A QM/MM study of the active species of the human cytochrome P450 3A4, and the influence thereof of the multiple substrate binding

Documenti analoghi

• Theoretical Characterization of Substrate Access/Exit Channels in the Human Cytochrome P450 3A4 Enzyme: Involvement of Phenylalanine Residues in the Gating Mechanism
  di: Fishelovitch, Dan, et al.
  Pubblicazione: (2009)
• How Does the Reductase Help To Regulate the Catalytic Cycle of Cytochrome P450 3A4 Using the Conserved Water Channel?
  di: Fishelovitch, Dan, et al.
  Pubblicazione: (2010)
• How Do Perfluorinated Alkanoic Acids Elicit Cytochrome P450 to Catalyze Methane Hydroxylation? An MD and QM/MM Study
  di: Li, Chunsen, et al.
  Pubblicazione: (2012)
• MD simulations and QM/MM calculations show that single-site mutations of cytochrome P450(BM3) alter the active site’s complexity and the chemoselectivity of oxidation without changing the active species
  di: Dubey, Kshatresh Dutta, et al.
  Pubblicazione: (2017)
• The Effect of Heme Environment on the Hydrogen Abstraction Reaction of Camphor in P450(cam) Catalysis: A QM/MM Study
  di: Altun, Ahmet, et al.
  Pubblicazione: (2006)