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Metal ion dependent adhesion sites in integrins: A Combined DFT and QMC Study on Mn2+
Örebro University, Department of Natural Sciences. (Biophysical Chemistry)
Örebro University, Department of Natural Sciences. (Biophysical Chemistry)
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2007 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 111, no 30, p. 9099-9103Article in journal (Refereed) Published
Abstract [en]

The theoretical study of relative energies of different spin states of Mn2+ has been carried out for the isolated cation and for structures in which the cation is coordinated to ligands that represent the first coordination shell in a protein environment that contains a metal ion dependent adhesion site (MIDAS, found in the ligand binding domain of protein LFA-1). The calculations determine whether the ligand field generated by a prototype protein environment affects the relative energies between high, intermediate, and low spin states. Geometry optimizations and vibrational frequency calculations were carried out at the B3LYP/SKBJ+* level of theory. Single point calculations were performed at the B3LYP/6-311++G(2df,2p) and diffusion monte carlo (DMC) levels for the refinement of the electronic energies. These calculations reveal important differences in the relative energies between high/low spin complexes obtained by B3LYP and DMC and show that although both DFT and DMC show similar trends, a higher level method such as DMC is necessary for a quantitative description of the interactions between Mn2+ and its natural ligands. (G)s of acetate-type ligand binding reactions were calculated that show that the higher the spin of the manganese complex, the lower the affinity for the ligand.

Place, publisher, year, edition, pages
Washington, DC: American Chemical Society , 2007. Vol. 111, no 30, p. 9099-9103
Keywords [en]
Binding Sites, Integrins, Ligands, Manganese, Metalloproteins, Protein Binding, Quantum Theory, Thermodynamics
National Category
Theoretical Chemistry Natural Sciences Chemical Sciences
Research subject
Chemistry
Identifiers
URN: urn:nbn:se:oru:diva-4108DOI: 10.1021/jp071065sPubMedID: 17608410OAI: oai:DiVA.org:oru-4108DiVA, id: diva2:138407
Available from: 2007-12-17 Created: 2007-12-17 Last updated: 2017-12-14Bibliographically approved

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Matxain, Jon M.Eriksson, Leif A.

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