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Accounts of Chemical Research Mar 2024ConspectusAn understanding of the mechanistic processes that underpin reactions catalyzed by 3d transition metals is vital for their development as potential...
ConspectusAn understanding of the mechanistic processes that underpin reactions catalyzed by 3d transition metals is vital for their development as potential replacements for scarce platinum group metals. However, this is a significant challenge because of the tendency of 3d metals to undergo mechanistically diverse pathways when compared with their heavier congeners, often as a consequence of one-electron transfer reactions and/or intrinsically weaker metal-ligand bonds. We have developed and implemented a new methodology to illuminate the pathways that underpin C-H bond functionalization pathways in reactions catalyzed by Mn-carbonyl compounds. By integrating measurements performed on catalytic reactions with in situ reaction monitoring and state-of-the-art ultrafast spectroscopic methods, unique insight into the mode of action and fate of the catalyst have been obtained.Using a combination of time-resolved spectroscopy and in situ low-temperature NMR studies, we have shown that photolysis of manganese-carbonyl precatalysts results in rapid (<5 ps) CO dissociation─the same process that occurs under thermal catalytic conditions. This enabled the detection of the key states relevant to catalysis, including solvent and alkyne complexes and their resulting transformation into manganacycles, which results from a migratory insertion reaction into the Mn-C bond. By systematic variation of the substrates (many of which are real-world structurally diverse substrates and not simple benchmark systems) and quantification of the resulting rate constants for the insertion step, a universal model for this migratory insertion process has been developed. The time-resolved spectroscopic method gave insight into fundamental mechanistic pathways underpinning other aspects of modern synthetic chemistry. The most notable was the first direct experimental observation of the concerted metalation deprotonation (CMD) mechanism through which carboxylate groups are able to mediate C-H bond activation at a metal center. This step underpins a host of important synthetic applications. This study demonstrated how the time-resolved multiple probe spectroscopy (TRPS) method enables the observation of mechanistic process occurring on time scales from several picoseconds through to μs in a single experiment, thereby allowing the sequential observation of solvation, ligand substitution, migratory insertion, and ultimate protonation of a Mn-C bond.These studies have been complemented by an investigation of the "in reaction flask" catalyst behavior, which has provided additional insight into new pathways for precatalyst activation, including evidence that alkyne C-H bond activation may occur before heterocycle activation. Crucial insight into the fate of the catalyst species showed that excess water played a key role in deactivation to give higher-order hydroxyl-bridged manganese carbonyl clusters, which were independently found to be inactive. Traditional in situ IR and NMR spectroscopic analysis on the second time scale bridges the gap to the analysis of real catalytic reaction systems. As a whole, this work has provided unprecedented insight into the processes underpinning manganese-catalyzed reactions spanning 16 orders of magnitude in time.
PubMed: 38412502
DOI: 10.1021/acs.accounts.3c00774 -
Structural Dynamics (Melville, N.Y.) Jan 2024A long-standing motivation driving high-speed electron microscopy development is to capture phase transformations and material dynamics in real time with high spatial...
A long-standing motivation driving high-speed electron microscopy development is to capture phase transformations and material dynamics in real time with high spatial and temporal resolution. Current dynamic transmission electron microscopes (DTEMs) are limited to nanosecond temporal resolution and the ability to capture only a few frames of a transient event. With the motivation to overcome these limitations, we present our progress in developing a streak-mode DTEM (SM-DTEM) and demonstrate the recovery of picosecond images with high frame sequence depth. We first demonstrate that a zero-dimensional (0D) SM-DTEM can provide temporal information on any local region of interest with a 0.37 m diameter, a 20-GHz sampling rate, and 1200 data points in the recorded trace. We use this method to characterize the temporal profile of the photoemitted electron pulse, finding that it deviates from the incident ultraviolet laser pulse and contains an unexpected peak near its onset. Then, we demonstrate a two-dimensional (2D) SM-DTEM, which uses compressed-sensing-based tomographic imaging to recover a full spatiotemporal photoemission profile over a 1.85-m-diameter field of view with nanoscale spatial resolution, 370-ps inter-frame interval, and 140-frame sequence depth in a 50-ns time window. Finally, a perspective is given on the instrumental modifications necessary to further develop this promising technique with the goal of decreasing the time to capture a 2D SM-DTEM dataset.
