Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin

I. C. Gunsalus, S. G. Sligar, T. Nordlund, H. Frauenfelder

Research output: Chapter in Book/Report/Conference proceedingChapter

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.
Original languageEnglish (US)
Title of host publicationTissue Hypoxia and Ischemia
EditorsMartin Reivich, Ronald Coburn, Sukhamay Lahiri, Britton Chance
Place of PublicationBoston
PublisherSpringer
Pages37-50
Number of pages14
ISBN (Electronic)9781461590354
ISBN (Print)9781461590378
StatePublished - 1977
Externally publishedYes

Publication series

NameAdvances in Experimental Medicine and Biology
PublisherSpringer
Volume78
ISSN (Print)0065-2598

Keywords

  • Hydration Shell
  • Pyridine Nucleotide
  • Heme Protein
  • Activation Enthalpy
  • Heme Iron

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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