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Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B12-Dependent Ethanolamine Ammonia Lyase


  • We thank the UK Biotechnology and Biological Sciences Research Council (BBSRC) for funding. S.H. is a BBSRC David Phillips Fellow and A.R.J. is Colt Foundation Postdoctoral Research Fellow. N.S.S. is a Royal Society Wolfson Merit Award holder and holds an Engineering and Physical Sciences Research Council (EPSRC) Established Career Fellowship. The time-resolved infrared measurements were carried out through program access support of the Science and Technology Facilities Council (STFC).


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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 B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture).

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