Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases

J Am Chem Soc. 2012 Jan 18;134(2):890-2. doi: 10.1021/ja210657t. Epub 2011 Dec 28.


Fungal-derived, copper-dependent polysaccharide monooxygenases (PMOs), formerly known as GH61 proteins, have recently been shown to catalyze the O(2)-dependent oxidative cleavage of recalcitrant polysaccharides. Different PMOs isolated from Neurospora crassa were found to generate oxidized cellodextrins modified at the reducing or nonreducing ends upon incubation with cellulose and cellobiose dehydrogenase. Here we show that the nonreducing end product formed by an N. crassa PMO is a 4-ketoaldose. Together with isotope labeling experiments, further support is provided for a mechanism involving oxygen insertion and subsequent elimination to break glycosidic bonds in crystalline cellulose.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Carbohydrate Conformation
  • Cellulose / analogs & derivatives
  • Cellulose / metabolism*
  • Copper / chemistry*
  • Dextrins / chemistry
  • Mixed Function Oxygenases / chemistry
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Neurospora crassa / enzymology*
  • Oxidation-Reduction


  • Dextrins
  • Copper
  • Cellulose
  • Mixed Function Oxygenases