A5100773348- Photosynthetic Processes and Mechanisms
- Photoreceptor and optogenetics research
- Spectroscopy and Quantum Chemical Studies
- Algal biology and biofuel production
- Mitochondrial Function and Pathology
- Metal-Catalyzed Oxygenation Mechanisms
- Electrocatalysts for Energy Conversion
- Marine and coastal ecosystems
- Light effects on plants
- Enzyme Structure and Function
- Microbial Community Ecology and Physiology
- ATP Synthase and ATPases Research
- Porphyrin and Phthalocyanine Chemistry
- Protist diversity and phylogeny
- Electrochemical Analysis and Applications
- Metalloenzymes and iron-sulfur proteins
- Microbial Fuel Cells and Bioremediation
- Electrochemical sensors and biosensors
- Plant Stress Responses and Tolerance
- Origins and Evolution of Life
- Diatoms and Algae Research
- Advanced Photocatalysis Techniques
- Copper-based nanomaterials and applications
- Electron Spin Resonance Studies
- Advanced Electron Microscopy Techniques and Applications
Institute of Botany
2016-2025
Chinese Academy of Sciences
2016-2025
Okayama University
2016-2025
Okayama University of Science
2016-2025
Ocean University of China
2025
Beijing Botanical Garden
2023-2024
University of Tartu
2024
Jiangsu University
2024
Affiliated Hospital of Jiangsu University
2024
China National Botanical Garden
2023-2024
Photosystem II (PSII) is a multisubunit membrane protein complex performing light-induced electron transfer and water-splitting reactions, leading to the formation of molecular oxygen. The first crystal structure PSII from thermophilic cyanobacterium Thermosynechococcus elongatus was reported recently [Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W. & Orth, P. (2001) Nature 409, 739–743)] at 3.8-Å resolution. To analyze in more detail, we have obtained another...
Much is known about the transport of arsenite and antimonite into microbes, but identities mammalian proteins are unknown. The Saccharomyces cerevisiae FPS1 gene encodes a membrane protein homologous to bacterial aquaglyceroporin GlpF aquaglyceroporins AQP7 AQP9. Fps1p mediates glycerol uptake efflux in response hypoosmotic shock. has been shown facilitate metalloids antimonite, Escherichia coli homolog, GlpF, facilitates sensitivity metalloid salts. In this study, ability AQP9 substitute...
Mimicking the oxygen evolution center Making a synthetic analog of plant photosynthesis is key goal for exploiting solar energy and replacing fossil fuels. Zhang et al. synthesized manganese-calcium cluster that looks acts like in photosystem II (see Perspective by Sun). The mimic structurally resembles biological complex, with notable exception bridging protein ligands water-binding sites on dangling Mn atom. Functionally, however, cluster's metal readily undergoes four redox transitions,...
Photosystem I enters into the spotlight Plants rely on large complexes of proteins, chlorophyll, and other cofactors to turn light chemical energy. Qin et al. present crystal structures photosystem (PSI) light-harvesting complex (LHCI) supercomplex from pea plants (see Perspective by Croce). The well-resolved structure outer antenna their interaction with PSI core provide a structural basis for calculating excitation energy transfer efficiency. Moreover, organization orientation chlorophyll...
Saccharomyces cerevisiae has two independent transport systems for the removal of arsenite from cytosol. Acr3p is a plasma membrane transporter that confers resistance to arsenite, presumably by extrusion cells. Ycf1p, member ABC superfamily, catalyzes ATP-driven uptake As(III) into vacuole, also producing arsenite. Vacuolar accumulation requires reductant such as glutathione, suggesting substrate glutathione conjugate, As(GS)3. Disruption either ACR3 or YCF1 gene results in sensitivity and...
Photosynthetic water oxidation is catalyzed by the Mn4CaO5 cluster of photosystem II (PSII) with linear progression through five S-state intermediates (S0 to S4). To reveal mechanism oxidation, we analyzed structures PSII in S1, S2, and S3 states x-ray free-electron laser serial crystallography. No insertion was found but flipping D1 Glu189 upon transition leads opening a channel provides space for incorporation an additional oxygen ligand, resulting open cubane Mn4CaO6 oxyl/oxo bridge....
All the hues, even blues Photosynthetic organisms must balance maximizing productive light absorption and protecting themselves from too much light, which causes damage. Both tasks require pigments—chlorophylls carotenoids—which absorb energy either transfer it to photosystems or disperse as heat. Wang et al. determined structure of a fucoxanthin chlorophyll a/c–binding protein (FCP) diatom. The reveals arrangement specialized photosynthetic pigments in this light-harvesting protein....
A light-harvesting array in diatoms Photosynthetic organisms use huge arrays of pigments to draw light energy into the core photosystem II. The arrangement these influences how much reaches reaction center. Pi et al. determined structure II from a diatom complex with an antenna fucoxanthin–chlorophyll a/c binding proteins (FCPs) (see Perspective by Büchel). specialized this allow microalgae harvest within wide range visible spectrum. FCPs are arranged pattern analogous complexes plants....
