Identification of an active site-bound nitrile hydratase intermediate through single turnover stopped-flow spectroscopy.
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The Active Site Sulfenic Acid Ligand in Nitrile Hydratases Can Function as a NucleophileAnalyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1Time-Resolved Crystallography of the Reaction Intermediate of Nitrile Hydratase: Revealing a Role for the Cysteinesulfenic Acid Ligand as a Catalytic NucleophileSpectroscopic and Computational Studies of Nitrile Hydratase: Insights into Geometric and Electronic Structure and the Mechanism of Amide Synthesis.Nitrile-converting enzymes as a tool to improve biocatalysis in organic synthesis: recent insights and promises.Multiple States of Nitrile Hydratase from Rhodococcus equi TG328-2: Structural and Mechanistic Insights from Electron Paramagnetic Resonance and Density Functional Theory Studies.
P2860
Identification of an active site-bound nitrile hydratase intermediate through single turnover stopped-flow spectroscopy.
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name
Identification of an active si ...... ver stopped-flow spectroscopy.
@en
type
label
Identification of an active si ...... ver stopped-flow spectroscopy.
@en
prefLabel
Identification of an active si ...... ver stopped-flow spectroscopy.
@en
P2093
P2860
P356
P1476
Identification of an active si ...... ver stopped-flow spectroscopy.
@en
P2093
Misty L Kuhn
Natalia Hajnas
Natalie Gumataotao
Richard C Holz
P2860
P304
15532-15536
P356
10.1074/JBC.M112.398909
P407
P577
2013-04-15T00:00:00Z