Natural metalloproteins perform many functions—ranging from sensing to electron transfer
and catalysis—in which the position and property of each ligand and metal are dictated by …

One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Artificial metalloenzymes combine the advantages of both natural enzymes and chemically
synthesized models, which have achieved significant progress in the last decade. This …

Synthetic iron–sulfur clusters of general formulation [Fe m S q L l] z with core atoms Fe and S
and terminal ligands L constitute a family of molecular clusters with remarkably diverse …

Iron–sulfur clusters have been reported to catalyze various redox transformations, including
the multielectron reduction of CO2 to hydrocarbons. Herein, we report the design and …

The ubiquity, structural variation, and functional diversity of iron-sulfur (Fe-S) clusters in
biological environments has long fascinated scientists. In nature, Fe-S clusters form a variety …

Metalloproteins are crucial for life. The mutual relationship between metal ions and proteins
makes metalloproteins able to accomplish key processes in biological systems, often very …

A symmetric origin for bacterial ferredoxins was first proposed over 50 y ago, yet, to date, no
functional symmetric molecule has been constructed. It is hypothesized that extant proteins …

To mimic a hypothetical pathway for protein evolution, we previously tailored a monomeric
protein (cyt cb562) for metal‐mediated self‐assembly, followed by re‐design of the resulting …

Bacterial microcompartments (BMCs) are self-assembling organelles composed of a
selectively permeable protein shell and encapsulated enzymes. They are considered …