Many fungi growing on plant biomass produce proteins currently classified as glycoside hydrolase family 61 (GH61), some of which are known to act synergistically with cellulases. In this study we show that PcGH61D, the gene product of an open reading frame in the genome of Phanerochaete chrysosporium, is an enzyme that cleaves cellulose using a metal-dependent oxidative mechanism that leads to generation of aldonic acids. The activity of this enzyme and its beneficial effect on the efficiency of classical cellulases are stimulated by the presence of electron donors. Experiments with reduced cellulose confirmed the oxidative nature of the reaction catalyzed by PcGH61D and indicated that the enzyme may be capable of penetrating into the substrate. Considering the abundance of GH61-encoding genes in fungi and genes encoding their functional bacterial homologues currently classified as carbohydrate binding modules family 33 (CBM33), this enzyme activity is likely to turn out as a major determinant of microbial biomass-degrading efficiency.

Background: Lytic polysaccharide monooxygenases (LPMOs) represent a recently discovered enzymatic route to cleave carbohydrates. Results:We report the first basidiomycete LPMO structure and describe enzyme-cellulose interactions with simulation. Conclusion:We characterize the copper-containing active site and identify loops important for substrate recognition and binding. Significance: This structure is the first LPMO from a model basidiomycete fungus that contains many LPMO genes.

We have demonstrated that the electronic and magnetic properties of graphene sheet can be delicately tuned by surface modification. Applying an external electric field to a fully hydrogenated graphene sheet can unload hydrogen atoms on one side, while keeping the hydrogen atoms on the other side, thus forming a half-hydrogenated graphene sheet, where the unpaired electrons in the unsaturated C sites give rise to magnetic moments, coupled through extended p-p interactions. Furthermore, the electronic structure of the resulting half-hydrogenated graphene sheet can be further tuned by introducing F atoms on the other side, making a nonmagnetic semiconductor with a direct band gap.

Background: Lytic polysaccharide monooxygenases (LPMOs) exhibit a copper center that binds dioxygen for catalysis. Results: We present LPMO structures from Cu(II) to Cu(I) and analyze the transition with quantum mechanical calculations. Conclusion: Reduction changes the copper coordination state but requires only minor structural and electronic changes. Significance: These structures provide insight into LPMO catalytic activation for further mechanistic studies.

Magnetic superoxidizers: A series of magnetic superhalogens formed of (MnxCl2x+1)− units has been discovered (see picture; Mn violet, Cl green). The series was characterized by photoelectron spectroscopy, mass spectrometry, and theoretical studies.