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Multiple Irradiation 1H NMR Experiments with Hemoproteins

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Biological Magnetic Resonance

Abstract

Hemoproteins are conjugated proteins which consist of one or several polypeptide chains and one or several heme groups. The heme groups are iron porphyrin complexes (Figure 1) which can be combined with the polypeptide chains through one or several covalent or coordinative bonds and through a multitude of weaker interactions. The presence of the heme groups and their interactions with the surrounding polypeptide moiety confer a variety of physicochemical properties to hemoproteins which are not found in other proteins. As a consequence a wide range of physical techniques were applied to hemoproteins, and several hemoproteins are among the most thoroughly studied biological macromolecules. High resolution NMR is one of the prominent methods for studies of structure function relations in hemoproteins. The NMR spectral properties are markedly influenced by the heme groups, which act as natural shift and relaxation probes (Wuthrich, 1970, 1976).

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Authors and Affiliations

  1. Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, 8093, Zürich-Hönggerberg, Switzerland

    Regula M. Keller & Kurt Wüthrich

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  1. Regula M. Keller
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Editors and Affiliations

  1. Ohio State University, Columbus, Ohio, USA

    Lawrence J. Berliner

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

    Jacques Reuben

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Keller, R.M., Wüthrich, K. (1981). Multiple Irradiation 1H NMR Experiments with Hemoproteins. In: Berliner, L.J., Reuben, J. (eds) Biological Magnetic Resonance. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3201-5_1

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  • DOI: https://doi.org/10.1007/978-1-4613-3201-5_1

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