Allosteric Mechanisms in Cytochrome P450 3A4 Studied by High-Pressure Spectroscopy: Pivotal Role of Substrate-Induced Changes in the Accessibility and Degree of Hydration of the Heme Pocket

Lignende værker

• Allosteric transitions in cytochrome P450eryF explored with pressure-perturbation spectroscopy, lifetime FRET, and a novel fluorescent substrate, Fluorol-7GA
  af: Davydov, Dmitri R., et al.
  Udgivet: (2008)
• Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein
  af: Fernando, Harshica, et al.
  Udgivet: (2007)
• Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization.
  af: Davydov, Dmitri R., et al.
  Udgivet: (2005)
• Resolution of multiple substrate binding sites in cytochrome P450 3A4: the stoichiometry of the enzyme-substrate complexes probed by FRET and Job’s titration
  af: Fernando, Harshica, et al.
  Udgivet: (2006)
• Allosteric P450 mechanisms: multiple binding sites, multiple conformers, or both?
  af: Davydov, Dmitri R., et al.
  Udgivet: (2008)