title: Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases.
abstract: 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.
authors.affiliation: Department of Chemistry, University of California, Berkeley, California 94720, USA.
authors.forename: William T
authors.initials: WT
authors.lastname: Beeson
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Phillips
authors.forename: Jamie H D
authors.initials: JH
authors.lastname: Cate
authors.forename: Michael A
authors.initials: MA
authors.lastname: Marletta
mesh_terms: D002236:Carbohydrate Conformation; D002482:Cellulose / Q000031:analogs & derivatives / Q000378:metabolism*; D003300:Copper / Q000737:chemistry*; D003912:Dextrins / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009492:Neurospora crassa / Q000201:enzymology*; D010084:Oxidation-Reduction
chemical_list: D003912:Dextrins; D003300:Copper; D002482:Cellulose; D006899:Mixed Function Oxygenases