Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain.

Photosystem I (PS I) is a light-driven oxidoreductase responsible for converting photons into chemical bond energy. Its application for renewable energy was revolutionized by the creation of the MenB deletion (Δ) variant in the cyanobacterium sp. PCC 6803, in which phylloquinone is replaced by plastoquinone-9 with a low binding affinity.

Bicarbonate is a key regulator but not a substrate for O evolution in Photosystem II.

Photosystem II (PSII) uses light energy to oxidize water and to reduce plastoquinone in the photosynthetic electron transport chain. O is produced as a byproduct. While most members of the PSII research community agree that O originates from water molecules, alternative hypotheses involving bicarbonate persist in the literature.

Revisiting the Preparation and Catalytic Performance of a Phosphine-Modified Co(II) Hydroformylation Precatalyst.

In light of recent conflicting reports regarding the hydroformylation catalytic activity derived from cationic Co(II) precatalysts of the form [Co(acac)(bis(phosphine))]BF, the synthetic procedures and characterization of [Co(acac)(dppBz)]BF, , are evaluated. Leveraging calibrated ESI-TOF MS methodologies, substantial quantities of Co(acac)(dppBz), , were observed within samples of . The source of the impurity, , is determined to derive from incomplete protonolysis of the Co(acac) precursor and ligand scrambling occurring during the synthesis of .

Assembly and Repair of Photosystem II in .

Oxygenic photosynthetic organisms use Photosystem II (PSII) to oxidize water and reduce plastoquinone. Here, we review the mechanisms by which PSII is assembled and turned over in the model green alga . This species has been used to make key discoveries in PSII research due to its metabolic flexibility and amenability to genetic approaches.

Conformational changes in a Photosystem II hydrogen bond network stabilize the oxygen-evolving complex.

The MnCaO oxygen-evolving complex (OEC) in Photosystem II (PSII) is assembled in situ and catalyzes water oxidation. After OEC assembly, the PsbO extrinsic subunit docks to the lumenal face of PSII and both stabilizes the OEC and facilitates efficient proton transfer to the lumen. D1 residue R334 is part of a hydrogen bond network involved in proton release during catalysis and interacts directly with PsbO.

Cationic Cobalt(II) Bisphosphine Hydroformylation Catalysis: In Situ Spectroscopic and Reaction Studies.

[HCo(CO)(bisphosphine)](BF), = 1-3, is a highly active hydroformylation catalyst system, especially for internal branched alkenes. In situ infrared spectroscopy (IR), electron paramagnetic resonance (EPR), and nuclear magnetic resonance studies support the proposed catalyst formulation. IR studies reveal the formation of a dicationic Co(I) paramagnetic CO-bridged dimer, [Co(μ-CO)(CO)(bisphosphine)], at lower temperatures formed from the reaction of two catalyst complexes via the elimination of H.

A low-cost and realistic noisy light system for studying photosynthesis.

Unlike the light conditions commonly used to grow photosynthetic organisms in the research laboratory, the light intensity in real environments is dynamic. A simple and low-cost system is described in which a commercial dimmable LED panel is controlled to simulate a sinusoidal function representing daylight hours and overlaid with stochastic shading events. The output closely resembles light intensity measurements on Earth's surface on partly cloudy days or in lower levels of plant canopies.

Chloride facilitates Mn(III) formation during photoassembly of the Photosystem II oxygen-evolving complex.

The MnCa oxygen-evolving complex (OEC) in Photosystem II (PSII) is assembled in situ from free Mn, Ca, and water. In an early light-driven step, Mn in a protein high-affinity site is oxidized to Mn. Using dual-mode electron paramagnetic resonance spectroscopy, we observed that Mn accumulation increases as chloride concentration increases in spinach PSII membranes depleted of all extrinsic subunits.

Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls d and f.

Far-red light (FRL) photoacclimation in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700-800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light.

Highly active cationic cobalt(II) hydroformylation catalysts.

The cobalt complexes HCo(CO) and HCo(CO)(PR) were the original industrial catalysts used for the hydroformylation of alkenes through reaction with hydrogen and carbon monoxide to produce aldehydes. More recent and expensive rhodium-phosphine catalysts are hundreds of times more active and operate under considerably lower pressures. Cationic cobalt(II) bisphosphine hydrido-carbonyl catalysts that are far more active than traditional neutral cobalt(I) catalysts and approach rhodium catalysts in activity are reported here.