PubMed: 38406321
DOI: 10.1063/4.0000219 -
Micromachines Jan 2024Utilizing the principle of laser-induced periodic surface structures (LIPSSs), this research delves into the morphological evolution of single-crystal silicon surfaces...
Utilizing the principle of laser-induced periodic surface structures (LIPSSs), this research delves into the morphological evolution of single-crystal silicon surfaces irradiated by a near-infrared picosecond laser through a scanning mode. With the increase in laser energy density, the nanostructure morphology on single-crystal silicon surfaces induced by incident lasers with different polarization directions sequentially produces high spatial-frequency LIPSSs (HSFLs) with a period of 220 nm ± 10 nm parallel to the laser polarization, low spatial-frequency LIPSSs (LSFLs) with a period of 770 nm ± 85 nm perpendicular to the direction of the polarization, and groove structures. Furthermore, by varying the angle between the laser polarization and the scanning direction, the study examined the combined anisotropic effects of the laser polarization scanning direction angle and the laser polarization crystal orientation angle on the genesis of LIPSSs on single-crystal silicon (100) surfaces. The experiments revealed polarization-related anisotropic characteristics in the morphology of HSFLs. It was found that when the polarization angle approached 45°, the regularity of the LSFLs deteriorated, the modification width decreased, and the periodicity increased. This is critical for the precise control of the LSFLs' morphology.
PubMed: 38398929
DOI: 10.3390/mi15020200 -
Life (Basel, Switzerland) Feb 2024Nonlinear microscopy (NM) enables us to investigate the morphology or monitor the physiological processes of the skin through the use of ultrafast lasers. Fiber (or...
Nonlinear microscopy (NM) enables us to investigate the morphology or monitor the physiological processes of the skin through the use of ultrafast lasers. Fiber (or fiber-coupled) lasers are of great interest because they can easily be combined with a handheld, scanning nonlinear microscope. This latter feature greatly increases the utility of NM for pre-clinical applications and in vivo tissue imaging. Here, we present a fiber-coupled, sub-ps Ti-sapphire laser system being optimized for in vivo, stain-free, 3D imaging of skin alterations with a low thermal load of the skin. The laser is pumped by a low-cost, 2.1 W, 532 nm pump laser and delivers 0.5-1 ps, high-peak-power pulses at a ~20 MHz repetition rate. The spectral bandwidth of the laser is below 2 nm, which results in a low sensitivity for dispersion during fiber delivery. The reduction in the peak intensity due to the increased pulse duration is compensated by the lower repetition rate of our laser. In our proof-of-concept imaging experiments, a ~1.8 m long, commercial hollow-core photonic bandgap fiber was used for fiber delivery. Fresh and frozen skin biopsies of different skin alterations (e.g., adult hemangioma, basal cell cancer) and an unaffected control were used for high-quality, two-photon excitation fluorescence microscopy (2PEF) and second-harmonic generation (SHG) z-stack (3D) imaging.
PubMed: 38398740
DOI: 10.3390/life14020231 -
Science Advances Feb 2024Photosystem II (PSII) is an integral part of the photosynthesis machinery, in which several light-harvesting complexes rely on inter-complex excitonic energy transfer...
Photosystem II (PSII) is an integral part of the photosynthesis machinery, in which several light-harvesting complexes rely on inter-complex excitonic energy transfer (EET) processes to channel energy to the reaction center. In this paper, we report on a direct observation of the inter-complex EET in a minimal PSII supercomplex from plants, containing the trimeric light-harvesting complex II (LHCII), the monomeric light-harvesting complex CP26, and the monomeric PSII core complex. Using two-dimensional (2D) electronic spectroscopy, we measure an inter-complex EET timescale of 50 picoseconds for excitations from the LHCII-CP26 peripheral antenna to the PSII core. The 2D electronic spectra also reveal that the transfer timescale is nearly constant over the pump spectrum of 600 to 700 nanometers. Structure-based calculations reveal the contribution of each antenna complex to the measured inter-complex EET time. These results provide a step in elucidating the full inter-complex energy transfer network of the PSII machinery.
