Catalysis and Electron Transfer in De Novo Designed Metalloproteins

KJ Koebke, TBJ Pinter, WC Pitts, VL Pecoraro - Chemical reviews, 2022 - ACS Publications
One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Lytic polysaccharide monooxygenases: enzymes for controlled and site-specific Fenton-like chemistry

B Bissaro, VGH Eijsink - Essays in biochemistry, 2023 - portlandpress.com
The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic
polysaccharide monooxygenases (LPMOs) has profoundly changed our current …

A conserved second sphere residue tunes copper site reactivity in lytic polysaccharide monooxygenases

KR Hall, C Joseph, I Ayuso-Fernández… - Journal of the …, 2023 - ACS Publications
Lytic polysaccharide monooxygenases (LPMOs) are powerful monocopper enzymes that
can activate strong C–H bonds through a mechanism that remains largely unknown. Herein …

Fenton-like Chemistry by a Copper(I) Complex and H2O2 Relevant to Enzyme Peroxygenase C–H Hydroxylation

B Kim, MT Brueggemeyer, WJ Transue… - Journal of the …, 2023 - ACS Publications
Lytic polysaccharide monooxygenases have received significant attention as catalytic
convertors of biomass to biofuel. Recent studies suggest that its peroxygenase activity (ie …

The “life-span” of lytic polysaccharide monooxygenases (LPMOs) correlates to the number of turnovers in the reductant peroxidase reaction

S Kuusk, VGH Eijsink, P Väljamäe - Journal of Biological Chemistry, 2023 - ASBMB
Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that degrade the
insoluble crystalline polysaccharides cellulose and chitin. Besides the H 2 O 2 cosubstrate …

Amyloid fibrils formed by short prion-inspired peptides are metalloenzymes

S Navarro, M Díaz-Caballero, F Peccati… - ACS …, 2023 - ACS Publications
Enzymes typically fold into defined 3D protein structures exhibiting a high catalytic efficiency
and selectivity. It has been proposed that the earliest enzymes may have arisen from the self …

Functional and protective hole hopping in metalloenzymes

HB Gray, JR Winkler - Chemical Science, 2021 - pubs.rsc.org
Electrons can tunnel through proteins in microseconds with a modest release of free energy
over distances in the 15 to 20 Å range. To span greater distances, or to move faster, multiple …

Expanding the catalytic landscape of metalloenzymes with lytic polysaccharide monooxygenases

A Munzone, VGH Eijsink, JG Berrin… - Nature Reviews …, 2024 - nature.com
Lytic polysaccharide monooxygenases (LPMOs) have an essential role in global carbon
cycle, industrial biomass processing and microbial pathogenicity by catalysing the oxidative …

Deciphering the oxygen activation mechanism at the CuC site of particulate methane monooxygenase

W Peng, X Qu, S Shaik, B Wang - Nature Catalysis, 2021 - nature.com
The enzymatic oxidation of methane to methanol was discovered in methanotrophs over 110
years ago. Nevertheless, the mechanism of action of particulate methane monooxygenase …

Insights into the H2O2‐driven catalytic mechanism of fungal lytic polysaccharide monooxygenases

TM Hedison, E Breslmayr, M Shanmugam… - The FEBS …, 2021 - Wiley Online Library
Fungal lytic polysaccharide monooxygenases (LPMOs) depolymerise crystalline cellulose
and hemicellulose, supporting the utilisation of lignocellulosic biomass as a feedstock for …