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Photosynthetic water oxidation by Photosystem II (PSII) is a fascinating process because it sustains life on Earth and serves as a blue print for scalable synthetic catalysts required for renewable energy applications. The biophysical, computational, and structural description of this process, which started more than 50 years ago, has made tremendous progress over the past two decades, with its high-resolution crystal structures being available not only of the dark-stable state of PSII, but of all the semi-stable reaction intermediates and even some transient states. Here, we summarize the current knowledge on PSII with emphasis on the basic principles that govern the conversion of light energy to chemical energy in PSII, as well as on the illustration of the molecular structures that enable these reactions. The important remaining questions regarding the mechanism of biological water oxidation are highlighted, and one possible pathway for this fundamental reaction is described at a molecular level.

The physics and chemistry of liquid solutions play a central role in science, and our understanding of life on Earth. Unfortunately, key tools for interrogating aqueous systems, such as infrared and soft X-ray spectroscopy, cannot readily be applied because of strong absorption in water. Here we use gas-dynamic forces to generate free-flowing, sub-micron, liquid sheets which are two orders of magnitude thinner than anything previously reported. Optical, infrared, and X-ray spectroscopies are used to characterize the sheets, which are found to be tunable in thickness from over 1 μm  down to less than 20 nm, which corresponds to fewer than 100 water molecules thick. At this thickness, aqueous sheets can readily transmit photons across the spectrum, leading to potentially transformative applications in infrared, X-ray, electron spectroscopies and beyond. The ultrathin sheets are stable for days in vacuum, and we demonstrate their use at free-electron laser and synchrotron light sources. X-ray spectroscopy is a tool used for the investigation of aqueous solutions but the strong absorption of water means that very thin liquid sheets are needed for accurate analysis. Here the authors produce free-flowing liquid sheets 2 orders of magnitude thinner than sheets obtained with existing techniques.

Photosystem II (PSII) catalyzes the first light-dependent step in photosynthesis. An improved structural model of a cyanobacterial PSII provides complete assignment of all subunits in the complex and reveals possible channels used for the transport of protons, oxygen and water to the thylakoid lumen. Photosystem II (PSII) is a large homodimeric protein–cofactor complex located in the photosynthetic thylakoid membrane that acts as light-driven water:plastoquinone oxidoreductase. The crystal structure of PSII from Thermosynechococcus elongatus at 2.9-Å resolution allowed the unambiguous assignment of all 20 protein subunits and complete modeling of all 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer. The presence of a third plastoquinone Q C and a second plastoquinone-transfer channel, which were not observed before, suggests mechanisms for plastoquinol-plastoquinone exchange, and we calculated other possible water or dioxygen and proton channels. Putative oxygen positions obtained from a Xenon derivative indicate a role for lipids in oxygen diffusion to the cytoplasmic side of PSII. The chloride position suggests a role in proton-transfer reactions because it is bound through a putative water molecule to the Mn 4 Ca cluster at a distance of 6.5 Å and is close to two possible proton channels.

First light The first step of photosynthesis in plants, algae and cyanobacteria is the activation of photosystem II, a large protein-cofactor complex embedded in the chloroplast membrane. Although several medium-resolution X-ray crystal structures of this complex exist, a new structure published this week shows previously unseen cofactors in close company with photosystem II, and reveals details of the geometry and coordination of the Mn 4 Ca cluster, where the oxidation of water occurs. Oxygenic photosynthesis in plants, algae and cyanobacteria is initiated at photosystem II, a homodimeric multisubunit protein–cofactor complex embedded in the thylakoid membrane 1 . Photosystem II captures sunlight and powers the unique photo-induced oxidation of water to atmospheric oxygen 1 , 2 . Crystallographic investigations of cyanobacterial photosystem II have provided several medium-resolution structures (3.8 to 3.2 Å) 3 , 4 , 5 , 6 that explain the general arrangement of the protein matrix and cofactors, but do not give a full picture of the complex. Here we describe the most complete cyanobacterial photosystem II structure obtained so far, showing locations of and interactions between 20 protein subunits and 77 cofactors per monomer. Assignment of 11 β-carotenes yields insights into electron and energy transfer and photo-protection mechanisms in the reaction centre and antenna subunits. The high number of 14 integrally bound lipids reflects the structural and functional importance of these molecules for flexibility within and assembly of photosystem II. A lipophilic pathway is proposed for the diffusion of secondary plastoquinone that transfers redox equivalents from photosystem II to the photosynthetic chain. The structure provides information about the Mn 4 Ca cluster, where oxidation of water takes place. Our study uncovers near-atomic details necessary to understand the processes that convert light to chemical energy.