Abstract Photosystem II (PSII) uses solar energy to oxidize water and delivers electrons for life on Earth. The photochemical reaction center of PSII is known possess two stationary states. In the open state (PSIIO), absorption a single photon triggers electron-transfer steps, which convert into charge-separated closed (PSIIC). Here, by using steady-state time-resolved spectroscopic techniques Spinacia oleracea Thermosynechococcus vulcanus preparations, we show that additional illumination...
Abstract Photosystem II (PSII) catalyses the oxidation of water through a four-step cycle S i states ( = 0–4) at Mn 4 CaO 5 cluster 1–3 , during which an extra oxygen (O6) is incorporated 3 state to form possible dioxygen 4–7 . Structural changes metal and its environment S-state transitions have been studied on microsecond timescale. Here we use pump-probe serial femtosecond crystallography reveal structural dynamics PSII from nanoseconds milliseconds after illumination with one flash (1F)...
Light-harvesting complexes (LHCs) are diversified among photosynthetic organisms, and the structure of photosystem I-LHC (PSI-LHCI) supercomplex has been shown to be variable depending on species organisms. However, structural evolutionary correlations red-lineage LHCs unknown. Here, we determined a 1.92-Å resolution cryoelectron microscopic PSI-LHCI isolated from red alga Cyanidium caldarium RK-1 (NIES-2137), which is an important taxon in Cyanidiophyceae. We subsequently investigated...
Marine photosynthetic dinoflagellates are a group of successful phytoplankton that can form red tides in the ocean and also symbiosis with corals. These features closely related to properties dinoflagellates. We report here three structures photosystem I (PSI)–chlorophylls (Chls) / c -peridinin protein complex (PSI–AcpPCI) from two species by single-particle cryoelectron microscopy. The crucial PsaA/B subunits tidal dinoflagellate Amphidinium carterae remarkably smaller hence losing over 20...
Cytochrome c-550, a low-potential c-type cytochrome, and 12-kDa protein were recently shown to be associated extrinsically stoichiometrically with purified photosystem II (PSII) complex of the thermophilic cyanobacterium Synechococcus vulcanus [Shen, J.-R., Ikeuchi, M., & Inoue, Y. (1992) FEBS Lett. 301, 145-149]. The binding functional properties these two extrinsic components in PSII studied by means release-reconstitution thermoluminescence techniques. following results obtained: (i) cyt...
The chloride ion, Cl − , is an essential cofactor for oxygen evolution of photosystem II (PSII) and closely associated with the Mn 4 Ca cluster. Its detailed location function have not been identified, however. We substituted a bromide ion (Br ) or iodide (I in PSII analyzed crystal structures Br I substitutions. Substitution did inhibit evolution, whereas substitution completely inhibited indicating efficient replacement by . substitutions were crystallized, their analyzed. results showed...
We introduce a quantum mechanics/molecular mechanics model of the oxygen-evolving complex photosystem II in S(1) Mn(4)(IV,III,IV,III) state, where Ca(2+) is bridged to manganese centers by carboxylate moieties D170 and A344 on basis new X-ray diffraction (XRD) recently reported at 1.9 Å resolution. The also consistent with high-resolution spectroscopic data, including polarized extended absorption fine structure data oriented single crystals. Our results provide refined intermetallic...
Full geometry optimizations of several inorganic model clusters, CaMn(4)O(4)XYZ(H(2)O)(2) (X, Y, Z = H(2)O, OH(-) or O(2-)), by the use B3LYP hybrid density functional theory (DFT) have been performed to illuminate plausible molecular structures catalytic site for water oxidation in S(0), S(1), S(2) and S(3) states Kok cycle oxygen-evolving complex (OEC) photosystem II (PSII). Optimized geometries obtained energy gradient method revealed degree symmetry breaking unstable three-center...
Significance Photosystem I (PSI) is one of the most efficient nanophotochemical machines in nature. To adapt to various environments, photosynthetic organisms developed different PSI structure during evolution from prokaryotic cyanobacteria higher plants. Red algae are primitive eukaryotic algae, and their apparatus represents a transitional state between eukaryotes. We determined two forms PSI-LHCR red alga by cryo-EM. Our results revealed unique features energy transfer pathways algal...
Oxygen-evolving complex of photosystem II (PSII) is a tetra-manganese calcium penta-oxygenic cluster (Mn4CaO5) catalyzing light-induced water oxidation through several intermediate states (S-states) by mechanism that not fully understood. To elucidate the roles Ca(2+) in this and possible location substrates process, we crystallized Sr(2+)-substituted PSII from Thermosynechococcus vulcanus, analyzed its crystal structure at resolution 2.1 Å, compared it with 1.9 Å native PSII. Our analysis...