Topics: Photosystem II Protein Complex; Chlorophyll; Photosynthesis; Thylakoids; Plants; Energy Transfer
PubMed: 38394196
DOI: 10.1126/sciadv.adh0911 -
Frontiers in Medicine 2024This work demonstrates significant advantages in ophthalmic surgeries through the use of picosecond ultrashort laser pulses instead of state-of-the-art nanosecond laser...
PURPOSE
This work demonstrates significant advantages in ophthalmic surgeries through the use of picosecond ultrashort laser pulses instead of state-of-the-art nanosecond laser pulses. These ultrashort lasers shall serve as universal tools more effectively combining advantages of high precision, low impact and economic advantages compared to existing instruments.
METHODS
As samples, we used post-mortem porcine eyes on which we performed the experiments with both picosecond and nanosecond lasers. Performed surgeries were laser iridotomy, (post-) cataract treatment/capsulotomy and selective laser-trabeculoplasty. Pulse widths were between 12 ps and 220 ns with pulse energies between 30 μJ and 10 mJ at 532 nm and 1,064 nm. Additionally, we investigated accompanying shock waves, cavitation bubbles, and heat effects during the ablation processes.
RESULTS
For all surgeries, significant differences were observed between picosecond and nanosecond pulses: It was possible to scale the pulse energy down to 10 of microjoules rather than requiring millijoules, and resulting tissue ablations are much more precise, more deterministic and less frayed. The shock wave and cavitation bubble investigation revealed major differences in pressure between picosecond pulses (0.25 MPa, 50 μJ) and nanosecond pulses (37 MPa, 5 mJ). The heat input during ablation could be lowered by two orders of magnitude.
CONCLUSION
Picosecond ultrashort laser pulses show substantial benefits for several ophthalmic surgeries, with regard to ablation precision, shock wave generation and heat input. They are better than state-of-the-art ophthalmic nanosecond lasers in all aspects tested.
PubMed: 38390574
DOI: 10.3389/fmed.2024.1345976 -
The Journal of Physical Chemistry... Feb 2024NMR chemical shifts provide a sensitive probe of protein structure and dynamics but remain challenging to predict and interpret. We examine the effect of protein... (Review)
Review
NMR chemical shifts provide a sensitive probe of protein structure and dynamics but remain challenging to predict and interpret. We examine the effect of protein conformational distributions on N chemical shifts for dihydrofolate reductase (DHFR), comparing QM/MM predicted shifts with experimental shifts in solution as well as frozen distributions. Representative snapshots from MD trajectories exhibit variation in predicted N chemical shifts of up to 25 ppm. The average over the fluctuations is in significantly better agreement with room temperature solution experimental values than the prediction for any single optimal conformations. Meanwhile, solid-state NMR (SSNMR) measurements of frozen solutions at 105 K exhibit broad lines whose widths agree well with the widths of distributions of predicted shifts for samples from the trajectory. The backbone torsion angle ψ varies over 60° on the picosecond time scale, compensated by φ. These fluctuations can explain much of the shift variation.
Topics: Temperature; Protein Conformation; Magnetic Resonance Spectroscopy; Proteins; Magnetic Resonance Imaging; Nuclear Magnetic Resonance, Biomolecular
PubMed: 38381862
DOI: 10.1021/acs.jpclett.3c02589 -
Accounts of Chemical Research Mar 2024ConspectusMass spectrometry is a powerful analytical method capable of identifying compounds given a minute amount of material. The fragmentation pattern that results...
ConspectusMass spectrometry is a powerful analytical method capable of identifying compounds given a minute amount of material. The fragmentation pattern that results following molecular activation serves as a fingerprint that can be matched to a database compound for identification. Over the past half century, studies have addressed and, in many cases, named the chemical reactions that lead to some of the principal fragment ions. Theories have been developed to predict the observed fragmentation patterns, many of which assume that energy redistributes prior to dissociation. However, the existence of rearrangements and nonergodic processes complicates the prediction of fragmentation patterns and the identification of compounds that have yet to be entered into a curated database. To date, very few studies have addressed the time-dependent nature of the fragmentation of radical cations and, in particular, processes occurring with picosecond or shorter time scales where one expects to find nonergodic reactions.This Account focuses on a novel approach that enables tracking of molecular fragmentation in electron-ionization mass spectrometry with ultrafast time resolution. The two challenges that have prevented the time-resolved studies following electron ionization are the random impact parameter and moment of ionization of each molecule. In addition, medium-sized molecules can produce fragmentation patterns with tens if not hundreds of product ions. Spectroscopically interrogating all of these ions as a function of time is another major challenge. We describe strong field disruptive probing, a method that ionizes molecules on a femtosecond time scale and allows us to track in time the formation of all fragment ions simultaneously.Molecular fragmentation following ionization can occur on a very wide range of time scales. Metastable ions can survive from nanoseconds to microseconds; reactions that depend on vibrational energy redistribution can take picoseconds to nanoseconds; and direct dissociation processes and some rearrangements can take place in femtoseconds to picoseconds. All of these processes depend on the dynamics that occur during attoseconds and femtoseconds following the ionization process. Following a discussion of these time scales, we provide three examples of fragmentations that have been studied with femtosecond time resolution. Each of these examples include unforeseen reaction dynamics that involve a nonergodic process, highlighting the importance of time resolution in mass spectrometry. Finally, we explore future challenges and unresolved questions in mass spectrometry and, more broadly, in the domain of electron-initiated chemical reactions.
