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The coordination sphere of the Fe(II) terpyridine complex1is rigidified by fourfold interlinking of both terpyridine ligands. Profiting from an octa‐aldehyde precursor complex, the ideal dimensions of the interlinking structures are determined by reversible Schiff‐base formation, before irreversible Wittig olefination provided the rigidified complex. Reversed‐phase HPLC enables the isolation of the all‐transisomer of the Fe(II) terpyridine complex1, which is fully characterized. While temperature independent low‐spin states were recorded with superconducting quantum interference device (SQUID) measurements for both, the open precursor8and the interlinked complex1, evidence of the increased rigidity of the ligand sphere in1was provided by proton T₂relaxation NMR experiments. The ligand sphere fixation in the macrocyclized complex1even reaches a level resisting substantial deformation upon deposition on an Au(111) surface, as demonstrated by its pristine form in a low temperature ultra‐high vacuum scanning tunneling microscope experiment.

Interlinking of two terpyridine ligands results in mononuclear chiral metal complexes (Fe and Ru) which were separated into their enantiomers.

Regulation of enzymatic activity is vital to living organisms. Here, we report the development and the genetic optimization of an artificial zymogen requiring the action of a natural protease to upregulate its latent asymmetric transfer hydrogenase activity.