing light beyond 700 nm. At cryogenic temperatures, the Red Chls become quasi-traps for excitations as uphill energy transfer is blocked. One pathway for de-excitation of the Red Chls is via transfer [...] Read more.
Photosystem I in most organisms contains long-wavelength or “Red” chlorophylls (Chls) absorbing light beyond 700 nm. At cryogenic temperatures, the Red Chls become quasi-traps for excitations as uphill energy transfer is blocked. One pathway for de-excitation of the Red Chls is via transfer to the oxidized RC (P700+), which has broad absorption in the near-infrared region. This study investigates the excitation dynamics of Red Chls in Photosystem I from the cyanobacterium Thermostichus vulcanus at cryogenic temperatures (77 K) and examines the role of the oxidized RC in modulating their fluorescence kinetics. Using time-resolved fluorescence spectroscopy, the kinetics of Red Chls were recorded for samples with open (neutral P700) and closed (P700+) RCs. We found that emission lifetimes in the range of 710–720 nm remained unaffected by the RC state, while more red-shifted emissions (>730 nm) decayed significantly faster when the RC was closed. A kinetic model describing the quenching by the oxidized RC was constructed based on simultaneous fitting to the recorded fluorescence emission in Photosystem I with open and closed RCs. The analysis resolved multiple Red Chl forms and variable quenching efficiencies correlated with their spectral properties. Only the most red-shifted Chls, with emission beyond 730 nm, are efficiently quenched by P700+, with rate constants of up to 6 ns−1. The modeling results support the notion that structural and energetic disorder in Photosystem I can have a comparable or larger effect on the excitation dynamics than the geometric arrangement of Chls. Full article
(This article belongs to the Special Issue New Insights into Photosystem I (Second Edition))
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