Copper–oxygen complexes revisited: structures, spectroscopy, and reactivity

CE Elwell, NL Gagnon, BD Neisen, D Dhar… - Chemical …, 2017 - ACS Publications
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-Promoted Functionalization of Organic Molecules: from Biologically Relevant Cu/O2 Model Systems to Organometallic Transformations

R Trammell, K Rajabimoghadam… - Chemical …, 2019 - ACS Publications
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 …

Bioinspired metal–organic framework catalysts for selective methane oxidation to methanol

J Baek, B Rungtaweevoranit, X Pei… - Journal of the …, 2018 - ACS Publications
Particulate methane monooxygenase (pMMO) is an enzyme that oxidizes methane to
methanol with high activity and selectivity. Limited success has been achieved in …

Phenol-directed C–H functionalization

Z Huang, JP Lumb - ACS Catalysis, 2018 - ACS Publications
Phenols are important starting materials, intermediates, and functional elements of a very
broad range of chemicals and materials. They are large-volume products of benzene …

Design and optimization of catalysts based on mechanistic insights derived from quantum chemical reaction modeling

S Ahn, M Hong, M Sundararajan, DH Ess… - Chemical …, 2019 - ACS Publications
Until recently, computational tools were mainly used to explain chemical reactions after
experimental results were obtained. With the rapid development of software and hardware …

Oxidation Reactions with Bioinspired Mononuclear Non‐Heme Metal–Oxo Complexes

X Engelmann, I Monte‐Pérez… - Angewandte Chemie …, 2016 - Wiley Online Library
The selective functionalization of strong C− H bonds and the oxidation of water by cheap
and nontoxic metals are some of the key targets of chemical research today. It has been …

Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function

SM Adam, GB Wijeratne, PJ Rogler, DE Diaz… - Chemical …, 2018 - ACS Publications
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Formation of [Cu2O2]2+ and [Cu2O]2+ toward C–H Bond Activation in Cu-SSZ-13 and Cu-SSZ-39

B Ipek, MJ Wulfers, H Kim, F Goltl, I Hermans… - Acs …, 2017 - ACS Publications
Cu-exchanged small-pore zeolites (CHA and AEI) form methanol from methane (> 95%
selectivity) using a 3-step cyclic procedure (Wulfers et al. Chem. Commun. 2015, 51, 4447 …

Activation of dioxygen by copper metalloproteins and insights from model complexes

DA Quist, DE Diaz, JJ Liu, KD Karlin - JBIC Journal of Biological Inorganic …, 2017 - Springer
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 …

Bracing copper for the catalytic oxidation of C–H bonds

L Ciano, GJ Davies, WB Tolman, PH Walton - Nature Catalysis, 2018 - nature.com
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 …