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Originally published as Biophys J. BioFAST on May 6, 2005.
doi:10.1529/biophysj.105.064675
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Biophysical Journal 89:L07-L09 (2005)
© 2005 The Biophysical Society

Structural Transformations in the Dynamics of Michaelis Complex Formation in Lactate Dehydrogenase

Sebastian McClendon *, Dung M. Vu {dagger}, Keith Clinch {ddagger}, Robert Callender * and R. Brian Dyer {dagger}

* Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, 10461; {dagger} Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87545; and {ddagger} Industrial Research, Lower Hutt, New Zealand

Correspondence: Address reprint requests to R. B. Dyer, Tel.: 505-667-4194; Fax: 505-667-0851; E-mail: bdyer{at}lanl.gov.

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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