Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions
| Autor: | Flora Meilleur, Gabriela C. Schröder, William B. O'Dell, Paul Swartz |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Reaction mechanism
Neutron diffraction Biophysics Protonation 010402 general chemistry Photochemistry 01 natural sciences Biochemistry Method Communications Protein Structure Secondary Catalysis Mixed Function Oxygenases Crystal 03 medical and health sciences chemistry.chemical_compound X-Ray Diffraction Structural Biology Polysaccharides Genetics Cellulose 030304 developmental biology chemistry.chemical_classification 0303 health sciences Neurospora crassa Chemistry Data Collection Glycosidic bond Hydrogen-Ion Concentration Condensed Matter Physics 0104 chemical sciences Neutron Diffraction X-ray crystallography |
| Zdroj: | Acta Crystallogr F Struct Biol Commun |
| Popis: | Lytic polysaccharide monooxygenases (LPMOs) are copper-center enzymes that are involved in the oxidative cleavage of the glycosidic bond in crystalline cellulose and other polysaccharides. The LPMO reaction is initiated by the addition of a reductant and oxygen to ultimately form an unknown activated copper–oxygen species that is responsible for polysaccharide-substrate H-atom abstraction. Given the sensitivity of metalloproteins to radiation damage, neutron protein crystallography provides a nondestructive technique for structural characterization while also informing on the positions of H atoms. Neutron cryo-crystallography permits the trapping of catalytic intermediates, thereby providing insight into the protonation states and chemical nature of otherwise short-lived species in the reaction mechanism. To characterize the reaction-mechanism intermediates of LPMO9D from Neurospora crassa, a cryo-neutron diffraction data set was collected from an ascorbate-reduced crystal. A second neutron diffraction data set was collected at room temperature from an LPMO9D crystal exposed to low-pH conditions to probe the protonation states of ionizable groups involved in catalysis under acidic conditions. |
| Databáze: | OpenAIRE |
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