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Monoclinic HfO₂ stabilizes hydroxylated indium atoms that drive efficient CO₂ hydrogenation to methanol, offering a general strategy for coupling single-atom catalysis with reducible metal oxides and wide-bandgap dielectric supports.

An integrated structural biology approach is utilized to elucidate the solution structure of the polypyrimidine-tract binding protein 1 (PTBP1/hnRNP I) complexed with an internal ribosome entry site (IRES) RNA fragment from encephalomyocarditis virus (EMCV).

The restructuring of carbon-based supports under reaction conditions limits catalyst stability for vinyl chloride synthesis. Here, the authors report that hydrogen chloride generates defect sites on carbon nitride supports, promoting acetylene polymerization and accelerating catalyst deactivation.

Solid-state spin qubits offer promise as building blocks for quantum computers. Now, efficient quantum control is demonstrated over hybrid nuclear–electronic qubits in bismuth-doped silicon, as a consequence of the strong hyperfine interactions in this system.

Fe-exchanged zeolite catalysts are known for their ability to remediate NO_x and N₂O emissions, but their reactivity in mixed streams of NO and N₂O remains unclear. Now a suite of operando spectroscopies reveals the active Fe species involved in the process and their synergistic effect during the simultaneous conversion of these pollutants.

Born et al. describe interdomain allostery in the two domain peptidyl-prolyl isomerase Pin1 upon binding of two ligands. These ligands couple population shifts of extended and compact states to changes in the catalytic site of Pin1.

Here, the authors use solid-state NMR and EPR measurements to characterise the ATP hydrolysis transition state of the oligomeric bacterial DnaB helicase from Helicobacter pylori, which was trapped by using aluminium fluoride as a chemical mimic. They identify protein protons that coordinate to the phosphate groups of ADP and DNA and observe that the aluminium fluoride unit is highly mobile and fast-rotating.

An agarose hydrogel mimicking cytoskeleton stabilizes protein liquid droplets and enables precise quantification of protein percentage in phase-separated droplets and in the dispersed phases as well as intramolecular distances via NMR and EPR.

A haem–carbenoid has been proposed to be involved in abiological enzymatic reactions. Now, Hilvert and co-workers provide crystallographic evidence for a haem–carbenoid intermediate as the reactive species in an olefin cyclopropanation reaction catalysed by an artificial metalloenzyme.

Carbon is a key support for metal-catalyzed acetylene hydrochlorination to vinyl chloride but its role remains elusive. Here, the authors, by means of operando spectroscopy, demonstrate the co-catalytic function of neighboring carbon and isolated metal atoms, constituting the active ensemble.

High-resolution structures of large RNAs and protein–RNA complexes are difficult to solve due to inherent structural flexibility and a high risk of crystallization artefacts. Here, Duss et al. present a novel EPR-based approach to aid structure determination of large RNAs and protein–RNA complexes in solution.

Assembling multicomponent catalysts to harness synergic effects is challenging. Now, flame spray pyrolysis permits the synthesis of ternary Pd-In₂O₃-ZrO₂ catalysts with an optimal architecture and an enriched density of oxygen vacancies for maximal performance in CO₂-based methanol synthesis.

The ideal metal selection and atomic-level arrangement for catalysts in CO₂ hydrogenation are still uncertain. Here, copper is identified as the most effective promoter for enhancing ZnZrO_x catalysts when precisely structured into CuZn ensembles, offering new insights for designing superior catalysts for CO₂-based methanol synthesis.

The conversions of methanol or methyl chloride over zeolite catalysts are promising processes to produce valuable hydrocarbons, but their mechanisms are still not fully understood. Now these are evaluated using operando photoelectron photoion coincidence spectroscopy, which enables the direct observation of elusive intermediates such as methyl radicals or ketene.

A novel combined NMR and EPR spectroscopy approach reveals the structure and assembly mechanism of a 70-kDa bacterial ribonucleoprotein complex acting as a protein sponge in translational regulation.

HDL particles transport cholesterol and contain apolipoprotein A-I as their major protein. The solution structure of discoidal HDL particles reconstituted with a shortened apoA-I is now solved via a combination of NMR and EPR analyses.