Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase

Sebastian McClendon, Dung M. Vu, Keith Clinch, Robert Callender, R. Brian Dyer

Research output: Contribution to journalArticle

24 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)L07-L09
JournalBiophysical journal
Issue number1
StatePublished - Jul 2005


ASJC Scopus subject areas

  • Biophysics

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