Chromophore Dynamics in the PYP Photocycle from Femtosecond Stimulated Raman Spectroscopy

Creelman, Mark; Kumauchi, Masato; Hoff, Wouter D.; Mathies, Richard A.

doi:10.1021/jp408584v

Cited by 46 publications

(43 citation statements)

References 46 publications

(119 reference statements)

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“…Furthermore, the C1=O1 carbonyl out-of-plane vibration downshifts from 665 to 640 cm -1 concurrent with excited state decay which was interpreted as resulting from motion along the photoisomerisation coordinate [31]. The correspondence between X-ray structural and Raman structural measurements of Franck-Condon motions in PYP also highlights that selection rules must be considered for each ultrafast observation.…”

Section: Primary Photochemical Reactions and Coherence Of Pypmentioning

confidence: 89%

“…Creelman et al [31] observed using femtosecond stimulated Raman spectroscopy a FranckCondon intermediate already at ~100 fs, distinct from the major S1 decay process with a ~450 fs time constant. The FC state already showed gained intensity of a 958 cm -1 Hydrogen-outof-plane (HOOP) mode, indicative of chromophore distortion at the ethylenic C2=C3 [31].…”

Section: Primary Photochemical Reactions and Coherence Of Pypmentioning

confidence: 99%

“…The FC state already showed gained intensity of a 958 cm -1 Hydrogen-outof-plane (HOOP) mode, indicative of chromophore distortion at the ethylenic C2=C3 [31].…”

Section: Primary Photochemical Reactions and Coherence Of Pypmentioning

confidence: 99%

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Populations and coherence in femtosecond time resolved X-ray crystallography of the photoactive yellow protein

Hutchison

Thor

2017

International Reviews in Physical Chemistry

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Ultrafast X-ray crystallography of the Photoactive Yellow Protein with femtosecond delays using an X-ray Free Electron Laser has successfully probed the dynamics of an early FranckCondon species. The femtosecond pump-probe application of protein crystallography represents a new experimental regime that provides an X-ray structural probe for coherent processes that were previously accessible primarily using ultrafast spectroscopy. We address how the optical regime of the visible pump, that is necessary to successfully resolve ultrafast structural differences, affects the motions that are measured using the technique. The subpicosecond photochemical dynamics in PYP involves evolution of a mixture of electronic ground and excited state populations. Additionally, within the dephasing time structural motion include vibrational coherence arising from excited states, the ground state and a ground state intermediate under experimental conditions used for ultrafast crystallography. Intense optical pulses are required to convert population levels in PYP crystals that allow detection by X-ray crystallography, but the compromise currently needed for the optical bandwidth and power has consequences with regard to the contributions to the motions that are experimentally measured with femtosecond delays. We briefly review the ultrafast spectroscopy literature of the primary photoreactions of PYP and discuss relevant physical models taken from coherent control and femtosecond coherence spectroscopy literature that address both the population transfer as well 2 as the vibrational coherences. We apply linear response theory, with the additional use of a high power approximation, of on-resonance impulsive vibrational coherence in the ground state and the non-impulsive coherence in the excited state and discuss experimental approaches to manipulate the coherence contributions. The results are generalised and extended to discuss the future capabilities of high repetition rate XFEL instruments providing enhanced sensitivity to perform the crystallographic equivalent of an impulsive Raman measurement of vibrational coherence.

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Section: Primary Photochemical Reactions and Coherence Of Pypmentioning

confidence: 89%

Section: Primary Photochemical Reactions and Coherence Of Pypmentioning

confidence: 99%

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Populations and coherence in femtosecond time resolved X-ray crystallography of the photoactive yellow protein

Hutchison

Thor

2017

International Reviews in Physical Chemistry

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“…Literature evidence suggests (Nakamura et al ., 2007; Creelman et al ., 2014) that the pCA isomerization takes place on an ultrafast, sub-ps time scale. The ultrafast, fs X-ray pulses available at the XFEL were exploited to structurally characterize this transition (Pande et al ., 2016).…”

