Advances in the Structural Investigation of Photosystem I and II: New Insights into Their Function and Physiology

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Physiology and Metabolism".

Deadline for manuscript submissions: closed (30 April 2021) | Viewed by 4434

Special Issue Editors


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Guest Editor
Department of Applied Science and Technology–BioSolar Lab, Politecnico di Torino, 10144 Torino, Italy
Interests: Plants; cyanobacteria; photosynthesis; thylakoid membranes; photosystems; light acclimation; plant physiology; plant biochemistry; proteomics; structural biology; molecular enzymology

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Guest Editor
Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK
Interests: Photosystems; energy transfer; electron transfer; electrochemistry; bicarbonate; reactive oxygen species; bioenergetics; far-red photoacclimation; photodamage; bioenergy; molecular enzymology; photobiology; photochemistry; biophysics; bioinorganic chemistry

Special Issue Information

Dear Colleagues,

Photosystems I (PSI) and II (PSII) are large membrane pigment–protein complexes that convert solar energy into the chemical energy that powers life on Earth. Over the last decade, we have witnessed an explosion of high-resolution structures of PSI and PSII from diverse photosynthetic organisms, sometimes in different oligomerization states and even from organisms grown in different light conditions. This has been the result of exceptional advances in the development of the instrumentation and software adopted for the structural techniques used to determine these challenging structures. Among these techniques, single particle cryo-electron microscopy and serial femtosecond crystallography have recently emerged to flank traditional X-ray crystallography.

Knowledge of the structure of PSI and PSII in diverse photosynthetic organisms allows new ideas to be developed on the evolution of the reaction centers, the functional role of the oligomerization state of PSI, and the diversification of the light-harvesting antenna components of PSII within supercomplexes. These structures also update our understanding on many aspects of the PSI and PSII function, such as light harvesting and energy transfer from outer antenna systems to the photosystem cores, charge separation and acceptor side mechanisms of PSII, mechanistic description of the water oxidation catalytic cycle, state transitions in plants, and acclimation and non-photochemical quenching processes.

These high-resolution structures pave the way for a comprehensive understanding of the dynamic molecular mechanisms by which photosynthetic organisms adapt to different light and nutrient conditions. Complementary structural information obtained by electron microscopy at lower resolution together with cryo-electron tomography help in elucidating the PSI and PSII arrangement within the thylakoid membrane system. Furthermore, in the near future, it is expected that these high-resolution structures will increasingly become key players for investigations on protein–protein interactions and the docking of specific molecules of interest to the agri-food industry. They will constitute the basis for molecular dynamic simulations and structure-based computational analysis on excitation energy transfer and photochemistry. They will become the blueprint for targeted biotechnological applications.

This Special Issue of Plants aims to highlight recent advances in our understanding of the structure–function relationship of PSI and PSII, stemming from the outstanding advances currently available on their structures. New insights at the molecular, physiological, and evolutionary level will be showcased.

Dr. Cristina Pagliano
Dr. Andrea Fantuzzi
Guest Editors

Manuscript Submission Information

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Keywords

  • Photosystems I and II
  • supercomplexes
  • evolution of photosystems
  • photosynthetic molecular mechanism
  • cryo-electron microscopy
  • X-ray crystallography
  • serial femtosecond crystallography
  • computational analysis on excitation energy/electron transfer and charge separation
  • molecular dynamics simulation

Published Papers (1 paper)

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Research

15 pages, 3032 KiB  
Article
Binding Properties of Photosynthetic Herbicides with the QB Site of the D1 Protein in Plant Photosystem II: A Combined Functional and Molecular Docking Study
by Beatrice Battaglino, Alessandro Grinzato and Cristina Pagliano
Plants 2021, 10(8), 1501; https://doi.org/10.3390/plants10081501 - 21 Jul 2021
Cited by 21 | Viewed by 3957
Abstract
Photosystem II (PSII) is a multi-subunit enzymatic complex embedded in the thylakoid membranes responsible for the primary photosynthetic reactions vital for plants. Many herbicides used for weed control inhibit PSII by interfering with the photosynthetic electron transport at the level of the D1 [...] Read more.
Photosystem II (PSII) is a multi-subunit enzymatic complex embedded in the thylakoid membranes responsible for the primary photosynthetic reactions vital for plants. Many herbicides used for weed control inhibit PSII by interfering with the photosynthetic electron transport at the level of the D1 protein, through competition with the native plastoquinone for the QB site. Molecular details of the interaction of these herbicides in the D1 QB site remain to be elucidated in plants. Here, we investigated the inhibitory effect on plant PSII of the PSII-inhibiting herbicides diuron, metobromuron, bentazon, terbuthylazine and metribuzin. We combined analysis of OJIP chlorophyll fluorescence kinetics and PSII activity assays performed on thylakoid membranes isolated from pea plants with molecular docking using the high-resolution PSII structure recently solved from the same plant. Both approaches showed for terbuthylazine, metribuzin and diuron the highest affinity for the D1 QB site, with the latter two molecules forming hydrogen bonds with His215. Conversely, they revealed for bentazon the lowest PSII inhibitory effect accompanied by a general lack of specificity for the QB site and for metobromuron an intermediate behavior. These results represent valuable information for future design of more selective herbicides with enhanced QB binding affinities to be effective in reduced amounts. Full article
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