Hamstring injuries are associated with decreased hamstring strength. Matinlauri et al.’s 90:20 Isometric Posterior Chain Test (90:20 IPCT) efficiently assesses hamstring strength, but has not been validated so far. Furthermore, their rather unprecise original instruction allows high variability in test execution. We added a new instruction and variables and examined, whether this measure leads to increased reliability and validity. We assessed hamstring strength of 23 sport students via the 90:20 IPCT under the original instruction, to exert vertical force, and our new instruction, to exert vertical and horizontal force. Instead of only using bare vertical force as variable under the original (Fz_V) and our new instruction (Fz_VH), we also calculated the resultant force (Fres_VH) and the applied torque onto the force place (M_F_ortho_VH). To test for validity, we correlated the outcome variables with peak torque of gold standard dynamometry. Furthermore, we measured muscle activities of the mm. rectus femoris, biceps femoris, semitendinosus, and gluteus maximus under our new instruction and compared them to those under the original variable (Fz_V) via one sample t-tests. To evaluate reliability, tests were repeated on two separate days, for which we calculated intra class correlation coefficients (ICCs) and coefficients of variation (CVs). Our new instruction and variables (Fz_VH, Fres_VH, M_F_ortho_VH) showed better validity (mean r = 0.77, r = 0.81, and r = 0.85) and equally good or better reliability (ICCs: 0.87, 0.89, and 0.94; CVs: 4.7%, 4.1%, and 4.7%) than the original instruction and variable (Fz_V) (mean r = 0.70; ICC: 0.91; CV: 5.6%). There were no differences in muscle activities between the variables and instructions of the 90:20 IPCT. We recommend our new instruction and the applied torque onto the force plate as it makes the 90:20 IPCT a more reliable and valid tool to assess hamstring strength.

Hamstring strain injuries are a prevalent burden in soccer. Low strength, muscle fatigue, and inter-limb differences in hamstring strength are associated with hamstring injury risk. Previous research shows increased hamstring injury incidence in soccer at the end of each half or the end of the match, respectively. This study aims at evaluating the aforementioned risk factors of hamstring injury over the course of a simulated soccer match. Ten active soccer players carried out the Loughborough Intermittent Shuttle Test, during which hamstring strength of both legs was assessed on seven occasions via the optimized 90:20 Isometric Posterior Chain Test. Hamstring strength of each limb and inter-limb differences in hamstring strength over the course of the Loughborough Intermittent Shuttle Test were parameters of interest. Repeated measures ANOVA were used to analyze the development of hamstring strength and limb-asymmetries in hamstring strength during the simulated soccer match. Compared to pre-match values, hamstring strength was significantly decreased after 15 and 30 minutes of simulated soccer match for the non-dominant and dominant leg, respectively. There were no further variations in hamstring strength within the simulated soccer match for either leg. We did neither measure significant recovery of hamstring strength to pre-match values at the beginning of the second half, as suspected by previous research, nor inter-limb differences, or a deterioration of limb asymmetries in hamstring strength during the simulated soccer match. Players who only participate for a short period in a soccer match may be exposed to the same risk of suffering hamstring injury like players who compete for a longer duration. Decreasing hamstring strength partly depicts the pattern of hamstring injury incidences during soccer matches. Additional factors may influence the increasing hamstring injury rate at the end of each half or the later stages of a match, respectively.

In natural photosynthesis, the light-driven splitting of water into electrons, protons and molecular oxygen forms the first step of the solar-to-chemical energy conversion process. The reaction takes place in photosystem II, where the Mn 4 CaO 5 cluster first stores four oxidizing equivalents, the S 0 to S 4 intermediate states in the Kok cycle, sequentially generated by photochemical charge separations in the reaction center and then catalyzes the O–O bond formation chemistry 1 – 3 . Here, we report room temperature snapshots by serial femtosecond X-ray crystallography to provide structural insights into the final reaction step of Kok’s photosynthetic water oxidation cycle, the S 3 →[S 4 ]→S 0 transition where O 2 is formed and Kok’s water oxidation clock is reset. Our data reveal a complex sequence of events, which occur over micro- to milliseconds, comprising changes at the Mn 4 CaO 5 cluster, its ligands and water pathways as well as controlled proton release through the hydrogen-bonding network of the Cl1 channel. Importantly, the extra O atom O x , which was introduced as a bridging ligand between Ca and Mn1 during the S 2 →S 3 transition 4 – 6 , disappears or relocates in parallel with Y z reduction starting at approximately 700 μs after the third flash. The onset of O 2 evolution, as indicated by the shortening of the Mn1–Mn4 distance, occurs at around 1,200 μs, signifying the presence of a reduced intermediate, possibly a bound peroxide. Using serial femtosecond X-ray cystallography, we provide structural insights into the final reaction step of Kok’s photosynthetic water oxidation cycle, specifically the S 3 →[S 4 ]→S 0 transition where O 2 is formed.

