Unique properties of metal complexes, such as structural diversity, adjustable ligand exchange kinetics, fine-tuned redox activities, and distinct spectroscopic signatures, make them exciting scaffolds not only for binding to nucleic acids but increasingly also to proteins as non-traditional targets. This feature article discusses recent trends in this field. These include the use of chemically inert metal complexes as structural scaffolds for the design of enzyme inhibitors, new strategies for inducing selective coordination chemistry at the protein binding site, recent advances in the development of catalytic enzyme inhibitors, and the design of metal complexes that can inject electrons or holes into redox enzymes. A common theme in many of the discussed examples is that binding selectivity is at least in part achieved through weak interactions between the ligand sphere and the protein binding site. These examples hint to an exciting future in which “organic-like” molecular recognition principles are combined with properties that are unique to metals and thus promise to yield compounds with novel and unprecedented properties.

Recent advances in merging visible light activated photochemistry with asymmetric catalysis are summarized and discussed.

A reaction design is reported in which a substrate-bound chiral Lewis acid complex absorbs visible light and generates an excited state that directly reacts with a cosubstrate in a highly stereocontrolled fashion. Specifically, a chiral rhodium complex catalyzes visible-light-activated intermolecular [2+2] cycloadditions, providing a wide range of cyclobutanes with up to >99% ee and up to >20:1 d.r. Noteworthy is the ability to create vicinal all-carbon-quaternary stereocenters including spiro centers in an intermolecular fashion.