Entropy changes drive the electron transfer reaction of triplet flavin mononucleotide from aromatic amino acids in cation-organized aqueous media. A laser-induced optoacoustic study.

The thermodynamic parameters for the formation of the free radicals upon electron transfer quenching of the flavin triplet state (3FMN) by tryptophan and tyrosine, Delta(FR)H and Delta(FR)V, were obtained in aqueous solution by the application of laser-induced optoacoustic spectroscopy at various temperatures. The Delta(FR)H and Delta(FR)V values include the electron transfer and charge separation steps plus the protonation of the FMN anion radical and the deprotonation of the amino-acid cation radical. A linear correlation was found between the Delta(FR)H and Delta(FR)V values for each of the amino acids in phosphate buffers of [CH3(CH2)3]4N+, Li+, NH4+, K+ and Cs+. The compensation between Delta(FR)H and Delta(FR)V within the salt series, and the independent evaluation of the Gibbs energy for electron transfer Delta(ET)G(o) afforded the entropy change, Delta(FR)S, for the reaction, different for the two amino acids. The values of Delta(FR)H, Delta(FR)V and Delta(FR)S in each buffer are mainly determined by the changes in strength and probably number of hydrogen bonds between the reacting partners and water produced along all steps leading to the radicals FMNH* and A*. The Delta(FR)V values linearly correlate with the tabulated entropy of organization of the water structure for the five cations, DeltaS(o)(cat). The entropy change upon formation of the free radicals, Delta(FR)S, quantitatively correlated to the Delta(FR)V value, drives the separation of the ion pair after the electron transfer reaction in the case of highly organizing cations. The ratio X = T Delta(FR)S/Delta(FR)V = (55 +/- 9) kJ cm(-3) for Trp as 3FMN quencher is smaller than X = (83 +/- 9) kJ cm(-3) for Tyr as quencher. These values are discussed in conjunction with the Marcus reorganization energy, as calculated from the Gibbs activation energy of the electron transfer process, which is independent of the salt present but different for each of the two quenchers.