We present an update and revision to our 2010 review on the topic of proton-coupled
electron transfer (PCET) reagent thermochemistry. Over the past decade, the data and …

A longstanding research goal has been to understand the nature and role of copper–oxygen
intermediates within copper-containing enzymes and abiological catalysts. Synthetic …

Copper is one of the most abundant and less toxic transition metals. Nature takes advantage
of the bioavailability and rich redox chemistry of Cu to carry out oxygenase and oxidase …

Lytic polysaccharide monooxygenases (LPMOs) are powerful monocopper enzymes that
can activate strong C–H bonds through a mechanism that remains largely unknown. Herein …

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

Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …

Highlights•Lytic polysaccharide monooxygenases are newly discovered copper
oxygenases.•LPMOs open up new thinking about oxidation mechanisms.•Copper histidine …

A structural unit found in the active site of some copper proteins, the histidine brace, is
comprised of an N-terminal histidine that chelates a single copper ion through its amino …

Coordination of alcohols to the single-electron reductant samarium diiodide (SmI2) results in
substantial O–H bond weakening, affording potent proton-coupled electron transfer (PCET) …

We report the systematic development of an electrooxidative methodology that translates
stoichiometric C–H fluorination reactivity of an isolable Cu III fluoride complex into a catalytic …