Repetitive head impacts (RHI) from routine soccer (football) heading have been suggested to contribute to the long-term development of neurodegenerative disorders. However, scientific evidence concerning the actual risk of these RHI on brain health remains inconclusive. Moreover, female athletes-despite a presumably increased vulnerability toward the effects of RHI-are largely underrepresented in previous approaches. Therefore, our aim was to prospectively investigate the effects of heading on cognitive and sensorimotor performances, health perception, and concussion symptoms in semi-professional female soccer players. An extensive test battery was used to assess cognitive and sensorimotor performances as well as health status (SF-36) and concussion symptoms (SCAT3) of a total of 27 female soccer players (22.2 ± 4.2 years) and 15 control subjects (23.2 ± 3.0 years) before and after one-and-a-half years. Throughout this period, soccer players' heading exposure was determined using video analysis. Subgroup comparisons (control [ = 12], low exposure [ = 7], high exposure [ = 8]) showed no time-dependent differences in SF-36 or SCAT3 scores. Similarly, across most behavioral tests, soccer players' performances evolved equally or more favorably as compared to the control subjects. However, there were significant effects pointing toward slightly negative consequences of heading on aspects of fine motor control ( = 0.001), which were confirmed by correlation and multiple regression analyses. The latter, further, yielded indications for a relationship between heading exposure and negative alterations in postural control ( = 0.002). Our findings do not provide evidence for negative effects of soccer heading on female players' health perception, concussion symptoms, and cognitive performances over the course of one-and-a-half years. However, we found subtle negative alterations in fine motor and postural control that could be attributed to heading exposure. Other factors, like the number of previous head injuries, were not linked to the observed changes. Given the reduction of our initial sample size due to player fluctuation, the results need to be interpreted with caution and validated in larger-scale studies. These should not only focus on cognitive outcomes but also consider sensorimotor changes as a result of RHI from soccer heading.

One of the reasons for the high efficiency and selectivity of biological catalysts arise from their ability to control the pathways of substrates and products using protein channels, and by modulating the transport in the channels using the interaction with the protein residues and the water/hydrogen-bonding network. This process is clearly demonstrated in Photosystem II (PS II), where its light-driven water oxidation reaction catalyzed by the Mn 4 CaO 5 cluster occurs deep inside the protein complex and thus requires the transport of two water molecules to and four protons from the metal center to the bulk water. Based on the recent advances in structural studies of PS II from X-ray crystallography and cryo-electron microscopy, in this review we compare the channels that have been proposed to facilitate this mass transport in cyanobacteria, red and green algae, diatoms, and higher plants. The three major channels (O1, O4, and Cl1 channels) are present in all species investigated; however, some differences exist in the reported structures that arise from the different composition and arrangement of membrane extrinsic subunits between the species. Among the three channels, the Cl1 channel, including the proton gate, is the most conserved among all photosynthetic species. We also found at least one branch for the O1 channel in all organisms, extending all the way from Ca/O1 via the ‘water wheel’ to the lumen. However, the extending path after the water wheel varies between most species. The O4 channel is, like the Cl1 channel, highly conserved among all species while having different orientations at the end of the path near the bulk. The comparison suggests that the previously proposed functionality of the channels in T. vestitus (Ibrahim et al., Proc Natl Acad Sci USA 117:12624–12635, 2020; Hussein et al., Nat Commun 12:6531, 2021) is conserved through the species, i.e. the O1-like channel is used for substrate water intake, and the tighter Cl1 and O4 channels for proton release. The comparison does not eliminate the potential role of O4 channel as a water intake channel. However, the highly ordered hydrogen-bonded water wire connected to the Mn 4 CaO 5 cluster via the O4 may strongly suggest that it functions in proton release, especially during the S 0  → S 1 transition (Saito et al., Nat Commun 6:8488, 2015; Kern et al., Nature 563:421–425, 2018; Ibrahim et al., Proc Natl Acad Sci USA 117:12624–12635, 2020; Sakashita et al., Phys Chem Chem Phys 22:15831–15841, 2020; Hussein et al., Nat Commun 12:6531, 2021).

Light-driven oxidation of water to molecular oxygen is catalyzed by the oxygen-evolving complex (OEC) in Photosystem II (PS II). This multi-electron, multi-proton catalysis requires the transport of two water molecules to and four protons from the OEC. A high-resolution 1.89 Å structure obtained by averaging all the S states and refining the data of various time points during the S 2 to S 3 transition has provided better visualization of the potential pathways for substrate water insertion and proton release. Our results indicate that the O1 channel is the likely water intake pathway, and the Cl1 channel is the likely proton release pathway based on the structural rearrangements of water molecules and amino acid side chains along these channels. In particular in the Cl1 channel, we suggest that residue D1-E65 serves as a gate for proton transport by minimizing the back reaction. The results show that the water oxidation reaction at the OEC is well coordinated with the amino acid side chains and the H-bonding network over the entire length of the channels, which is essential in shuttling substrate waters and protons. The oxygen-evolving complex in Photosystem II (PSII) catalyzes the light-driven oxidation of water to oxygen and it is still under debate how the water reaches the active site. Here, the authors analyse time-resolved XFEL-based crystal structures of PSII that were determined at room temperature and report the structures of the waters in the putative channels surrounding the active site at various time-points during the reaction cycle and conclude that the O1 channel is the likely water intake pathway and the Cl1 channel the likely proton release pathway.