Enzymatic cellulose oxidation is linked to lignin by long-range electron transfer

Bjorge Westereng, David Cannella, Jane Wittrup Agger, Henning Jørgensen, Mogens Larsen Andersen, Vincent G. H. Eijsink, Claus Felby

Research output: Contribution to journalJournal articleResearchpeer-review

235 Downloads (Pure)


Enzymatic oxidation of cell wall polysaccharides by lytic polysaccharide monooxygenases (LPMOs) plays a pivotal role in the degradation of plant biomass. While experiments have shown that LPMOs are copper dependent enzymes requiring an electron donor, the mechanism and origin of the electron supply in biological systems are only partly understood. We show here that insoluble high molecular weight lignin functions as a reservoir of electrons facilitating LPMO activity. The electrons are donated to the enzyme by long-range electron transfer involving soluble low molecular weight lignins present in plant cell walls. Electron transfer was confirmed by electron paramagnetic resonance spectroscopy showing that LPMO activity on cellulose changes the level of unpaired electrons in the lignin. The discovery of a long-range electron transfer mechanism links the biodegradation of cellulose and lignin and sheds new light on how oxidative enzymes present in plant degraders may act in concert.
Original languageEnglish
Article number18561
JournalScientific Reports
Number of pages9
Publication statusPublished - 2015


Dive into the research topics of 'Enzymatic cellulose oxidation is linked to lignin by long-range electron transfer'. Together they form a unique fingerprint.

Cite this