Observation of Seeded Mn Kß Stimulated X-Ray Emission Using Two-Color X-Ray Free-Electron Laser Pulses.

Kß x-ray emission spectroscopy is a powerful probe for electronic structure analysis of 3d transition metal systems and their ultrafast dynamics. Selectively enhancing specific spectral regions would increase this sensitivity and provide fundamentally new insights. Recently we reported the observation and analysis of Kα amplified spontaneous x-ray emission from Mn solutions using an x-ray free-electron laser to create the 1s core-hole population inversion [Kroll et al., Phys. Rev. Lett. 120, 133203 (2018)PRLTAO0031-900710.1103/PhysRevLett.120.133203]. To apply this new approach to the chemically more sensitive but much weaker Kß x-ray emission lines requires a mechanism to outcompete the dominant amplification of the Kα emission. Here we report the observation of seeded amplified Kß x-ray emission from a NaMnO_{4} solution using two colors of x-ray free-electron laser pulses, one to create the 1s core-hole population inversion and the other to seed the amplified Kß emission. Comparing the observed seeded amplified Kß emission signal with that from conventional Kß emission into the same solid angle, we obtain a signal enhancement of more than 10^{5}. Our findings are the first important step of enhancing and controlling the emission of selected final states of the Kß spectrum with applications in chemical and materials science.

X-ray diffractive imaging of controlled gas-phase molecules: Toward imaging of dynamics in the molecular frame.

We report experimental results on the diffractive imaging of three-dimensionally aligned 2,5-diiodothiophene molecules. The molecules were aligned by chirped near-infrared laser pulses, and their structure was probed at a photon energy of 9.5 keV (λ ≈ 130 pm) provided by the Linac Coherent Light Source. Diffracted photons were recorded on the Cornell-SLAC pixel array detector, and a two-dimensional diffraction pattern of the equilibrium structure of 2,5-diiodothiophene was recorded. The retrieved distance between the two iodine atoms agrees with the quantum-chemically calculated molecular structure to be within 5%. The experimental approach allows for the imaging of intrinsic molecular dynamics in the molecular frame, albeit this requires more experimental data, which should be readily available at upcoming high-repetition-rate facilities.

Stimulated X-Ray Emission Spectroscopy in Transition Metal Complexes.

We report the observation and analysis of the gain curve of amplified Kα x-ray emission from solutions of Mn(II) and Mn(VII) complexes using an x-ray free electron laser to create the 1s core-hole population inversion. We find spectra at amplification levels extending over 4 orders of magnitude until saturation. We observe bandwidths below the Mn 1s core-hole lifetime broadening in the onset of the stimulated emission. In the exponential amplification regime the resolution corrected spectral width of ∼1.7 eV FWHM is constant over 3 orders of magnitude, pointing to the buildup of transform limited pulses of ∼1 fs duration. Driving the amplification into saturation leads to broadening and a shift of the line. Importantly, the chemical sensitivity of the stimulated x-ray emission to the Mn oxidation state is preserved at power densities of ∼10^{20} W/cm^{2} for the incoming x-ray pulses. Differences in signal sensitivity and spectral information compared to conventional (spontaneous) x-ray emission spectroscopy are discussed. Our findings build a baseline for nonlinear x-ray spectroscopy for a wide range of transition metal complexes in inorganic chemistry, catalysis, and materials science.

Structure of photosystem II and substrate binding at room temperature.

Light-induced oxidation of water by photosystem II (PS II) in plants, algae and cyanobacteria has generated most of the dioxygen in the atmosphere. PS II, a membrane-bound multi-subunit pigment protein complex, couples the one-electron photochemistry at the reaction centre with the four-electron redox chemistry of water oxidation at the Mn4CaO5 cluster in the oxygen-evolving complex (OEC). Under illumination, the OEC cycles through five intermediate S-states (S0 to S4), in which S1 is the dark-stable state and S3 is the last semi-stable state before O-O bond formation and O2 evolution. A detailed understanding of the O-O bond formation mechanism remains a challenge, and will require elucidation of both the structures of the OEC in the different S-states and the binding of the two substrate waters to the catalytic site. Here we report the use of femtosecond pulses from an X-ray free electron laser (XFEL) to obtain damage-free, room temperature structures of dark-adapted (S1), two-flash illuminated (2F; S3-enriched), and ammonia-bound two-flash illuminated (2F-NH3; S3-enriched) PS II. Although the recent 1.95 Å resolution structure of PS II at cryogenic temperature using an XFEL provided a damage-free view of the S1 state, measurements at room temperature are required to study the structural landscape of proteins under functional conditions, and also for in situ advancement of the S-states. To investigate the water-binding site(s), ammonia, a water analogue, has been used as a marker, as it binds to the Mn4CaO5 cluster in the S2 and S3 states. Since the ammonia-bound OEC is active, the ammonia-binding Mn site is not a substrate water site. This approach, together with a comparison of the native dark and 2F states, is used to discriminate between proposed O-O bond formation mechanisms.

Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein.

A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction.

Optical constants of electron-beam evaporated boron films in the 6.8-900 eV photon energy range.

The optical constants of electron-beam evaporated boron from 6.8 to 900 eV were calculated through transmittance measurements of boron thin films deposited onto carbon-coated microgrids or LiF substrates in ultrahigh-vacuum conditions. In the low-energy part of the spectrum the measurements were performed in situ on freshly deposited samples, whereas in the high-energy range the samples were exposed to the atmosphere before the measurements. The extinction coefficient was calculated directly from the transmittance data, and a Kramers-Kronig analysis that combined the current data with data from the literature was performed to determine the dispersive part of the index of refraction. Finally, two different sum-rule tests were performed that indicated the good consistency of the data.

Coherent soft x-ray generation in the water window with quasi-phase matching.

We demonstrate enhanced generation of coherent light in the "water window" region of the soft x-ray spectrum at 4.4 nanometers, using quasi-phase-matched frequency conversion of ultrafast laser pulses. By periodically modulating the diameter of a gas-filled hollow waveguide, the phase mismatch normally present between the laser light and the generated soft x-ray light can be partially compensated. This makes it possible to use neon gas as the nonlinear medium to coherently convert light up to the water window, illustrating that techniques of nonlinear optics can be applied effectively in the soft x-ray region of the spectrum. These results advance the prospects for compact coherent soft x-ray sources for applications in biomicroscopy and in chemical spectroscopy.