QUANTUMMECHANICALMETHODS FORENZYMEKINETICS

Article Properties
  • Language
    English
  • Publication Date
    2002/10/01
  • Indian UGC (Journal)
  • Refrences
    286
  • Citations
    538
  • Jiali Gao Department of Chemistry and Supercomputer Institute, University of Minnesota, 207 Pleasant Street S.E., Minneapolis, Minnesota 55455-0431;
  • Donald G. Truhlar Department of Chemistry and Supercomputer Institute, University of Minnesota, 207 Pleasant Street S.E., Minneapolis, Minnesota 55455-0431;
Abstract
Cite
Gao, Jiali, and Donald G. Truhlar. “QUANTUMMECHANICALMETHODS FORENZYMEKINETICS”. Annual Review of Physical Chemistry, vol. 53, no. 1, 2002, pp. 467-05, https://doi.org/10.1146/annurev.physchem.53.091301.150114.
Gao, J., & Truhlar, D. G. (2002). QUANTUMMECHANICALMETHODS FORENZYMEKINETICS. Annual Review of Physical Chemistry, 53(1), 467-505. https://doi.org/10.1146/annurev.physchem.53.091301.150114
Gao J, Truhlar DG. QUANTUMMECHANICALMETHODS FORENZYMEKINETICS. Annual Review of Physical Chemistry. 2002;53(1):467-505.
Journal Categories
Science
Chemistry
Science
Chemistry
Physical and theoretical chemistry
Description

Can quantum mechanics enhance our understanding of enzyme behavior? This review explores methods for incorporating quantum mechanical effects into enzyme kinetics simulations, where the enzyme is explicitly included in the model. The review focuses on three key aspects: the use of quantum mechanical electronic structure methods (molecular orbital theory and density functional theory), treating vibrational motions quantum mechanically (harmonic approximation, path integrals, or a three-dimensional wave function coupled to classical nuclear motion), and incorporating multidimensional tunneling approximations into reaction rate calculations. These approaches aim to provide a more accurate description of enzyme kinetics by accounting for quantum phenomena that classical simulations often neglect. This comprehensive review provides valuable insights into the use of quantum mechanical methods in enzyme kinetics, guiding future research in this field.

Refrences
Citations
Citations Analysis
The first research to cite this article was titled Kinetic Isotope Effects for Concerted Multiple Proton Transfer:  A Direct Dynamics Study of an Active-Site Model of Carbonic Anhydrase II and was published in 2002. The most recent citation comes from a 2024 study titled Kinetic Isotope Effects for Concerted Multiple Proton Transfer:  A Direct Dynamics Study of an Active-Site Model of Carbonic Anhydrase II . This article reached its peak citation in 2007 , with 44 citations.It has been cited in 140 different journals, 8% of which are open access. Among related journals, the Journal of Chemical Theory and Computation cited this research the most, with 57 citations. The chart below illustrates the annual citation trends for this article.
Citations used this article by year