Oxidative Cleavage of Cellulose by Fungal Copper-Dependent Polysaccharide Monooxygenases

被引：367

作者：

Beeson, William T. ^{[1
]}

Phillips, Christopher M. ^{[2
]}

Cate, Jamie H. D. ^{[1
,2
,3
,4
]}

Marletta, Michael A. ^{[1
,2
,3
,4
]}

机构：

[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Calif Inst Quantitat Biosci, Berkeley, CA 94720 USA

[4] Univ Calif Berkeley, Lawrence Berkeley Natl Lab, Div Phys Biosci, Berkeley, CA 94720 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2012年 / 134卷 / 02期

关键词：

GLYCOSIDE HYDROLASE FAMILY; NEUROSPORA-CRASSA; MYCELIOPHTHORA-THERMOPHILA; CELLOBIOSE DEHYDROGENASE; DEGRADATION; CONVERSION; ENZYMES;

D O I：

10.1021/ja210657t

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：890 / 892

页数：3

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