Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase
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Updated: Aug 18, 2026

Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue
Published on: June 21, 2018
Sebastian McClendon1, Dung M Vu, Keith Clinch
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, 10461, USA.
Abstract:
The dynamical nature of the binding of a substrate surrogate to lactate dehydrogenase is examined on the nanoseconds to milliseconds timescale by laser-induced temperature-jump relaxation spectroscopy. Fluorescence emission of the nicotinamide group of bound NADH is used to define the pathway and kinetics of substrate binding. Assignment of specific kinetic states and elucidation of their structures are accomplished using isotope edited infrared absorption spectroscopy. Such studies are poised to yield a detailed picture of the coupling of protein dynamics to function.
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