Abstract
The oxygen binding hemoproteins hemoglobin (Hb), myoglobin (Mb), and cytochrome P-450 are important to the biological transport, storage, and metabolism of oxygen. Nevertheless the nature of the coordinate link between iron and dioxygen in these hemoproteins has not been defined at the atomic level. Furthermore the way in which the glogin proteinheme interaction directs reversible oxygen binding has been obscure. My students have addressed and partially clarified these issues by preparing crystalline iron(II) porphyrin-dioxygen complexes.1–5 These remarkable Mb models which reversibly bind oxygen in solution or in the solid state at ambient temperature have been characterized by Mossbauer1,5, ir spectra4 and X-ray crystallographic analysis.2
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© 1975 Plenum Press, New York
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Collman, J.P., Gagnè, R.R., Reed, C.A. (1975). Synthetic Models for the Oxygen-Binding Hemoproteins. In: Ishii, Y., Tsutsui, M. (eds) Organotransition-Metal Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2142-2_31
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DOI: https://doi.org/10.1007/978-1-4684-2142-2_31
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