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Nitrogen-15 NMR in Biological Systems

  • Chapter
Biological Magnetic Resonance

Abstract

Nitrogen is found in almost every biological system. Active centers of enzymes contain nitrogen in the charged amino acid side chains; in coenzymes and nucleic acids nitrogen forms the essential functional part of the molecule. In particular histidine, arginine, and lysine are important in many enzymes. The histidine in the catalytic triad of serine proteases acts as the proton transferring group. The imidazole side chain is vital in nucleases such as ribonuclease T1 and ribonuclease A. In other enzymes the gua-nidinium group of arginine is of interest. A protonated lysine often acts as part of an ion pair stabilizing the catalytically active conformation of an enzyme. The activity of many enzymes is controlled by this kind of pH-dependent interaction. Nitrogen is also very important in the field of nucleic acids. The complex interactions of nucleic acids with each other or with proteins and sugars are dominated by nitrogen-nitrogen or nitrogen-oxygen interactions by way of hydrogen bonds, the best-known of these being the Watson-Crick H-bonds needed for the transfer of the genetic information. The special electronic properties of nitrogen are of importance in many coenzymes. Nitrogen heterocycles occur in redox coenzymes as an electron trap as well as an electron donor in the redox process.

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Authors and Affiliations

  1. Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Frankfurt am Main, German Federal Republic

    Felix Blomberg & Heinz Rüterjans

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  1. Felix Blomberg
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  2. Heinz Rüterjans
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  1. Ohio State University, Columbus, Ohio, USA

    Lawrence J. Berliner

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

    Jacques Reuben

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Blomberg, F., Rüterjans, H. (1983). Nitrogen-15 NMR in Biological Systems. In: Berliner, L.J., Reuben, J. (eds) Biological Magnetic Resonance. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6543-7_2

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