Related Experiment Video
Updated: Mar 25, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Dihydrofolate reductase as a model for studies of enzyme dynamics and catalysis
1Department of Chemistry, University of Iowa, Iowa City, IA, USA.
Abstract:
Dihydrofolate reductase from Escherichia coli (ecDHFR) serves as a model system for investigating the role of protein dynamics in enzyme catalysis. We discuss calculations predicting a network of dynamic motions that is coupled to the chemical step catalyzed by this enzyme. Kinetic studies testing these predictions are presented, and their potential use in better understanding the role of these dynamics in enzyme catalysis is considered. The cumulative results implicate motions across the entire protein in catalysis.
More Related Videos
Related Concept Videos
Induced-fit Model
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Catalytically Perfect Enzymes
Most enzymes...
Introduction to Mechanisms of Enzyme Catalysis
Introduction to Mechanisms of Enzyme Catalysis
Phase I Reactions: Reductive Reactions
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

