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 …

Heme proteins utilize the heme cofactor, an iron porphyrin, to perform a diverse range of
reactions including dioxygen binding and transport, electron transfer, and oxidation …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Protein lysine methylation is a distinct posttranslational modification that causes minimal
changes in the size and electrostatic status of lysine residues. Lysine methylation plays …

The coordination chemistry of corrole is one of the most intriguing aspects of this contracted
porphyrinoid, for both theoretical and practical reasons. Corrole, in fact, shows a remarkable …

Lytic polysaccharide monooxygenases have received significant attention as catalytic
convertors of biomass to biofuel. Recent studies suggest that its peroxygenase activity (ie …

The increasing global energy and environmental crises make it urgent to find and use
renewable, clean, and environmentally benign new energy resources. New energy …

Enzymes are highly efficient catalysts in Nature that often react with high stereo-, chemo-,
and regioselectivity. Usually, enzymes achieve this selectivity through substrate binding and …

Despite the growing interest in the synthesis of fluorinated organic compounds, few
reactions are able to incorporate fluoride ions directly into alkyl C–H bonds. Here, we report …

Herein, we describe a convenient and general method for the oxidation of olefins to ketones
using either tris (dibenzoylmethanato) iron (III)[Fe (dbm) 3] or a combination of iron (II) …