Interpretation of the temperature dependence of rate constants in biosensor studies.
A comparison is made between Arrhenius and transition-state analyses of the temperature dependence of rate constants reported in four published biosensor studies. Although the Eyring transition-state theory seemingly affords a more definitive solution to the problem of characterizing the activation energetics, the analysis is equivocal because of inherent assumptions about reaction mechanism and the magnitude of the transmission coefficient. In view of those uncertainties it is suggested that a preferable course of action entails reversion to the empirical Arrhenius analysis with regard to the energy of activation and a preexponential factor. The former is essentially equivalent to the enthalpy of activation, whereas the magnitude of the latter indicates directly the extent of disparity between the frequency of product formation and the universal frequency factor (temperature multiplied by the ratio of the Boltzmann and Planck constants) and hence the likelihood of a more complicated kinetic mechanism than that encompassed by the Eyring transition-state theory.
Winzor
Donald J
DJ
Department of Biochemistry, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld. 4072, Australia. d.winzor@mailbox.uq.edu.au
Jackson
Craig M
CM
D015374:Biosensing Techniques / Q000379:methods*; D004791:Enzyme Inhibitors / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D013696:Temperature; D013816:Thermodynamics; D048051:p38 Mitogen-Activated Protein Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism
D004791:Enzyme Inhibitors; D048051:p38 Mitogen-Activated Protein Kinases