A theoretical study of the conformational properties of a small heme peptide in aqueous solution is carried out by classical, long-timescale molecular dynamics simulations. The electronic properties of this species, that is, the relative energies of its excited electronic states and the redox potential, are reproduced and related to the conformational behavior using the perturbed matrix method and basic statistical mechanics. Our results show an interesting coupling between the conformational transitions and the electronic properties. These investigatons, beyond the biophysically relevant results addressing the long-stading question of the actual role of the enzyme structure on the enzyme activity, are also of some methodological interest since they offer a further computational perspective for incuding the electronic degrees of freedom into the modeling of rather complex molecular systems. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Conformational and electronic properties of a microperoxidase in aqueous solution: A computational study / Carla Di, Teodoro; Massimiliano, Aschi; Andrea, Amadei; Danilo, Roccatano; Malatesta, Francesco; Luca, Ottaviano. - In: CHEMPHYSCHEM. - ISSN 1439-4235. - 6:4(2005), pp. 681-689. [10.1002/cphc.200400493]