The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.

The nucleotide binding protein 35 (Nbp35)/cytosolic Fe-S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe-S cluster assembly scaffold required for the maturation of Fe-S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe-S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe-4S] cluster that can be transferred to a [4Fe-4S] apoprotein.

Insights into Proton-Transfer Pathways during Water Oxidation in Photosystem II.

Water oxidation by photosystem II (PSII) involves the release of O, electrons, and protons at the oxygen-evolving complex (OEC). These processes are facilitated by a hydrogen-bonded network of amino acid residues and waters surrounding the OEC. It is crucial to probe the proton-transfer pathways from the OEC as proton release helps to maintain the charge balance required for efficient water oxidation.

Photosystem II oxygen-evolving complex photoassembly displays an inverse H/D solvent isotope effect under chloride-limiting conditions.

Photosystem II (PSII) performs the solar-driven oxidation of water used to fuel oxygenic photosynthesis. The active site of water oxidation is the oxygen-evolving complex (OEC), a MnCaO cluster. PSII requires degradation of key subunits and reassembly of the OEC as frequently as every 20 to 40 min.

Thylakoid localized bestrophin-like proteins are essential for the CO concentrating mechanism of .

The green alga possesses a CO concentrating mechanism (CCM) that helps in successful acclimation to low CO conditions. Current models of the CCM postulate that a series of ion transporters bring HCO from outside the cell to the thylakoid lumen, where the carbonic anhydrase 3 (CAH3) dehydrates accumulated HCO to CO, raising the CO concentration for Ribulose bisphosphate carboxylase/oxygenase (Rubisco). Previously, HCO transporters have been identified at both the plasma membrane and the chloroplast envelope, but the transporter thought to be on the thylakoid membrane has not been identified.

Desiccation tolerant lichens facilitate in vivo H/D isotope effect measurements in oxygenic photosynthesis.

We have used the desiccation-tolerant lichen Flavoparmelia caperata, containing the green algal photobiont Trebouxia gelatinosa, to examine H/D isotope effects in Photosystem II in vivo. Artifact-free H/D isotope effects on both PSII primary charge separation and water oxidation yields were determined as a function of flash rate from chlorophyll-a variable fluorescence yields. Intact lichens could be reversibly dehydrated/re-hydrated with HO/DO repeatedly without loss of O evolution, unlike all isolated PSII preparations.

Iron and Cobalt Diazoalkane Complexes Supported by β-Diketiminate Ligands: A Synthetic, Spectroscopic, and Computational Investigation.

Diazoalkanes are interesting redox-active ligands and also precursors to carbene fragments. We describe a systematic study of the binding and electronic structure of diphenyldiazomethane complexes of β-diketiminate supported iron and cobalt, which span a range of formal d-electron counts of 7-9. In end-on diazoalkane complexes of formally monovalent three-coordinate transition metals, the electronic structures are best described as having the metal in the +2 oxidation state with an antiferromagnetically coupled radical anion diazoalkane as shown by crystallography, spectroscopy, and computations.

Endothelial Cell Autonomous Role of Akt1: Regulation of Vascular Tone and Ischemia-Induced Arteriogenesis.

Objective: The importance of PI3K/Akt signaling in the vasculature has been demonstrated in several models, as global loss of Akt1 results in impaired postnatal ischemia- and VEGF-induced angiogenesis. The ubiquitous expression of Akt1, however, raises the possibility of cell-type-dependent Akt1-driven actions, thereby necessitating tissue-specific characterization.

Approach And Results: Herein, we used an inducible, endothelial-specific Akt1-deleted adult mouse model (Akt1iECKO) to characterize the endothelial cell autonomous functions of Akt1 in the vascular system.

A full set of iridium(iv) pyridine-alkoxide stereoisomers: highly geometry-dependent redox properties.

