As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …

Enzyme mimics, especially nanozymes, play a crucial role in replacing natural enzymes for
diverse applications related to bioanalysis, therapeutics and other enzyme-like catalysis …

Conventional nanozyme technologies face formidable challenges of intricate size-,
composition-, and facet-dependent catalysis and inherently low active site density. We …

The atomistic change of C (sp3)–H to C (sp3)–O can have a profound impact on the physical
and biological properties of small molecules. Traditionally, chemical synthesis has relied on …

Utilization of O2 as an abundant and environmentally benign oxidant is of great interest in
the design of bioinspired synthetic catalytic oxidation systems. Metalloenzymes activate O2 …

Iron is an especially important redox-active cofactor in biology because of its ability to
mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth …

Inspired by the key role of the coordination environment in the catalytic activity of enzymes, a
rational design of the coordination structure of active sites at the atom scale is expected to …

Abstract [FeFe]-hydrogenases are efficient H2-catalysts, yet upon contact with dioxygen their
catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray …

The introduction of fluoroalkyl groups into organic compounds can significantly alter
pharmacological characteristics. One enabling but underexplored approach for the …

Conspectus Aerobic organisms have evolved to activate oxygen from the atmosphere, which
allows them to catalyze the oxidation of different kinds of substrates. This activation of …