Solvent dependent structural perturbations of chemical reaction intermediates visualized by time-resolved x-ray diffraction

Vincent, Jonathan; Andersson, Magnus; Eklund, Mattias; Wöhri, Annemarie B.; Odelius, Michael; Malmerberg, Erik; Kong, Qingyu; Wulff, Michaël; Neutze, Richard; Davidsson, Jan

doi:10.1063/1.3111401

Cited by 39 publications

(56 citation statements)

References 35 publications

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“…The presence of heavy atoms within the photochemical of study was an essential ingredient since the challenge was to reliably extract a transient structural signal from a low-concentration photochemical intermediate of interest when, at the same time, the surrounding solvent molecules become heated and thereby also cause transient changes in the X-ray scattering data (Cammarata et al, 2006;Georgiou et al, 2006). For timeresolved X-ray scattering studies of small molecules in solution this problem has proven tractable, and several studies have unambiguously observed the transient conformations of short-lived photochemical systems in solution (Plech et al, 2004;Davidsson et al, 2005;Ihee, Lorenc et al, 2005: Vincent et al, 2009Kong et al, 2006Kong et al, , 2007Kong et al, , 2008.…”

Section: Time-resolved Wide-angle X-ray Scatteringmentioning

confidence: 99%

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

et al. 2010

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Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein's resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein's conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein's reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and timeresolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics. These methods are illustrated using a limited set of examples including myoglobin and haemoglobin in complex with carbon monoxide, the simple light-driven proton pump bacteriorhodopsin, and the superoxide scavenger superoxide reductase. In conclusion, likely future developments of these methods at synchrotron X-ray sources and the potential impact of emerging X-ray free-electron laser facilities are speculated upon.

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Section: Time-resolved Wide-angle X-ray Scatteringmentioning

confidence: 99%

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

et al. 2010

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“…Furthermore, TR-XSS was also applied in the investigation of the iodine elimination reaction in haloalkanes, disclosing also the solvent polarity role on the intermediates' structure and their kinetics [58,63,165,166].…”

Section: Applicationsmentioning

confidence: 99%

Synchrotron ultrafast techniques for photoactive transition metal complexes

Borfecchia

Garino

Salassa

et al. 2013

Phil. Trans. R. Soc. A.

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In the last decade, the use of time-resolved X-ray techniques has revealed the structure of lightgenerated transient species for a wide range of samples, from small organic molecules to proteins. Time resolutions of the order of 100 ps are typically reached, allowing one to monitor thermally equilibrated excited states and capture their structure as a function of time. This review aims at providing a general overview of the application of timeresolved X-ray solution scattering (TR-XSS) and time-resolved X-ray absorption spectroscopy (TR-XAS), the two techniques prevalently employed in the investigation of light-triggered structural changes of transition metal complexes. In particular, we herein describe the fundamental physical principles for static XSS and XAS and illustrate the theory of timeresolved XSS and XAS together with data acquisition and analysis strategies. Selected pioneering examples of photoactive transition metal complexes studied by TR-XSS and TR-XAS are discussed in depth.

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“…Time-resolved X-ray solution scattering17-19 together with time-resolved X-ray crystallography20, X-ray absorption spectroscopy21 and electron diffraction21 can provide direct structural information, and thus complements time-resolved optical spectroscopy in the analysis of solution-phase reaction mechanisms. Recently time-resolved solution scattering technique has been applied to follow conformational changes in proteins with nanosecond22-24 and picosecond25 time resolution.…”

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Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering

et al. 2011

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Here we report structural dynamics of equine myoglobin (Mb) in response to the CO photodissociation visualized by picosecond time-resolved X-ray solution scattering. The data clearly reveals new structural dynamics that occurs in the timescale of ~360 picoseconds (ps) and 9 nanoseconds (ns), which have not been clearly detected in previous studies.Myoglobin (Mb) is a heme protein that carries small-molecule ligands such as O 2 , CO and NO in muscles, and can be considered as a subunit of hemoglobin, a paradigm protein for the study of allostery. Due to its small size, availability and photosensitivity of the hemeligand bond, Mb has served as a prototypical model system for studying protein structural dynamics. Accordingly, structural dynamics of Mb have been intensively studied with various spectroscopic 1-8 and structural 9-16 tools. The ligands form covalent bonds with Fe 2+ of the heme group and can be photolyzed by visible light on sub-picosecond time scale. [2][3] Upon the CO photolysis of MbCO, a small portion of the dissociated CO ligands geminately rebind to the heme, while the remainder travels to various pockets that can accommodate the ligand and eventually escapes the protein matrix to the solvent. On a longer time scale, the vacant heme recovers the ligand via non-geminate recombination.To directly track the structural changes associated with the ligand migration and rebinding and capture structurally distinct intermediates, we used pump-probe time-resolved X-ray solution scattering technique, where the time-dependent scattering of short X-ray pulses from a synchrotron are used to interrogate the structural dynamics of a liquid solution sample that is pumped with optical laser pulses in a pump-probe manner. Time-resolved Xray solution scattering [17][18][19] together with time-resolved X-ray crystallography 20 , X-ray absorption spectroscopy 21 and electron diffraction 21 can provide direct structural information, and thus complements time-resolved optical spectroscopy in the analysis of solution-phase reaction mechanisms. Recently time-resolved solution scattering technique has been applied to follow conformational changes in proteins with nanosecond 22-24 and picosecond 25 time resolution. Here, we show its application to another type of protein, Mb from equine heart, with picosecond time resolution.Time-resolved X-ray solution scattering data were measured at 14IDB beamline of Advanced Photon Source. The usual experimental protocol 22, 25 was followed. Specifically,

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Solvent dependent structural perturbations of chemical reaction intermediates visualized by time-resolved x-ray diffraction

Cited by 39 publications

References 35 publications

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

Synchrotron ultrafast techniques for photoactive transition metal complexes

Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering

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