Related Experiment Video
Updated: Jun 28, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Simultaneous determination of kinetic and thermodynamic parameters from fast-reaction kinetic measurements
H H Trimm1, H Ushio, R C Patel
1Chemistry Department, Clarkson College of Technology, Potsdam, NY 13676, U.S.A.
Abstract:
A combined stopped-flow temperature-jump apparatus interfaced with a dedicated microcomputer has been used to study the complexation reaction of iron(III) with thiocyanate in aqueous solution. Kinetic rate-constants (k(f) = 143 l.mole(-1) .sec(-1) from T-jump, k(f) = 150 l.mole(-1) .sec(-1) from stopped flow), equilibrium constants (K = 143 from T-jump, K = 150 from stopped flow) and the thermodynamic enthalpy change (DeltaH(c) = -6.7 kJ/mole) could be independently determined from the simultaneous application of the two techniques.
Related Concept Videos
Fast Reactions
Measuring Reaction Rates
Introduction to Enzyme Kinetics
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Predicting Reaction Outcomes
Reversible or Opposing Reactions
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

