期刊
NATURE COMMUNICATIONS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms8542
关键词
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资金
- Swedish Research Council FORMAS [2008-495, 2013-1741]
- Swedish Research Council VR [2008-4056, 2011-5768, 2011-6510]
- Carl Tryggers Foundation [CTS08:78]
- European Commission Project INDOX [FP7-KBBE-2013-7-613549]
- Austrian Science Fund (FWF) [P25148-B20]
- Doctoral programme 'BioToP-Biomolecular Technology of Proteins' (FWF) [W1224]
- European Community's Seventh Framework Programme (FP7) under BioStruct-X [283570]
- DOE Office of Biological and Environmental Research
- National Institute of Health project MINOS [R01GM105404]
- MAX II SAXS beamline at MAX IV Laboratory, Lund, Sweden [I911-SAXS]
- WeNMR project (European FP7 e-Infrastructure grant) [261572]
- European Grid Initiative (EGI) through the national GRID Initiative of Belgium
- European Grid Initiative (EGI) through the national GRID Initiative of France
- European Grid Initiative (EGI) through the national GRID Initiative of Italy
- European Grid Initiative (EGI) through the national GRID Initiative of Germany
- European Grid Initiative (EGI) through the national GRID Initiative of the Netherlands
- European Grid Initiative (EGI) through the national GRID Initiative of Poland
- European Grid Initiative (EGI) through the national GRID Initiative of Portugal
- European Grid Initiative (EGI) through the national GRID Initiative of Spain
- European Grid Initiative (EGI) through the national GRID Initiative of UK
- European Grid Initiative (EGI) through the national GRID Initiative of South Africa
- European Grid Initiative (EGI) through the national GRID Initiative of Malaysia
- European Grid Initiative (EGI) through the national GRID Initiative of Taiwan
- Latin America GRID infrastructure via the Gisela project
- International Desktop Grid Federation (IDGF)
- US Open Science Grid (OSG)
- Austrian Science Fund (FWF) [P25148] Funding Source: Austrian Science Fund (FWF)
A new paradigm for cellulose depolymerization by fungi focuses on an oxidative mechanism involving cellobiose dehydrogenases (CDH) and copper-dependent lytic polysaccharide monooxygenases (LPMO); however, mechanistic studies have been hampered by the lack of structural information regarding CDH. CDH contains a haem-binding cytochrome (CYT) connected via a flexible linker to a flavin-dependent dehydrogenase (DH). Electrons are generated from cellobiose oxidation catalysed by DH and shuttled via CYT to LPMO. Here we present structural analyses that provide a comprehensive picture of CDH conformers, which govern the electron transfer between redox centres. Using structure-based site-directed mutagenesis, rapid kinetics analysis and molecular docking, we demonstrate that flavin-tohaem interdomain electron transfer (IET) is enabled by a haem propionate group and that rapid IET requires a closed CDH state in which the propionate is tightly enfolded by DH. Following haem reduction, CYT reduces LPMO to initiate oxygen activation at the copper centre and subsequent cellulose depolymerization.
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