Isomer-Dependent Electron Affinities of Fluorophenyl Radicals, •C6H5-xFx (2 ≤ x ≤ 4).

Di-, tri-, and tetrafluorophenyl radicals each have three regioisomers, several of which can form multiple distinct radical structures. We present the photoelectron spectra of the di-, tri-, and tetrafluorophenide regioisomer anions generated from their associated fluorobenzene precursors. By comparing the spectra to the results of density functional theory calculations, we determine that in cases where more than one possible radical isomer is possible for a given regioisomer (radicals formed from 1,2-difluorobenzene, 1,3-difluorobenzene, 1,2,3-trifluorobenzene, and 1,2,4-trifluorobenzene) the most stable anion corresponds to a less stable neutral, suggesting that the reactive C-center on these fluorine-substituted phenyl groups can be controlled by charge state. Full analyses of the spectra and computational results yield further insights into the differences between the electronic and molecular structures of the fluorophenyl radicals and their associated anions.

Anion Photoelectron Imaging Spectroscopy of C6F5X- (X = F, Cl, Br, I).

The photoelectron (PE) spectra of C6F5X- (X = Cl, Br, I) and computational results on the anions and neutrals are presented and compared to previously reported results on C6F6- [McGee, C. J. J. Phys. Chem. A 2023, 127, 8556-8565.]. The spectra all exhibit broad, vibrationally unresolved detachment transitions, indicating that the equilibrium structures of the anions are significantly different from the neutrals. The PE spectrum of C6F5Cl- exhibits a parallel photoelectron angular distribution (PAD), similar to that of the previously reported C6F6- spectrum, while the PE spectra of C6F5Br- and C6F5I- have isotropic PADs, and also exhibit a prominent X- PE feature due to photodissociation of C6F5X- resulting in X- formation. Identification of the C6F5X- detachment transition origins, which is equivalent to the neutral electron affinity (EA), in all three cases is difficult, since the broadness of the detachment feature is accompanied by vanishingly small detachment cross section near the origin. Upper limits on the EAs were determined to be 1.70 eV for C6F5Cl, 2.10 eV for C6F5Br, and 2.00 eV for C6F5I, all significantly higher than the 0.76 eV upper limit determined for C6F6 with the same experiment. The broad detachment transitions are consistent with computational results, which predict very large differences between the neutral and anionic C-X (X = Cl, Br, I) bond lengths. Based on differences between the MBIS atom charges in the anions and neutrals, the excess charge in the anion is on the unique C atom and X, in contrast to the nonplanar C2v structured C6F6- anion, for which the charge is delocalized over the molecule. In C6F5Cl-, the C-Cl bond is predicted to be bent out of the plane, while both C6F5Br- and C6F5I- are predicted to be planar on average. The impact of the interruption of the symmetry in the hexafluorobenzene neutral and anion on the molecular and electronic structure of C6F5X/C6F5X- is considered, as well as the possible dissociative state leading to X- (X = Br, I) formation, and the nature of the C-X bond.

Structural basis of P[II] rotavirus evolution and host ranges under selection of histo-blood group antigens.

Group A rotaviruses cause severe gastroenteritis in infants and young children worldwide, with P[II] genogroup rotaviruses (RVs) responsible for >90% of global cases. RVs have diverse host ranges in different human and animal populations determined by host histo-blood group antigen (HBGA) receptor polymorphism, but details governing diversity, host ranges, and species barriers remain elusive. In this study, crystal structures of complexes of the major P[II] genogroup P[4] and P[8] genotype RV VP8* receptor-binding domains together with Lewis epitope-containing LNDFH I glycans in combination with VP8* receptor-glycan ligand affinity measurements based on NMR titration experiments revealed the structural basis for RV genotype-specific switching between ßß and ßα HBGA receptor-binding sites that determine RV host ranges. The data support the hypothesis that P[II] RV evolution progressed from animals to humans under the selection of type 1 HBGAs guided by stepwise host synthesis of type 1 ABH and Lewis HBGAs. The results help explain disease burden, species barriers, epidemiology, and limited efficacy of current RV vaccines in developing countries. The structural data has the potential to impact the design of future vaccine strategies against RV gastroenteritis.

