XI is an important enzyme because it can convert sugars that resist bioconversion to fuel into those readily fermented by, for example, yeasts. Through neutron diffraction experiments at the Los Alamos Neutron Science Center, researchers were able to map the positioning of individual hydrogen atoms as XI moves them from one carbon to another on a sugar molecule. They were able to model how specific amino acids in the XI structure are involved in proton movement. Results may enable new approaches for modifying the enzyme to improve its performance for biofuel and other applications. This research was featured on the June 9, 2010, cover of Structure.
Reference: Kovalevsky, A. Y., et al. 2010. “Metal Ion Roles and the Movement of Hydrogen During Reaction Catalyzed by D-Xylose Isomerase: A Joint X-Ray and Neutron Diffraction Study,” Structure 18, 688–99.
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