Quantum Chemical Modelling of the Oxidation of Myoglobin

• Autorzy: Ilkowska E. , Witko M. , Tokarz-Sobieraj R. , Stochel G.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

oxyheme; electronic structure; oxidation process; ZINDO method

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Polish Journal of Chemistry
• Rocznik: 2004
• Tom: Vol. 78 / nr 10
• Strony: 1907--1924
• Opis fizyczny: Bibliogr. 52 poz., rys.

Twórcy

autor

Ilkowska E.

• Faculty of Chemistry, Jagiellonian University, ul. Ingardena 3, 30-060 Cracow, Poland

autor

Witko M.

• Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, ul. Niezapominajek 8, 30-239 Cracow, Poland fax: [phone]

autor

Tokarz-Sobieraj R.

• Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, ul. Niezapominajek 8, 30-239 Cracow, Poland fax: [phone]

autor

Stochel G.

• Faculty of Chemistry, Jagiellonian University, ul. Ingardena 3, 30-060 Cracow, Poland

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