Studies on the stimulation of cytochrome P-450-dependent monooxygenase activity by dilauroylphosphatidylcholine☆
References (26)
- et al.
J. Biol. Chem
(1968) - et al.
J. Biol. Chem
(1970) - et al.
Biochim. Biophys. Acta
(1977) - et al.
Biochem. Biophys. Res. Commun
(1969) - et al.
Biochim. Biophys. Acta
(1979) - et al.
J. Biol. Chem
(1979) - et al.
J. Biol. Chem
(1979) - et al.
J. Biol. Chem
(1980) - et al.
Arch. Biochem. Biophys
(1979) - et al.
J. Biol. Chem
(1964)
J. Biol. Chem
Biochem. Biophys. Res. Commun
J. Biol. Chem
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Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy
2015, Journal of Biological ChemistryCitation Excerpt :This implies the ability of lipids to facilitate tighter binding between wt-CYP2B4 and cytb5. Our results are in agreement with the previous findings that phospholipids enhance the interactions between P450s and the other redox partner, CPR (27–30). In order to investigate the influence of different membrane mimetic environments on CYP2B4-cytb5 interaction, two-dimensional 15N/1H TROSY-HSQC NMR spectra were recorded to monitor the interaction between 15N-labeled cytb5 and unlabeled wt-CYP2B4 in lipid-free solution, DLPC/DHPC isotropic bicelles, and DPC micelles.
Two surfaces of cytochrome b<inf>5</inf> with major and minor contributions to CYP3A4-catalyzed steroid and nifedipine oxygenation chemistries
2014, Archives of Biochemistry and BiophysicsCitation Excerpt :The phospholipid composition markedly influences P450 turnover and b5 stimulation [30,31], and CYP3A family activities are highest when reconstituted with acidic phospholipids such as PS [22,32]. PS with unsaturated fatty acids improves interactions between the P450 and POR [32–34] and binds to CYP3Al, which alters its conformation [35]. In our assay system, CYP3A4-catalyzed testosterone 6β-hydroxylation decreases with phospholipids in the order PS > PE > PC.
Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners
2010, Biochimica et Biophysica Acta - Proteins and ProteomicsElectrochemical characterisation of the human cytochrome P450 CYP2C9
2005, Biochemical PharmacologyCitation Excerpt :Thus, without any other contributing factors like substrate or even oxygen, a lipid environment may be able to alter the electron transfer event from a thermodynamically unfavourable process (positive ΔG) to a favourable, spontaneous process (negative ΔG). This point is further emphasised by the fact that a lipid-like environment is required for catalytic activity [12,50–52] and numerous other structural and electronic properties [20–27] for many P450 enzymes. We have expressed and purified CYP2C9, and characterised the enzyme by direct electrochemistry.
Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b<inf>5</inf> enzymes
2005, Archives of Biochemistry and BiophysicsCitation Excerpt :Both proteins aggregate in solution [59], and the addition of non-ionic detergents to favor monomers will either alter the apparent binding parameters, due to facilitated interaction in vesicles, or disrupt interaction of the P450s with the other proteins [60,61]. Although P450 · NPR complexes have been discussed in the literature [56–66], estimates of dissociation constants are limited. French et al. [63] estimated Kd values for 0.04–0.12 μM for the P450 2B4 · NPR complex, depending upon conditions, utilizing spectral perturbation of the P450 heme by NPR.
Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid
1998, Archives of Biochemistry and Biophysics
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Preliminary results of this work were presented at the 4th International Symposium on Microsomes and Drug Oxidations held at Ann Arbor, Mich, in July 1979.