Adeline Bonvalet

Generation of ultrabroadband femtosecond pulses in the mid‐infrared by optical rectification of 15 fs light pulses at 100 MHz repetition rate

Quasi‐single‐cycle near‐infrared light pulses with a measured spectrum extending from 7 to 15 μm have been generated, opening up new perspectives in IR spectroscopy. The method is based on the rectification of 0.8 μm 10–15 fs light pulses from a 100 MHz oscillator, using the instantaneous second‐order polarizability of bulk semiconductors such as GaAs.

Femtosecond diffracting Fourier-transform infrared interferometer

We have developed a new scheme of Fourier-transform spectroscopy in the mid and the far infrared. The method relies on an interferometer in the visible or the near infrared, providing a sequence of two femtosecond pulses, which in turn generate a sequence of infrared pulses. The geometrical properties of the different diffracted infrared waves are used to isolate the relevant signal. An experimental demonstration is shown in the mid infrared by use of optical rectification of near-infrared 15-fs pulses.

Removing cross-phase modulation from midinfrared chirped-pulse upconversion spectra

We observe that narrow spectral features in mid-infrared spectra obtained by chirped-pulse up-conversion are strongly distorted by cross-phase modulation between the mid-infrared field and the chirped pulse. We discuss the consequences of this effect on spectral resolution, and introduce a correction method that recovers masked lines. This simple correction can be applied either when the upconverted field is fully characterized, such as in multidimensional spectroscopy, or when causality can be used, such as in absorption spectroscopy, which we demonstrate experimentally.

Direct mid-infrared femtosecond pulse shaping with a calomel acousto-optic programmable dispersive filter

Direct amplitude and phase shaping of mid-infrared femtosecond pulses is realized with a calomel-based acousto-optic programmable dispersive filter transparent between 0.4 and 20 μm. The shaped pulse electric field is fully characterized with high accuracy, using chirped-pulse upconversion and time-encoded arrangement spectral phase interferometry for direct electric field reconstruction techniques. Complex mid-infrared pulse shapes at a center wavelength of 4.9 μm are generated with a spectral resolution of 14 cm(-1), which exceeds by a factor of 5 the reported experimental resolutions of calomel-based filters.

Strong Ligand–Protein Interactions Revealed by Ultrafast Infrared Spectroscopy of CO in the Heme Pocket of the Oxygen Sensor FixL

In heme-based sensor proteins, ligand binding to heme in a sensor domain induces conformational changes that eventually lead to changes in enzymatic activity of an associated catalytic domain. The bacterial oxygen sensor FixL is the best-studied example of these proteins and displays marked differences in dynamic behavior with respect to model globin proteins. We report a mid-IR study of the configuration and ultrafast dynamics of CO in the distal heme pocket site of the sensor PAS domain FixLH, employing a recently developed method that provides a unique combination of high spectral resolution and range and high sensitivity. Anisotropy measurements indicate that CO rotates toward the heme plane upon dissociation, as is the case in globins. Remarkably, CO bound to the heme iron is tilted by ~30° with respect to the heme normal, which contrasts to the situation in myoglobin and in present FixLH-CO X-ray crystal structure models. This implies protein-environment-induced strain on the ligand, which is possibly at the origin of a very rapid docking-site population in a single conformation. Our observations likely explain the unusually low affinity of FixL for CO that is at the origin of the weak ligand discrimination between CO and O(2). Moreover, we observe orders of magnitude faster vibrational relaxation of dissociated CO in FixL than in globins, implying strong interactions of the ligand with the distal heme pocket environment. Finally, in the R220H FixLH mutant protein, where CO is H-bonded to a distal histidine, we demonstrate that the H-bond is maintained during photolysis. Comparison with extensively studied globin proteins unveils a surprisingly rich variety in both structural and dynamic properties of the interaction of a diatomic ligand with the ubiquitous b-type heme-proximal histidine system in different distal pockets.

Asynchronous optical sampling with arbitrary detuning between laser repetition rates.

A method of asynchronous optical sampling based on free-running lasers with no requirement on the repetition rates is presented. The method is based on the a posteriori determination of the delay between each pair of pulses. A resolution better than 400 fs over 13 ns total delay scan is demonstrated. In addition to the advantages of conventional asynchronous sampling techniques, this method allows a straightforward implementation on already-existing laser systems using a fiber-based setup and an appropriate acquisition procedure.

Characterization of mid-infrared femtosecond pulses [Invited]

We review different methods for characterizing mid-infrared femtosecond pulses, including linear methods such as electro-optic sampling, time- and frequency-domain interferometry, and nonlinear self-referenced methods such as frequency-resolved optical gating (FROG) and spectral phase interferometry for direct electric-field reconstruction (SPIDER). Of particular interest are methods based on upconversion through nonlinear mixing with chirped 800 nm pulses, enabling a complete measurement of mid-infrared pulses with visible-light spectrometers.

1 kHz tabletop ultrashort hard x-ray source for time-resolved x-ray protein crystallography.

We describe a compact, reliable, and high-average-power femtosecond x-ray source and its first application to diffraction on protein crystal. The setup relies on a homemade Ti: sapphire system delivering 12 mJ at a 1 kHz repetition rate, associated with a small vacuum chamber especially designed for laser-plasma interaction and x-ray applications. This device allows the generation of 5 x 10(9) photons/s/sr at 8 keV and optimized x-ray irradiation of the studied sample, which can be placed close to the source. We present the diffraction pattern of a protein crystal in a divergent beam geometry, which is a first step to a subpicosecond x-ray diffraction experiment.

Ultrafast Dynamics of Carboxy-Hemoglobin: Two-Dimensional Infrared Spectroscopy Experiments and Simulations

This Letter presents a comparison between experimental and simulated 2D mid-infrared spectra of carboxy-hemoglobin in the spectral region of the carbon monoxide stretching mode. The simulations rely on a fluctuating potential energy surface that includes both the effect of heme and the protein surroundings computed from molecular dynamics simulations. A very good agreement between theory and experiment is obtained with no adjustable parameters. The simulations show that the effect of the distal histidine through the hydrogen bond is strong and is directly responsible for the slow decay of the frequency-frequency correlation function on a 10 ps time scale. This study confirms that fluctuations in carboxy-hemoglobin are more inhomogeneous than those in the more frequently studied carboxy-myoglobin. The comparison between simulations and experiments brings valuable information on the complex relation between protein structure and spectral diffusion.

Suppression of perturbed free-induction decay and noise in experimental ultrafast pump-probe data

We apply a Fourier filtering technique for the global removal of coherent contributions, like perturbed free-induction decay, and noise, to experimental pump-probe spectra. A further filtering scheme gains access to spectra otherwise only recordable by scanning the probes center frequency with adjustable spectral resolution. These methods cleanse pump-probe data and allow improved visualization and simpler analysis of the contained dynamics. We demonstrate these filters using visible pump/mid-infrared probe spectroscopy of ligand dissociation in carboxyhemoglobin.