Anion Photoelectron Imaging Spectroscopy of C6HF5-, C6F6-, and the Absence of C6H2F4.

Substituents have a profound effect on the electronic structure of the benzene molecule. In this paper, we present new photoelectron spectra of the C5HF5- molecular anion, to test predictions [ Int. J. Quant. Chem. 2017, 188, e25504] that pentafluorobenzene has a positive electron affinity, as hexafluorobenzene was already known to have. The PE spectrum of C6HF5- exhibits a broad and vibrationally unresolved band due to significant differences between the structure of the anion and the neutral. The vertical detachment energy (VDE) of C5HF5- is determined to be 1.33 ± 0.05 eV, and the lowest binding energy at which the signal is observed is 0.53 ± 0.05 eV, which, if taken as the electron affinity, is in good agreement with the computed value. In addition, we attempted to generate intact C6H2F4- molecular ions using the 1,2,3,4-tetrafluorobenzene, 1,2,3,5-tetrafluorobenzene, and 1,2,4,5-tetrafluorobenzene precursors, as tetrafluorobenzene was predicted to have a near-zero but marginally positive electron affinity. Using a photoemission anion source, we were not able to produce the intact tetrafluorobenzene anion. Density functional theory calculations support a more detailed discussion of the impact of fluorine substitution on the electronic structure of these species.

Trend in the Electron Affinities of Fluorophenyl Radicals ·C6H5-xFx (1 ≤ x ≤ 4).

The electron affinities (EAs) of a series of ·C6H5-xFx (1 ≤ x ≤ 4) fluorophenyl radicals are determined from the photoelectron spectra of their associated fluorophenide anions generated from C6H6-xFx (1 ≤ x ≤ 4) fluorobenzene precursors. The spectra show a near-linear incremental increase in EA of 0.4 eV/x. The spectra exhibit vibrationally unresolved and broad detachment transitions consistent with significant differences in the molecular structures of the anion and neutral radical species. The experimental EAs and broad spectra are consistent with density functional theory calculations on these species. While the anion detachment transitions all involve an electron in a non-bonding orbital, the differences in structure between the neutral and anion are in part due to repulsion between the lone pair on the C-center on which the excess charge is localized and neighboring F atoms. The C6H5-xFx- (2 ≤ x ≤ 4) spectra show features at lower binding energy that appear to be due to constitutional isomers formed in the ion source.

Molecular basis of P[II] major human rotavirus VP8* domain recognition of histo-blood group antigens.

Initial cell attachment of rotavirus (RV) to specific cell surface glycan receptors, which is the essential first step in RV infection, is mediated by the VP8* domain of the spike protein VP4. Recently, human histo-blood group antigens (HBGAs) have been identified as receptors or attachment factors for human RV strains. RV strains in the P[4] and P[8] genotypes of the P[II] genogroup share common recognition of the Lewis b (Leb) and H type 1 antigens, however, the molecular basis of receptor recognition by the major human P[8] RVs remains unknown due to lack of experimental structural information. Here, we used nuclear magnetic resonance (NMR) spectroscopy-based titration experiments and NMR-derived high ambiguity driven docking (HADDOCK) methods to elucidate the molecular basis for P[8] VP8* recognition of the Leb (LNDFH I) and type 1 HBGAs. We also used X-ray crystallography to determine the molecular details underlying P[6] recognition of H type 1 HBGAs. Unlike P[6]/P[19] VP8*s that recognize H type 1 HBGAs in a binding surface composed of an α-helix and a ß-sheet, referred as the "ßα binding site", the P[8] and P[4] VP8*s bind Leb HBGAs in a previously undescribed pocket formed by the edges of two ß-sheets, referred to as the "ßß binding site". Importantly, the P[8] and P[4] VP8*s retain binding capability to non-Leb type 1 HBGAs using the ßα binding site. The presence of two distinct binding sites for Leb and non-Leb HBGA glycans in the P[8] and P[4] VP8* domains suggests host-pathogen co-evolution under structural and functional adaptation of RV pathogens to host glycan polymorphisms. Assessment and understanding of the precise impact of this co-evolutionary process in determining RV host ranges and cross-species RV transmission should facilitate improved RV vaccine development and prediction of future RV strain emergence and epidemics.