Section: Xfel Example: Early Events In the Photoactive Yellow Protmentioning

confidence: 99%

Watching proteins function with time-resolved x-ray crystallography

Šrajer

Schmidt

2017

J. Phys. D: Appl. Phys.

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Macromolecular crystallography was immensely successful in the last two decades. To a large degree this success resulted from use of powerful third generation synchrotron X-ray sources. An expansive database of more than 100,000 protein structures, of which many were determined at resolution better than 2 Å, is available today. With this achievement, the spotlight in structural biology is shifting from determination of static structures to elucidating dynamic aspects of protein function. A powerful tool for addressing these aspects is time-resolved crystallography, where a genuine biological function is triggered in the crystal with a goal of capturing molecules in action and determining protein kinetics and structures of intermediates (Schmidt et al., 2005a; Schmidt 2008; Neutze and Moffat, 2012; Šrajer 2014). In this approach, short and intense X-ray pulses are used to probe intermediates in real time and at room temperature, in an ongoing reaction that is initiated synchronously and rapidly in the crystal. Time-resolved macromolecular crystallography with 100 ps time resolution at synchrotron X-ray sources is in its mature phase today, particularly for studies of reversible, light-initiated reactions. The advent of the new free electron lasers for hard X-rays (XFELs; 5–20 keV), which provide exceptionally intense, femtosecond X-ray pulses, marks a new frontier for time-resolved crystallography. The exploration of ultra-fast events becomes possible in high-resolution structural detail, on sub-picosecond time scales (Tenboer et al., 2014; Barends et al., 2015; Pande et al., 2016). We review here state-of-the-art time-resolved crystallographic experiments both at synchrotrons and XFELs. We also outline challenges and further developments necessary to broaden the application of these methods to many important proteins and enzymes of biomedical relevance.

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“…The FSRS technology has been successfully applied to a number of important photosensitive molecular systems including rhodopsin [27], bacteriorhodopsin [28], phytochrome [29], organic dyes in solar cells [30], Fe(II) spin crossover in solution [31], fluorescent proteins [7,32,33], and calcium-ion-sensing protein biosensors [34][35][36]. The main goal of this work is to construct a versatile, tunable FSRS setup that extends the wavelength detection window to the UV regime with desired resonance Raman enhancement.…”

Section: Resultsmentioning

confidence: 99%

Sum-Frequency-Generation-Based Laser Sidebands for Tunable Femtosecond Raman Spectroscopy in the Ultraviolet

et al. 2015

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Femtosecond stimulated Raman spectroscopy (FSRS) is an emerging molecular structural dynamics technique for functional materials characterization typically in the visible to near-IR range. To expand its applications we have developed a versatile FSRS setup in the ultraviolet region. We use the combination of a narrowband, ~400 nm Raman pump from a home-built second harmonic bandwidth compressor and a tunable broadband probe pulse from sum-frequency-generation-based cascaded four-wave mixing (SFG-CFWM) laser sidebands in a thin BBO crystal. The ground state Raman spectrum of a laser dye Quinolon 390 in methanol that strongly absorbs at ~355 nm is systematically studied as a standard sample to provide previously unavailable spectroscopic characterization in the vibrational domain. Both the Stokes and anti-Stokes Raman spectra can be collected by selecting different orders of SFG-CFWM sidebands as the probe pulse. The stimulated Raman gain with the 402 nm Raman pump is >21 times larger than that with the 550 nm Raman pump when measured at the 1317 cm −1 peak for the aromatic ring deformation and ring-H rocking mode of the dye molecule, demonstrating that pre-resonance enhancement is effectively achieved in the unique UV-FSRS setup. This added tunability in the versatile and compact optical setup enables FSRS to better capture transient conformational snapshots of photosensitive molecules that absorb in the UV range. OPEN ACCESSAppl. Sci. 2015, 5 49

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Chromophore Dynamics in the PYP Photocycle from Femtosecond Stimulated Raman Spectroscopy

Cited by 46 publications

References 46 publications

Populations and coherence in femtosecond time resolved X-ray crystallography of the photoactive yellow protein

Populations and coherence in femtosecond time resolved X-ray crystallography of the photoactive yellow protein

Watching proteins function with time-resolved x-ray crystallography

Sum-Frequency-Generation-Based Laser Sidebands for Tunable Femtosecond Raman Spectroscopy in the Ultraviolet

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