Free Energy of Activation for the Comorosan Effect

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dc.creatorBass, George E.
dc.creatorMeibohm, Bernd
dc.creatorDalton, James T.
dc.creatorSayre, Robert
dc.date2007-06-11
dc.date.accessioned2026-07-07T08:04:56Z
dc.date.available2026-07-07T08:04:56Z
dc.descriptionInitial 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.
dc.description21 pages, 3 figures, 2 tables
dc.identifierhttps://arxiv.org/abs/0706.1504
dc.identifierhttp://arxiv.org/abs/0706.1504
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/130146
dc.subjectSubcellular Processes
dc.subjectBiomolecules
dc.titleFree Energy of Activation for the Comorosan Effect
dc.typetext

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