Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase-Reference-Cited by-同舟云学术

Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase

Published:2022 Issue:45 Volume:13 Page:13303-13320
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Schröder Gabriela C.¹²^ORCID,O'Dell William B.¹²^ORCID,Webb Simon P.³^ORCID,Agarwal Pratul K.⁴^ORCID,Meilleur Flora¹²^ORCID

Affiliation:

1. Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA

2. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA

3. VeraChem LLC, 12850 Middlebrook Rd. Ste 205, Germantown, MD 20874-5244, USA

4. Department of Physiological Sciences and High-Performance Computing Center, Oklahoma State University, Stillwater, OK 74078, USA

Abstract

Superoxo and hydroperoxo intermediates were cryotrapped at the copper active site of lytic polysaccharide monooxygenase using neutron protein crystallography.

Funder

Oak Ridge National Laboratory

Basic Energy Sciences

North Carolina State University

U.S. Department of Agriculture

National Institute of Food and Agriculture

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC05031E

Reference111 articles.

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3. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components

4. Activity, stability and 3-D structure of the Cu(ii) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens

5. The framework of polysaccharide monooxygenase structure and chemistry

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