A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to
effect substrate oxidations that range from the hydroxylation of methane and the …

Metal ions provide considerable functionality across biological systems, and their utilization
within biomolecules has adapted through changes in the chemical environment to maintain …

Microcrystal electron diffraction (MicroED) has recently shown potential for structural biology.
It enables the study of biomolecules from micrometer-sized 3D crystals that are too small to …

The aerobic oxidation of carbon–hydrogen (C–H) bonds in biology is currently known to be
accomplished by a limited set of cofactors that typically include heme, nonheme iron, and …

Dinuclear monooxygenases mediate challenging C–H bond oxidation reactions throughout
nature. Many of these enzymes are presumed to exclusively utilize diiron cofactors. Herein …

Metalloproteins with dinuclear cores are known to bind and activate dioxygen, with a
subclass of these proteins having active sites containing FeMn cofactors and activities …

Apart from oxygenic photosynthesis, the extent of manganese utilization in bacteria varies
from species to species and also appears to depend on external conditions. This …

Class Ic ribonucleotide reductases (RNRIc) and R2-like ligand-binding oxidases (R2lox) are
known to contain heterobimetallic MnIIFeII cofactors. How these enzymes assemble MnIIFeII …

Traditionally, the ferritin-like superfamily of proteins was thought to exclusively use a diiron
active site in catalyzing a diverse array of oxygen-dependent reactions. In recent years …

Heterobimetallic Mn/Fe proteins represent a new cofactor paradigm in bioinorganic
chemistry and pose countless outstanding questions. The assembly of the active site defies …