Journal article

Authors list: Tietze, D; Voigt, S; Mollenhauer, D; Buntkowsky, G

Publication year: 2014

Pages: 841-857

Journal: Applied Magnetic Resonance

Volume number: 45

Issue number: 9

DOI Link: https://doi.org/10.1007/s00723-014-0576-9

Publisher: Springer

Abstract: 

Nuclear magnetic resonance (NMR) crystallography is an approach for
revealing molecular and supramolecular structures and molecular packing
for systems where standard X-ray crystallography gives no results. It
combines solid-state NMR techniques with chemical models and/or
molecular dynamics and/or quantum chemical calculations. These
techniques are often supported by other structure characterization
methods. In the present review, recent results on the application of NMR
crystallography for the investigation of the mode of action of
superoxide dismutases are discussed. Studies of substrate–inhibitor
complexes of human manganese and Streptomyces
nickel superoxide dismutase are presented, which are chemical models of
the transient enzyme–substrate complex. The review is completed by new,
previously unpublished results, calculating an NMR structure of NiSOD
model peptide-bound cyanide based on experimental restraints measured by
us and derived from the literature and extended DFT calculations.

Harvard Citation style: Tietze, D., Voigt, S., Mollenhauer, D. and Buntkowsky, G. (2014) NMR Crystallography as a Novel Tool for the Understanding of the Mode of Action of Enzymes: SOD a Case Study, Applied Magnetic Resonance, 45(9), pp. 841-857. https://doi.org/10.1007/s00723-014-0576-9

APA Citation style: Tietze, D., Voigt, S., Mollenhauer, D., & Buntkowsky, G. (2014). NMR Crystallography as a Novel Tool for the Understanding of the Mode of Action of Enzymes: SOD a Case Study. Applied Magnetic Resonance. 45(9), 841-857. https://doi.org/10.1007/s00723-014-0576-9