Free Energy of Activation for the Comorosan Effect

TL;DR

This study quantifies the activation free energy changes in enzyme reactions influenced by time-specific irradiation of crystalline substrates, suggesting a role for photoproducts from atmospheric gases rather than direct substrate excitation.

Contribution

It provides the first quantitative analysis of activation free energies associated with the Comorosan effect, linking reaction rate increases to conformational changes and atmospheric gas photoproducts.

Findings

Activation free energies are -329, -195, and -221 cal/mole for the studied reactions.

Approximately 10% of irradiation energy could account for observed rate increases.

Photoproducts from atmospheric gases, not substrate photo-excitation, likely cause the effect.

Abstract

Initial reaction rate data for lactic dehydrogenase / pyruvate, lactic dehydrogenase / lactate and malic dehydrogenase / malate enzyme reactions were analyzed to obtain activation free energy changes of -329, -195 and -221 cal/mole, respectively, for rate increases associated with time-specific irradiation of the crystalline substrates prior to dissolution and incorporation in the reaction solutions. These energies, presumably, correspond to conformational or vibrational changes in the reactants or the activated complex. For the lactic dehydrogenase / pyruvate reaction, it is estimated that on the order of 10% of the irradiation energy (546 nm, 400 footcandles for 5 seconds) would be required to produce the observed reaction rate increase if a presumed photoproduct is consumed stoichiometrically with the pyruvate substrate. These findings are consistent with the proposition that the observed reaction rate enhancement involves photoproducts derived from oscillatory atmospheric gas reactions at the crystalline enzyme substrate surfaces rather than photo-excitations of the substrate molecules, per se.