Dynamic Characteristics of Guanosine-5′-monophosphate Reductase Complexes Revealed by High-Resolution 31P Field-Cycling NMR Relaxometry

The ability of enzymes to modulate the dynamics of bound substrates and cofactors is a critical feature of catalysis, but the role of dynamics has largely been approached from the perspective of the protein. Here, we use an underappreciated NMR technique, subtesla high-resolution field-cycling 31P N...

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Veröffentlicht in:	Biochemistry (Easton) 2018-06, Vol.57 (22), p.3146-3154
Hauptverfasser:	Rosenberg, Masha M, Redfield, Alfred G, Roberts, Mary F, Hedstrom, Lizbeth
Format:	Artikel
Sprache:	eng
Schlagworte:	catalytic activity deamination deuterium oxide enzymes guanosine monophosphate hydrides inosine monophosphate mutation nuclear magnetic resonance spectroscopy phosphorus stable isotopes
Online-Zugang:	Volltext
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