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Electron spin-labelling of the EutC subunit in B12-dependent ethanolamine ammonia-lyase reveals dynamics and a two-state conformational equilibrium in the N-terminal, signal-sequence-associated domain.Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200-265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide.Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in B12-Dependent Ethanolamine Ammonia-Lyase Resolve Contributions of Native Protein Configurations and Collective Configurational Fluctuations to Catalysis.Sacrificial Cobalt-carbon Bond Homolysis in Coenzyme B12 as a Cofactor Conservation StrategyItaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repairDeuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B12-Dependent Ethanolamine Ammonia-LyaseControl of Solvent Dynamics around the B12-Dependent Ethanolamine Ammonia-Lyase Enzyme in Frozen Aqueous Solution by Using Dimethyl Sulfoxide Modulation of Mesodomain Volume
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description
researcher (ORCID 0000-0002-3587-3720)
@en
wetenschapper
@nl
name
Kurt Warncke
@en
Kurt Warncke
@nl
type
label
Kurt Warncke
@en
Kurt Warncke
@nl
prefLabel
Kurt Warncke
@en
Kurt Warncke
@nl
P31
P496
0000-0002-3587-3720