Quantum chemical modelling of the oxidation of myoglobin

2004
journal article
article
dc.abstract.enThe 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.affiliationWydział Chemii : Zakład Chemii Nieorganicznejpl
dc.contributor.authorIlkowska, E.pl
dc.contributor.authorWitko, M.pl
dc.contributor.authorTokarz-Sobieraj, R.pl
dc.contributor.authorStochel, Grażyna - 132108 pl
dc.date.accessioned2014-12-20T10:54:37Z
dc.date.available2014-12-20T10:54:37Z
dc.date.issued2004pl
dc.description.number10pl
dc.description.physical1907-1924pl
dc.description.volume78pl
dc.identifier.issn0137-5083pl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/2385
dc.languageengpl
dc.language.containerengpl
dc.rightsDodaję tylko opis bibliograficzny*
dc.rights.licenceBez licencji otwartego dostępu
dc.rights.uri*
dc.subtypeArticlepl
dc.titleQuantum chemical modelling of the oxidation of myoglobinpl
dc.title.journalPolish Journal of Chemistrypl
dc.typeJournalArticlepl
dspace.entity.typePublication
dc.abstract.enpl
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.
dc.affiliationpl
Wydział Chemii : Zakład Chemii Nieorganicznej
dc.contributor.authorpl
Ilkowska, E.
dc.contributor.authorpl
Witko, M.
dc.contributor.authorpl
Tokarz-Sobieraj, R.
dc.contributor.authorpl
Stochel, Grażyna - 132108
dc.date.accessioned
2014-12-20T10:54:37Z
dc.date.available
2014-12-20T10:54:37Z
dc.date.issuedpl
2004
dc.description.numberpl
10
dc.description.physicalpl
1907-1924
dc.description.volumepl
78
dc.identifier.issnpl
0137-5083
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/2385
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Dodaję tylko opis bibliograficzny
dc.rights.licence
Bez licencji otwartego dostępu
dc.rights.uri*
dc.subtypepl
Article
dc.titlepl
Quantum chemical modelling of the oxidation of myoglobin
dc.title.journalpl
Polish Journal of Chemistry
dc.typepl
JournalArticle
dspace.entity.type
Publication
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