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Conformational selection or induced fit: A flux description of reaction mechanism
- G. Hammes, Yu-Chu Chang, T. Oas
- Chemistry, BiologyProceedings of the National Academy of Sciences
- 18 August 2009
A mixed mechanism likely will be discovered for many cases of coupled conformational change and ligand binding when kinetic data are analyzed by using a flux-based approach.
Interaction of dihydrofolate reductase with methotrexate: Ensemble and single-molecule kinetics
- P. Rajagopalan, Zhiquan Zhang, Lynn McCourt, M. Dwyer, S. Benkovic, G. Hammes
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 1 October 2002
The thermodynamics and kinetics of the interaction of dihydrofolate reductase with methotrexate have been studied by using fluorescence, stopped-flow, and single-molecule methods, and the association and dissociation rate constants were determined.
Calculation on fluorescence resonance energy transfer on surfaces.
Application of the Theory of Diffusion-controlled Reactions to Enzyme Kinetics
Binding of phosphate ligands to ribonuclease A.
Free-energy landscape of enzyme catalysis.
Experimental and theoretical evidence is presented to support the concept that enzyme mechanisms should be viewed as "catalytic networks" with multiple conformations that occur serially and in parallel in the mechanism.
ELEMENTARY STEPS IN ENZYME REACTIONS (AS STUDIED BY RELAXATION SPECTROMETRY).
Flexibility, diversity, and cooperativity: pillars of enzyme catalysis.
A general mechanism is presented for enzyme catalysis that includes multiple intermediates and a complex, multidimensional standard free energy surface and protein flexibility, diverse protein conformations, and cooperative conformational changes are important features of this model.
Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation.
The results obtained suggest only about half of the acetylation reactions are on the main catalytic pathway, apparently because dead-end intramolecular transfers of acetyl groups from the lipoic acids to other functional groups on the enzyme not essential for catalytic activity can occur.