Extracellular electron transfer systems fuel cellulose oxidative degradation

See allHide authors and affiliations

Science  27 May 2016:
Vol. 352, Issue 6289, pp. 1098-1101
DOI: 10.1126/science.aaf3165

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

The fuel for fungal enzymes

Many microorganisms have specialized enzymes to target and break down plant biomass. In fungi, these enzymes, called lytic polysaccharide monooxygenases (LPMOs), partner with electron transfer partners to oxidatively cleave the polysaccharide backbone of lignocellulosic polymers. Kracher et al. examined several potential extracellular electron transfer partners for LPMO, including other enzymes and small redoxactive metabolites (see the Perspective by Martínez). All three were able to donate electrons to the single-copper active site. Such versatility helps these fungi adapt to a range of redox conditions and potentially use other extracellular electron donors to fuel biomass degradation.

Science, this issue p. 1098; see also p. 1050


Ninety percent of lignocellulose-degrading fungi contain genes encoding lytic polysaccharide monooxygenases (LPMOs). These enzymes catalyze the initial oxidative cleavage of recalcitrant polysaccharides after activation by an electron donor. Understanding the source of electrons is fundamental to fungal physiology and will also help with the exploitation of LPMOs for biomass processing. Using genome data and biochemical methods, we characterized and compared different extracellular electron sources for LPMOs: cellobiose dehydrogenase, phenols procured from plant biomass or produced by fungi, and glucose-methanol-choline oxidoreductases that regenerate LPMO-reducing diphenols. Our data demonstrate that all three of these electron transfer systems are functional and that their relative importance during cellulose degradation depends on fungal lifestyle. The availability of extracellular electron donors is required to activate fungal oxidative attack on polysaccharides.

View Full Text

Stay Connected to Science