Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase.

Journal

ACS catalysis
ISSN: 2155-5435
Titre abrégé: ACS Catal
Pays: United States
ID NLM: 101562209

Informations de publication

Date de publication:
01 May 2020
Historique:
received: 13 02 2020
revised: 30 03 2020
entrez: 9 5 2020
pubmed: 10 5 2020
medline: 10 5 2020
Statut: ppublish

Résumé

Large-scale protein domain dynamics and electron transfer are often associated. However, as protein motions span a broad range of time and length scales, it is often challenging to identify and thus link functionally relevant dynamic changes to electron transfer in proteins. It is hypothesized that large-scale domain motions direct electrons through a FAD and a heme

Identifiants

DOI: 10.1021/acscatal.0c00754 PMID: 32382450 PMC: PMC7199207
pubmed: 32382450
doi: 10.1021/acscatal.0c00754
pmc: PMC7199207
doi:

Types de publication

Journal Article

Langues

eng

Pagination

4842-4853

Subventions

Organisme : Austrian Science Fund FWF
ID : W 1224
Pays : Austria

Informations de copyright

Copyright © 2020 American Chemical Society.

Déclaration de conflit d'intérêts

The authors declare no competing financial interest.

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Auteurs

Erik Breslmayr (E)

Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.
Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Department of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, Muthgasse 18, 1190 Vienna, Austria.

Christophe V F P Laurent (CVFP)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Department of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, Muthgasse 18, 1190 Vienna, Austria.

Stefan Scheiblbrandner (S)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.

Anita Jerkovic (A)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.

Derren J Heyes (DJ)

Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.

Chris Oostenbrink (C)

Department of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, Muthgasse 18, 1190 Vienna, Austria.

Roland Ludwig (R)

Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.

Tobias M Hedison (TM)

Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.
EPSRC/BBSRC funded Future Biomanufacturing Research Hub, The Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.

Nigel S Scrutton (NS)

Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.
EPSRC/BBSRC funded Future Biomanufacturing Research Hub, The Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.

Daniel Kracher (D)

Manchester Institute of Biotechnology, The University of Manchester, M1 7DN Manchester, United Kingdom.
Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.

Classifications MeSH