We introduce and characterize the complete set of possible isomers of Ir(pyalk)Cl (pyalk = 2-(pyridin-2-yl)propan-2-oate), providing valuable insights on the properties of Ir(iv) species. The pyridine alkoxide ligand strongly stabilizes high oxidation states, essential to accessing the catalytically relevant Ir(iv) state, and results in robust complexes that can be handled under ambient conditions, even permitting chromatographic separation. The redox properties are isomer-dependent, spanning a 300 mV range, rationalized with ligand-field theory and DFT calculations.

Progress Toward a Molecular Mechanism of Water Oxidation in Photosystem II.

The active site of photosynthetic water oxidation is the oxygen-evolving complex (OEC) in the photosystem II (PSII) reaction center. The OEC is a MnCaO cluster embedded in the PSII protein matrix, and it cycles through redox intermediates known as S states (i = 0-4). Significant progress has been made in understanding the inorganic and physical chemistry of states S-S through experiment and theory.

Slow Equilibration between Spectroscopically Distinct Trap States in Reduced TiO Nanoparticles.

Understanding the nature of charge carriers in nanoscale titanium dioxide is important for its use in solar energy conversion, photocatalysis, and other applications. UV-irradiation of aqueous, colloidal TiO nanoparticles in the presence of methanol gives highly reduced suspensions. Two distinct types of electron traps were observed and characterized by EPR and optical spectroscopies.

Energetics of the S State Spin Isomers of the Oxygen-Evolving Complex of Photosystem II.

The S redox intermediate of the oxygen-evolving complex in photosystem II is present as two spin isomers. The S = 1/2 isomer gives rise to a multiline electron paramagnetic resonance (EPR) signal at g = 2.0, whereas the S = 5/2 isomer exhibits a broad EPR signal at g = 4.

Mechanistic Study of an Improved Ni Precatalyst for Suzuki-Miyaura Reactions of Aryl Sulfamates: Understanding the Role of Ni(I) Species.

Nickel precatalysts are potentially a more sustainable alternative to traditional palladium precatalysts for the Suzuki-Miyaura coupling reaction. Currently, there is significant interest in Suzuki-Miyaura coupling reactions involving readily accessible phenolic derivatives such as aryl sulfamates, as the sulfamate moiety can act as a directing group for the prefunctionalization of the aromatic backbone of the electrophile prior to cross-coupling. By evaluating complexes in the Ni(0), (I), and (II) oxidation states we report a precatalyst, (dppf)Ni(o-tolyl)(Cl) (dppf = 1,1'-bis(diphenylphosphino)ferrocene), for Suzuki-Miyaura coupling reactions involving aryl sulfamates and boronic acids, which operates at a significantly lower catalyst loading and at milder reaction conditions than other reported systems.

A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.

The sulfur-containing nucleosides in transfer RNA (tRNAs) are present in all three domains of life; they have critical functions for accurate and efficient translation, such as tRNA structure stabilization and proper codon recognition. The tRNA modification enzymes ThiI (in bacteria and archaea) and Ncs6 (in archaea and eukaryotic cytosols) catalyze the formation of 4-thiouridine (sU) and 2-thiouridine (sU), respectively. The ThiI homologs were proposed to transfer sulfur via cysteine persulfide enzyme adducts, whereas the reaction mechanism of Ncs6 remains unknown.

Ammonia Binding in the Second Coordination Sphere of the Oxygen-Evolving Complex of Photosystem II.

Ammonia binds to two sites in the oxygen-evolving complex (OEC) of Photosystem II (PSII). The first is as a terminal ligand to Mn in the S2 state, and the second is at a site outside the OEC that is competitive with chloride. Binding of ammonia in this latter secondary site results in the S2 state S = (5)/2 spin isomer being favored over the S = (1)/2 spin isomer.

S3 State of the O2-Evolving Complex of Photosystem II: Insights from QM/MM, EXAFS, and Femtosecond X-ray Diffraction.

The oxygen-evolving complex (OEC) of photosystem II has been studied in the S3 state by electron paramagnetic resonance, extended X-ray absorption fine structure (EXAFS), and femtosecond X-ray diffraction (XRD). However, the actual structure of the OEC in the S3 state has yet to be established. Here, we apply hybrid quantum mechanics/molecular mechanics methods and propose a structural model that is consistent with EXAFS and XRD.