Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450☆
References (48)
- et al.
J. Biol. Chem
(1968) - et al.
- et al.
J. Biol. Chem
(1969) - et al.
J. Biol. Chem
(1970) - et al.
J. Biol. Chem
(1974) - et al.
Biochem. Biophys. Res. Commun
(1974) - et al.
J. Biol. Chem
(1975) - et al.
FEBS Lett
(1974) - et al.
J. Biol. Chem
(1975) - et al.
Biochem. Biophys. Res. Commun
(1971)
Chem. Biol. Interact
Biochem. Biophys. Res. Commun
J. Biol. Chem
Biochim. Biophys. Acta
Biochim. Biophys. Acta
Biochem. Biophys. Res. Commun
Biochem. Biophys. Res. Commun
Biochem. Biophys. Res. Commun
FEBS Lett
Biochem. Biophys. Res. Commun
FEBS Lett
Biochem. Biophys. Res. Commun
Biochem. Biophys. Res. Commun
J. Biol. Chem
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The relationships between cytochromes P450 and H <inf>2</inf> O <inf>2</inf> : Production, reaction, and inhibition
2018, Journal of Inorganic BiochemistryCitation Excerpt :More in vivo studies will be needed to determine the contribution of P450s to proposed ROS-related toxicities [72]. Reactions with H2O2 as the oxygen donor for P450 peroxygenase and peroxidase reactions are known [93,94]. In these reactions, the ferric heme reacts directly with an oxygen of H2O2 or other hydroperoxide species and proceeds with heterolytic cleavage of the oxygen‑oxygen bond to form Compound I [95].
Sulfenylation of human liver and kidney microsomal cytochromes P450 and other drug-metabolizing enzymes as a response to redox alteration
2018, Molecular and Cellular ProteomicsCitation Excerpt :What is most relevant is the change in the amount of P450 seen between the reductase- and dithionite -reduced spectra (Fig. 2). It has been known that some P450s can catalyze reactions with the use of H2O2 alone for quite some time (43–46). Also, mutating residues around the proximal heme ligand allows for alterations in both the heme redox potential and reactivity (47).
Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway
2017, Journal of Biological ChemistryTearing down to build up: Metalloenzymes in the biosynthesis lincomycin, hormaomycin and the pyrrolo [1,4]benzodiazepines
2016, Biochimica et Biophysica Acta - Proteins and ProteomicsThin Iron Heme Enzyme Films on Electrodes and Nanoparticles for Biocatalysis
2013, New and Future Developments in Catalysis: Catalysis by NanoparticlesThe monooxygenase, peroxidase, and peroxygenase properties of cytochrome P450
2012, Archives of Biochemistry and BiophysicsCitation Excerpt :Three major mechanisms have been proposed for the hydroxylation of unactivated C–H bonds in P450 substrates: (1) a radical stepwise nonconcerted mechanism, known as hydrogen abstraction/oxygen rebound involving Cpd I or its ferryloxy radical resonance form [55,60,84,90]; (2) a non-radical concerted mechanism, based on the use of ultrafast substrate probes, involving insertion of a hydroxonium cation (OH+) from the ferrihydroperoxo species into the C–H bond of the substrate [233,238–242]; and (3) a two-state reactivity mechanism involving high spin and low spin states of Cpd I [63,168,193,194]. Early views of the hydroxylation mechanism focused on an oxygen atom insertion pathway promoted by an electrophilic P450 porphyrin ferryloxo species equivalent to Cpd I of peroxidase enzymes [21,128,154]. This mechanism was refined and supplanted by the hydrogen abstraction/oxygen rebound pathway, whereby highly reactive Cpd I (or its ferryloxy radical resonance form) abstracts a H atom from a carbon of the alkane substrate to generate a carbon radical, which can instantly recombine with the ferryl-bound hydroxyl radical by rebound to produce an unrearranged (U) alcohol product, or can undergo skeletal rearrangement and then rebound to give a rearranged (R) alcohol product [55,84,193].
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This research was supported by Grant BMS71-01195 from the National Science Foundation and Grant AM-10339 from the United States Public Health Service. Preliminary reports of part of this investigation have been presented (1, 2).
- 2
Postdoctoral Fellow, United States Public Health Service.