title: Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase.
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.
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, 10461, USA.
authors.forename: Sebastian
authors.initials: S
authors.lastname: McClendon
authors.forename: Dung M
authors.initials: DM
authors.lastname: Vu
authors.forename: Keith
authors.initials: K
authors.lastname: Clinch
authors.forename: Robert
authors.initials: R
authors.lastname: Callender
authors.forename: R Brian
authors.initials: RB
authors.lastname: Dyer
mesh_terms: D001665:Binding Sites; D001703:Biophysics / Q000379:methods*; D002384:Catalysis; D006860:Hydrogen Bonding; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000737:chemistry*; D007834:Lasers; D008956:Models, Chemical; D009243:NAD / Q000737:chemistry; D009536:Niacinamide / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D017550:Spectroscopy, Fourier Transform Infrared; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
chemical_list: D011506:Proteins; D009243:NAD; D009536:Niacinamide; D007770:L-Lactate Dehydrogenase