On the indirect relationship between protein dynamics and enzyme activity.
The behaviors of simple thermal systems have been well studied in physical chemistry and the principles obtained from such studies have been applied to complex thermal systems, such as proteins and enzymes. But the simple application of such principles is questionable and may lead to mistakes under some circumstances. In enzymology, the transition state theory of chemical reactions has been accepted as a fundamental theory, but the role of protein dynamics in enzyme catalysis is controversial in the context of transition state theory. By studying behaviors of complex thermal systems, we have revised the Arrhenius equation and transition state theory and our model is validated in enzymology. Formally speaking, the revised Arrhenius equation is apparently similar to a conventional Arrhenius equation, but the physical meanings of its parameters differ from that of traditional forms in principle. Within this model, the role of protein dynamics in enzyme catalysis is well defined and quantified.
Medical Institute, CRRC, Beijing PR China. Electronic address: qinyizhao@gmail.com.
Qinyi
Q
Zhao
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D004798:Enzymes; D011506:Proteins; D000426:Alcohol Dehydrogenase
Conformation; Enzyme; Motion; Protein dynamics; Thermodynamics