Analysis of Classical and Quantum Paths for Deprotonation of Methylamine by Methylamine Dehydrogenase-Reference-Cited by-同舟云学术

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Analysis of Classical and Quantum Paths for Deprotonation of Methylamine by Methylamine Dehydrogenase

Published:2007-08-24 Issue:12 Volume:8 Page:1816-1835
ISSN:1439-4235
Container-title:ChemPhysChem
language:en
Short-container-title:ChemPhysChem

Author:

Ranaghan Kara E.,Masgrau Laura,Scrutton Nigel S.,Sutcliffe Michael J.,Mulholland Adrian J.

Publisher

Wiley

Subject

Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics

Reference96 articles.

1. Evidence that both protium and deuterium undergo significant tunneling in the reaction catalyzed by bovine serum amine oxidase

2. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase

3. Deuterium Isotope Effects during Carbon–Hydrogen Bond Cleavage by Trimethylamine Dehydrogenase

4. Importance of Barrier Shape in Enzyme-catalyzed Reactions

5. H-tunneling in the Multiple H-transfers of the Catalytic Cycle of Morphinone Reductase and in the Reductive Half-reaction of the Homologous Pentaerythritol Tetranitrate Reductase

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