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Biophys. J. BioFAST: First Published May 6, 2005. doi:10.1529/biophysj.105.064675
© 2005 by the Biophysical Society.

A more recent version of this article appeared on July 1, 2005.
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BIOPHYSICAL LETTERS

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

Sebastian McClendon 1, Dung M Vu 2, Keith Clinch 3, Robert Callender 1 and Brian Dyer 2*

1 Albert Einstein College of Medicine
2 Los Alamos National Lab
3 Industrial Research, NZ

* To whom correspondence should be addressed. E-mail: bdyer{at}lanl.gov.

Submitted on April 13, 2005
Revised on April 19, 2005
Accepted on 26 April 2005


  Abstract
The dynamical nature of the binding of a substrate surrogate to lactate dehydrogenase is examined on the nanoseconds to milliseconds time scale 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.

Key Words: dehydrogenase, dynamics, enzyme, infrared, isotope, temperature jump




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Copyright © 2005 by the Biophysical Society.