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 …

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 …

The general atomic and molecular electronic structure system (GAMESS): novel methods on novel architectures

F Zahariev, P Xu, BM Westheimer, S Webb… - Journal of Chemical …, 2023 - ACS Publications
The primary focus of GAMESS over the last 5 years has been the development of new high-
performance codes that are able to take effective and efficient advantage of the most …

Copper–oxygen adducts: new trends in characterization and properties towards C–H activation

J De Tovar, R Leblay, Y Wang, L Wojcik… - Chemical …, 2024 - pubs.rsc.org
This review summarizes the latest discoveries in the field of C–H activation by copper
monoxygenases and more particularly by their bioinspired systems. This work first describes …

Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition

J Azadmanesh, K Slobodnik, LR Struble… - Nature …, 2024 - nature.com
Human manganese superoxide dismutase (MnSOD) is a crucial oxidoreductase that
maintains the vitality of mitochondria by converting superoxide (O2●−) to molecular oxygen …

A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase

Y Liu, KA Harnden, C Van Stappen… - Proceedings of the …, 2023 - National Acad Sciences
The “Histidine-brace”(His-brace) copper-binding site, composed of Cu (His) 2 with a
backbone amine, is found in metalloproteins with diverse functions. A primary example is …

Perdeuterated GbpA enables neutron scattering experiments of a lytic polysaccharide monooxygenase

HV Sørensen, M Montserrat-Canals, JSM Loose… - ACS …, 2023 - ACS Publications
Lytic polysaccharide monooxygenases (LPMOs) are surface-active redox enzymes that
catalyze the degradation of recalcitrant polysaccharides, making them important tools for …

Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure

KW Rush, KAS Eastman, EF Welch… - Journal of the …, 2024 - ACS Publications
Peptidylglycine monooxygenase is a copper-dependent enzyme that catalyzes C-alpha
hydroxylation of glycine extended pro-peptides, a critical post-translational step in peptide …

Current insights of factors interfering the stability of lytic polysaccharide monooxygenases

M Dan, Y Zheng, G Zhao, YSY Hsieh, D Wang - Biotechnology Advances, 2023 - Elsevier
Cellulose and chitin are two of the most abundant biopolymers in nature, but they cannot be
effectively utilized in industry due to their recalcitrance. This limitation was overcome by the …

Insight into the peroxygenase activity of lytic polysaccharide monooxygenases (LPMO): Recent progress and mechanistic understanding

W Gao, H Yin - Chemical Physics Reviews, 2023 - pubs.aip.org
The discovery of lytic polysaccharide monooxygenases (LPMOs) as monocopper enzymes
for the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides has …