PubMed: 38366970
DOI: 10.1021/acs.accounts.3c00713 -
Chemical Science Feb 2024The separation and anti-fouling performance of water purification membranes is governed by both macroscopic and molecular-scale water properties near polymer surfaces....
The separation and anti-fouling performance of water purification membranes is governed by both macroscopic and molecular-scale water properties near polymer surfaces. However, even for poly(ethylene oxide) (PEO) - ubiquitously used in membrane materials - there is little understanding of whether or how the molecular structure of water near PEO surfaces affects macroscopic water diffusion. Here, we probe both time-averaged bulk and local water dynamics in dilute and concentrated PEO solutions using a unique combination of experimental and simulation tools. Pulsed-Field Gradient NMR and Overhauser Dynamic Nuclear Polarization (ODNP) capture water dynamics across micrometer length scales in sub-seconds to sub-nanometers in tens of picoseconds, respectively. We find that classical models, such as the Stokes-Einstein and Mackie-Meares relations, cannot capture water diffusion across a wide range of PEO concentrations, but that free volume theory can. Our study shows that PEO concentration affects macroscopic water diffusion by enhancing the water structure and altering free volume. ODNP experiments reveal that water diffusivity near PEO is slower than in the bulk in dilute solutions, previously not recognized by macroscopic transport measurements, but the two populations converge above the polymer overlap concentration. Molecular dynamics simulations reveal that the reduction in water diffusivity occurs with enhanced tetrahedral structuring near PEO. Broadly, we find that PEO does not simply behave like a physical obstruction but directly modifies water's structural and dynamic properties. Thus, even in simple PEO solutions, molecular scale structuring and the impact of polymer interfaces is essential to capturing water diffusion, an observation with important implications for water transport through structurally complex membrane materials.
PubMed: 38362435
DOI: 10.1039/d3sc05377f -
Communications Chemistry Feb 2024Peptides or proteins containing small biomolecular aggregates, such as micelles, bicelles, droplets and nanodiscs, are pivotal in many fields ranging from structural...
Peptides or proteins containing small biomolecular aggregates, such as micelles, bicelles, droplets and nanodiscs, are pivotal in many fields ranging from structural biology to pharmaceutics. Monitoring dynamics of such systems has been limited by the lack of experimental methods that could directly detect their fast (picosecond to nanosecond) timescale dynamics. Spin relaxation times from NMR experiments are sensitive to such motions, but their interpretation for biomolecular aggregates is not straightforward. Here we show that the dynamic landscape of peptide-containing molecular assemblies can be determined by a synergistic combination of solution state NMR experiments and molecular dynamics (MD) simulations. Solution state NMR experiments are straightforward to implement without an excessive amount of sample, while direct combination of spin relaxation data to MD simulations enables interpretation of dynamic landscapes of peptides and other aggregated molecules. To demonstrate this, we interpret NMR data from transmembrane, peripheral, and tail anchored peptides embedded in micelles. Our results indicate that peptides and detergent molecules do not rotate together as a rigid body, but peptides rotate in a viscous medium composed of detergent micelle. Spin relaxation times also provide indirect information on peptide conformational ensembles. This work gives new perspectives on peptide dynamics in complex biomolecular assemblies.
PubMed: 38351219
DOI: 10.1038/s42004-024-01115-4