Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation

Tien-Chye Tan, Daniel Kracher, Rosaria Gandini, Christoph Sygmund, Roman Kittl, Dietmar Haltrich, B. Martin Hällberg, Roland Ludwig () and Christina Divne ()
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Tien-Chye Tan: School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center
Daniel Kracher: Food Biotechnology Laboratory, Vienna Institute of Biotechnology (VIBT), BOKU—University of Natural Resources and Life Sciences
Rosaria Gandini: School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center
Christoph Sygmund: Food Biotechnology Laboratory, Vienna Institute of Biotechnology (VIBT), BOKU—University of Natural Resources and Life Sciences
Roman Kittl: Food Biotechnology Laboratory, Vienna Institute of Biotechnology (VIBT), BOKU—University of Natural Resources and Life Sciences
Dietmar Haltrich: Food Biotechnology Laboratory, Vienna Institute of Biotechnology (VIBT), BOKU—University of Natural Resources and Life Sciences
B. Martin Hällberg: Karolinska Institutet
Roland Ludwig: Food Biotechnology Laboratory, Vienna Institute of Biotechnology (VIBT), BOKU—University of Natural Resources and Life Sciences
Christina Divne: School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract 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-to-haem 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.

Date: 2015
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DOI: 10.1038/ncomms8542

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