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Quantum chemical modelling of the oxidation of myoglobin

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Quantum chemical modelling of the oxidation of myoglobin

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dc.contributor.author Ilkowska, E. pl
dc.contributor.author Witko, M. pl
dc.contributor.author Tokarz-Sobieraj, R. pl
dc.contributor.author Stochel, Grażyna [SAP11011061] pl
dc.date.accessioned 2014-12-20T10:54:37Z
dc.date.available 2014-12-20T10:54:37Z
dc.date.issued 2004 pl
dc.identifier.issn 0137-5083 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/2385
dc.language eng pl
dc.title Quantum chemical modelling of the oxidation of myoglobin pl
dc.type JournalArticle pl
dc.description.physical 1907-1924 pl
dc.abstract.en 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. pl
dc.description.volume 78 pl
dc.description.number 10 pl
dc.title.journal Polish Journal of Chemistry pl
dc.language.container eng pl
dc.affiliation Wydział Chemii : Zakład Chemii Nieorganicznej pl
dc.subtype Article pl


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