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NMR Crystallography as a Novel Tool for the Understanding of the Mode of Action of Enzymes: SOD a Case Study

Tietze, D. and Voigt, S. and 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.
In: Applied Magnetic Resonance, pp. 841-857, 45, (9), [Online-Edition: http://apps.webofknowledge.com/full_record.do?product=WOS&se...],
[Article]

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 The review is completed by new, previously unpublished results, calculating an NMR structure of NiSOD model peptide-bound cyanide based on experimental restraints measured by us and derived from the literature and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.

Item Type: Article
Erschienen: 2014
Creators: Tietze, D. and Voigt, S. and Mollenhauer, D. and Buntkowsky, G.
Title: NMR Crystallography as a Novel Tool for the Understanding of the Mode of Action of Enzymes: SOD a Case Study
Language: English
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.

Journal or Publication Title: Applied Magnetic Resonance
Volume: 45
Number: 9
Uncontrolled Keywords: manganese superoxide-dismutase solid-state nmr double-resonance nmr gaussian-basis sets x-ray-structure chemical-shift propionibacterium-shermanii mechanistic implications dipolar interactions crystal-structure
Divisions: 07 Department of Chemistry
07 Department of Chemistry > Physical Chemistry
Date Deposited: 27 Oct 2014 20:51
Official URL: http://apps.webofknowledge.com/full_record.do?product=WOS&se...
Additional Information:

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