5 YEARS OF ION-LASER INTERACTION MASS SPECTROMETRY—STATUS AND PROSPECTS OF ISOBAR SUPPRESSION IN AMS BY LASERS

ABSTRACT A setup for ion-laser interaction was coupled to the state-of-the-art AMS facility VERA five years ago and its potential and applicability as a new means of isobar suppression in accelerator mass spectrometry (AMS) has since been explored. Laser photodetachment and molecular dissociation processes of anions provide unprecedented isobar suppression factors of >1010 for several established AMS isotopes like 36Cl or 26Al and give access to new AMS isotopes like 90Sr, 135Cs or 182Hf at a 3-MV-tandem facility. Furthermore, Ion-Laser InterAction Mass Spectrometry has been proven to meet AMS requirements regarding reliability and robustness with a typical reproducibility of results of 3%. The benefits of the technique are in principle available to any AMS machine, irrespective of attainable ion beam energy. Since isobar suppression via this technique is so efficient, there often is no need for any additional element separation in the detection setup and selected nuclides may even become accessible without accelerator at all.

Detection of OH at the evening terminator of the ultra-hot Jupiter WASP-76b

<p>Ultra-hot Jupiters have dayside temperatures similar to those of M-dwarfs. While molecular absorption from the hydroxyl radical (OH) is easily observed in near-infrared spectra of M-dwarfs, it is often not considered when studying the atmospheres of (ultra-)hot Jupiters. We use high-resolution spectroscopic near-infrared observations of a transit of WASP-76b obtained using CARMENES to assess the presence of OH. After validating the OH line list, we generate model transit spectra of WASP-76b with petitRADTRANS. The data are corrected for telluric contamination and cross-correlated with the model spectra. After combining all cross-correlation functions from the transit, a detection map is constructed. OH is detected in the atmosphere of WASP-76b with a signal-to-noise ratio of 6.1. From a Markov Chain Monte Carlo retrieval we obtain Kp=234 km/s and a blueshift of 13.9 km/s. Considering the fast spin-rotation of the planet, the OH signal is best explained with the signal mainly originating from the evening terminator and the presence of a strong day- to nightside wind. The signal appears to be broad, with a full width at half maximum of 16.2 km/s. The retrieval results in a weak constraint on the temperature of 2420-3150 K at the pressure of the OH signal. Our results demonstrate that OH is readily observable in the transit spectra of ultra-hot Jupiters. Studying this molecule can give new insights in the molecular dissociation processes in the atmospheres of such planets.</p>

Molecular dissociation and proton transfer in aqueous methane solution under electric field.

Methane-water mixtures are ubiquitous in our Solar System and they have been the subject of a wide variety of experimental, theoretical, and computational studies aimed at understanding their behaviour under...

Capturing roaming molecular fragments in real time

Since the discovery of roaming as an alternative molecular dissociation pathway in formaldehyde (H2CO), it has been indirectly observed in numerous molecules. The phenomenon describes a frustrated dissociation with fragments roaming at relatively large interatomic distances rather than following conventional transition-state dissociation; incipient radicals from the parent molecule self-react to form molecular products. Roaming has been identified spectroscopically through static product channel–resolved measurements, but not in real-time observations of the roaming fragment itself. Using time-resolved Coulomb explosion imaging (CEI), we directly imaged individual “roamers” on ultrafast time scales in the prototypical formaldehyde dissociation reaction. Using high-level first-principles simulations of all critical experimental steps, distinctive roaming signatures were identified. These were rendered observable by extracting rare stochastic events out of an overwhelming background using the highly sensitive CEI method.

Revealing Ultrafast Two-Electron Transfer Over Tryptophan with Mass Spectrometry

Electron transfer crucial to bioenergetics is ubiquitously present in biological systems but most of them escape from direct observations. By using tryptophan and its derivatives with 1-CH₃, 2-CH₃, 5-CH₃ and 5-OH substitutions as model molecules, we have unambiguously demonstrated successive two-electron transfer to tryptophan as well as electronic and vibrational excited molecular dissociation with mass spectrometry. The ultra-short time delay between two electrons down to sub-attosecond over a distance less than 10 Å was found to cause the strong coupling of electronic and vibrational excitations that was validated by the observation of radical-radical coupling. Intramolecular H migrations along with two-electron transfer was demonstrated with H/D exchange and ¹³C stable isotope labeling. This proposed technique allows us to observe the ultrafast electron transfer from tryptophan to the heme group in myoglobin proteins. It bridges electron transfer to energy transfer that has been revealed in FRET alone. FeII (porph•‐) and FeI (porph•‐) resulting from one- and two-electron transfer, respectively, have been unambiguously identified<br>

Revealing Ultrafast Two-Electron Transfer Over Tryptophan with Mass Spectrometry

Electron transfer crucial to bioenergetics is ubiquitously present in biological systems but most of them escape from direct observations. By using tryptophan and its derivatives with 1-CH₃, 2-CH₃, 5-CH₃ and 5-OH substitutions as model molecules, we have unambiguously demonstrated successive two-electron transfer to tryptophan as well as electronic and vibrational excited molecular dissociation with mass spectrometry. The ultra-short time delay between two electrons down to sub-attosecond over a distance less than 10 Å was found to cause the strong coupling of electronic and vibrational excitations that was validated by the observation of radical-radical coupling. Intramolecular H migrations along with two-electron transfer was demonstrated with H/D exchange and ¹³C stable isotope labeling. This proposed technique allows us to observe the ultrafast electron transfer from tryptophan to the heme group in myoglobin proteins. It bridges electron transfer to energy transfer that has been revealed in FRET alone. FeII (porph•‐) and FeI (porph•‐) resulting from one- and two-electron transfer, respectively, have been unambiguously identified<br>