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Proton NMR Spectroscopy of Model Hemes

  • Chapter
NMR of Paramagnetic Molecules

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 12))

Abstract

Hemes and heme proteins are vital components of essentially every cell of every living organism. Their roles in cells include

  1. 1

    the transport of dioxygen in the red blood cells of higher animals (hemoglobin);

  2. 2

    the storage of dioxygen in the muscles of higher animals (myoglobin);

  3. 3

    the transport of electrons in the respiratory chains of organisms as diverse as bacteria, yeasts, algae, plants, and animals, and in photosynthetic cells from those of the simplest photosynthetic bacteria to those of higher plants (cytochromes a, b, c, d, f);

  4. 4

    synthesis, modification and degradation of fatty acids, steroid and adrenal hormones, anesthetics and xenobiotics (cytochromes P-450);

  5. 5

    activation and metabolism of hydrogen peroxide (peroxidases, myeloperoxidase, haloperoxidases, catalases, etc.); and

  6. 6

    metabolism of the oxides of nitrogen and sulfur (nitrite reductase, sulfite oxidase, etc.).

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Authors and Affiliations

  1. Department of Chemistry, University of Arizona, Tucson, Arizona, 85721, USA

    F. Ann Walker

  2. Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, California, 94132, USA

    Ursula Simonis

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  1. F. Ann Walker
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  2. Ursula Simonis
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Editors and Affiliations

  1. Ohio State University, Columbus, Ohio, USA

    Lawrence J. Berliner

  2. Research Center, Hercules Incorporated, Wilmington, Delaware, USA

    Jacques Reuben

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Walker, F.A., Simonis, U. (1993). Proton NMR Spectroscopy of Model Hemes. In: Berliner, L.J., Reuben, J. (eds) NMR of Paramagnetic Molecules. Biological Magnetic Resonance, vol 12. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2886-9_4

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  • DOI: https://doi.org/10.1007/978-1-4615-2886-9_4

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