The location of active site opening and closing events in the prehydride transfer phase of the oxidative deamination reaction catalyzed by bovine liver glutamate dehydrogenase using a novel pH jump approach.
A pH jump approach has been developed and used to locate the opening and closing events occurring in the time course of the beef liver glutamate dehydrogenase catalyzed reaction. A comparison of the pH jump results, the resolved component time courses, and the 340 nm fluorescence signal suggests the existence and location on the reaction time course of a previously unreported prehydride transfer complex.
Saha
S K
SK
Laboratory of Molecular Biochemistry, Veterans Affairs Medical Center and Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, MO 64128, USA.
Fisher
H F
HF
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*
D005969:Glutamate Dehydrogenase