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Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B 12 ‐Dependent Ethanolamine Ammonia Lyase
Author(s) -
Russell Henry J.,
Jones Alex R.,
Hay Sam,
Greetham Gregory M.,
Towrie Michael,
Scrutton Nigel S.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201202502
Subject(s) - chemistry , cofactor , flash photolysis , ammonia , ethanolamine , substrate (aquarium) , lyase , infrared , protein dynamics , catalysis , stereochemistry , photochemistry , biochemistry , kinetics , protein structure , enzyme , biology , physics , optics , reaction rate constant , quantum mechanics , ecology
The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped‐flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B 12 ‐dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture).