Abstract
Knowledge of the electronic distribution and bond angles of the Fe-CO and Fe-O2 moieties and the conformational state of the proximal ligand is fundamental to the understanding of reversible binding of diatomic molecules to hemoproteins and synthetic model compounds. CO and O2 differ significantly in their electronic structure and mode of binding. The FeCO unit prefers a linear geometry, in order to maximize Fe dπ→π back-bonding, while the FeO2 unit is strongly bent (Momenteau and Reed, 1994). The purpose of this article is to present a synopsis of our recent work in the field of hemoproteins and synthetic model compounds by the use of multinuclear NMR spectroscopy.
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© 1997 Springer Science+Business Media Dordrecht
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Gerothanassis, I.P., Kalodimos, C.G., Momenteau, M. (1997). Multinuclear NMR Studies of Hemoproteins and Synthetic Model Compounds in Solution and in the Solid State. In: Carmona, P., Navarro, R., Hernanz, A. (eds) Spectroscopy of Biological Molecules: Modern Trends. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5622-6_28
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DOI: https://doi.org/10.1007/978-94-011-5622-6_28
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