Activation thermodynamics of the binding of carbon monoxide to horseradish peroxidase. Role of pressure, temperature and solvent.
The kinetics at 423 nm of the binding of carbon monoxide to ferrous horseradish peroxidase were studied as a function of three parameters: pressure (1-1200 bar), temperature (34 to -20 degrees C) and solvent (water, 40% ethylene glycol, 50% methanol) using a high-pressure stopped-flow apparatus. By using transition state theory the thermodynamic quantities delta V, delta S and delta H were determined under these different experimental conditions and were found to be greatly modulated by the physico-chemical parameters of the media. The results suggest that the macroscopic thermodynamic response is mainly controlled by the solvent. By adjusting two variables (among T, P, solvent), it is possible either to amplify or to cancel out the effect of the third.
Balny
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C
Institute National de la Santé et de la Recherche Médicale, U 128, C.N.R.S., Montpellier, France.
Travers
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F
D002248:Carbon Monoxide / Q000378:metabolism*; D004789:Enzyme Activation; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D010544:Peroxidases / Q000378:metabolism*; D011312:Pressure; D011485:Protein Binding; D013816:Thermodynamics
D002248:Carbon Monoxide; D006735:Horseradish Peroxidase; D010544:Peroxidases