@inbook{741ceca456e54d12bd5404ef9772ae35,
title = "Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin",
abstract = "Heme iron in the ferrous state is one of nature{\textquoteright}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.",
keywords = "Hydration Shell, Pyridine Nucleotide, Heme Protein, Activation Enthalpy, Heme Iron",
author = "Gunsalus, {I. C.} and Sligar, {S. G.} and T. Nordlund and H. Frauenfelder",
year = "1977",
doi = "10.1007/978-1-4615-9035-4_3",
language = "English (US)",
isbn = "9781461590378",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer",
pages = "37--50",
editor = "Martin Reivich and Ronald Coburn and Sukhamay Lahiri and Britton Chance",
booktitle = "Tissue Hypoxia and Ischemia",
address = "Germany",
}