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Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin

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Tissue Hypoxia and Ischemia

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 78))

Abstract

Heme iron in the ferrous state is one of nature’s best di-oxygen sensors.1 A wide variety of protein structural environments incorporate heme and permit either oxygen binding, single electron redox processes, or both. The oxygen transport proteins myoglobin (Mb) and hemoglobin (Hb), for example, alternately bind and release oxygen. The P450 oxygenase2,3 heme proteins and cytochrome c oxidase, also bind oxygen in their biological role and, in addition, shuttle heme in a ferric-ferrous reduction and. reoxidation cycle. The cytochromes, in contrast, do not accept small molecules as a heme axial ligand as both available positions are occupied by amino acid residues from the primary protein structure. The sole function of these proteins is electron transfer by univalent ferric-ferrous redox processes, which are often coupled with energy storage for cellular work. A unique additional property of monoxygenase proteins (as well as the deoxygenases which will not be discussed in this paper) is the sensing of carbon substrates in addition to oxygen.

Supported in part by Grants from the National Institutes of Health AM 00562, GM 21161, GM 18051, and the National Science Foundation BMS 74-01366.

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Gunsalus, I.C., Sligar, S.G., Nordlund, T., Frauenfelder, H. (1977). Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin. In: Reivich, M., Coburn, R., Lahiri, S., Chance, B. (eds) Tissue Hypoxia and Ischemia. Advances in Experimental Medicine and Biology, vol 78. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9035-4_3

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  • DOI: https://doi.org/10.1007/978-1-4615-9035-4_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9037-8

  • Online ISBN: 978-1-4615-9035-4

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