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Abstract Molecules that can reversibly switch between electronic states under an external stimulus are of interest to numerous applications. Complexes of open shell metal ions with redox active ligands undergo valence tautomerism, resulting in magnetic, colour and structural switching, relevant to data storage and actuators. However, the precise structural changes occurring during valence tautomerism in the solid state are unclear due to the lack of atomic-resolution characterization. Here, variable temperature and high-pressure single crystal X-ray diffraction is used to characterize valence tautomerism in two isostructural cobalt complexes, [Co(bis(6-methyl-2-pyridylmethyl) amine)(3,5-di-tert-butyl-1,2-dioxolene)]+ and [Co(tris(6-methyl-2-pyridylmethyl)amine)(3,5-di-tert-butyl-1,2-dioxolene)]+ to atomic resolution. The less sterically hindered dimethylated complex exhibits two-step thermally-induced interconversion between the high-spin CoII-seminquinonate and low-spin CoIII-catecholate forms (valence tautomerism) at 155 and 95 K due to the presence of two symmetry-independent complexes. In contrast, the more sterically hindered trimethylated complex does not display thermal valence tautomerism. Both complexes exhibit unique behaviour under high pressure. The dimethylated species undergoes gradual, one-step valence tautomerism in both symmetry-independent complexes concurrently between 0.43 GPa and 1.30 GPa. In the trimethylated species, pressure is sufficient to overcome steric hindrance, leading to one-step valence tautomerism between 2.60 GPa and 3.10 GPa, demonstrating pressure-triggered valence tautomerism in a thermally inactive complex. This study is among the few investigations using in situ high-pressure single crystal X-ray diffraction to achieve atomic-level structural characterization of valence tautomerism, aiding the development of robust structure-property relationships in these types of complexes.

Differentiation and activation of T cells are normally modulated by non-covalent interactions between T cell receptor (TCR) and antigenic peptides. Here the authors use step-wise mutations, biochemical characterization and structural insights to describe the contributions of natural covalent bonds between TCR and antigenic peptides during these processes.