Quantum chemical modelling of the oxidation of myoglobin

Bibliographic description

title:	Quantum chemical modelling of the oxidation of myoglobin
author:	Ilkowska E., Witko M., Tokarz-Sobieraj R., Stochel Grażyna
Journal title:	Polish Journal of Chemistry
volume:	78
issue:	10
date of publication:	2004
pages:	1907-1924
ISSN:	0137-5083
language:	English
Journal language:	English
abstract in english:	The electronic structure (charge distribution, bond indices) and the geometry (bond distances and angles) of the deoxyheme and the oxyheme with coordinated proximal histidine in their reduced and oxidized form were determined by the INDO method. The effect of the distal histidine (in the case of the oxyheme) and a water molecule (in the case of the metheme) on the geometry, charge distribution and stability of the systems was investigated. The method was adopted to model the oxidation of myoglobin in biological systems. The results revealed that both deoxy- and oxymyoglobin could spontaneously undergo one-electron oxidation. The mechanistic considerations based on the charge distribution and energetic effects led to the conclusion, that in oxymyoglobin’s case the electron transfer are followed by dissociation of a dioxygen molecule and addition of a water molecule, where both processes proceed in parallel.
affiliation:	Wydział Chemii : Zakład Chemii Nieorganicznej
type:	journal article
subtype:	academic paper