| Literature DB >> 24709164 |
Katarzyna Swiderek1, J Javier Ruiz-Pernía2, Vicent Moliner3, Iñaki Tuñón4.
Abstract
The role of protein motions in the chemical step of enzyme-catalyzed reactions is the subject of an open debate in the scientific literature. The systematic use of isotopically substituted enzymes has been revealed as a useful tool to quantify the role of these motions. According to the Born-Oppenheimer approximation, changing the mass of the protein does not change the forces acting on the system but alters the frequencies of the protein motions, which in turn can affect the rate constant. Experimental and theoretical studies carried out in this field are presented in this article and discussed in the framework of Transition State Theory.Mesh:
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Year: 2014 PMID: 24709164 DOI: 10.1016/j.cbpa.2014.03.005
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN: 1367-5931 Impact factor: 8.822