Heavy enzymes--experimental and computational insights in enzyme dynamics.
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.
Departamento de Química Física, Universitat de València, 46100 Burjassot, Spain; Institute of Applied Radiation Chemistry, Lodz University of Technology, 90-924 Lodz, Poland.
Katarzyna
K
Swiderek
Departamento de Química Física y Analítica, Universitat Jaume I, 12071 Castellón, Spain.
J Javier
JJ
Ruiz-Pernía
Departamento de Química Física y Analítica, Universitat Jaume I, 12071 Castellón, Spain. Electronic address: moliner@uji.es.
Vicent
V
Moliner
Departamento de Química Física, Universitat de València, 46100 Burjassot, Spain. Electronic address: tunon@uv.es.
Iñaki
I
Tuñón
D055162:Biocatalysis; D019295:Computational Biology / Q000379:methods*; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight
D004798:Enzymes