✦ LIBER ✦

Oxidation of sparteines by cytochrome P-450: evidence against the formation of N-oxides

✍ Scribed by Guengerich, F. Peter

Book ID: 126068422
Publisher: American Chemical Society
Year: 1984
Tongue: English
Weight: 418 KB
Volume: 27
Category: Article
ISSN: 0022-2623
DOI: 10.1021/jm00375a002

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Oxidation of substituted N,N-dimethylani

Oxidation of substituted N,N-dimethylanilines by cytochrome P-450: estimation of the effective oxidation-reduction potential of cytochrome P-450

✍ Macdonald, Timothy L.; Gutheim, William G.; Martin, R. Bruce; Guengerich, F. Pet 📂 Article 📅 1989 🏛 American Chemical Society 🌐 English ⚖ 935 KB

Formation of nitric oxide by cytochrome

Formation of nitric oxide by cytochrome P450-catalyzed oxidation of aromatic amidoximes

✍ V. Andronik-Lion; J.L. Boucher; M. Delaforge; Y. Henry; D. Mansuy 📂 Article 📅 1992 🏛 Elsevier Science 🌐 English ⚖ 438 KB

Evidence for altered catalytic propertie

Evidence for altered catalytic properties of the cytochrome P-450 involved in sparteine oxidation in poor metabolizers

✍ Osikowska-Evers, B; Dayer, P; Meyer, U A; Robertz, G M; Eichelbaum, M 📂 Article 📅 1987 🏛 Nature Publishing Group 🌐 English ⚖ 332 KB

Cytochrome P-450-dependent nicotine oxid

Cytochrome P-450-dependent nicotine oxidation by liver microsomes of guinea pigs: Immunochemical evidence with antibody against phenobarbital-inducible cytochrome P-450

✍ Hitoshi Nakayama; Toshikatsu Nakashima; Yutaka Kurogochi 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 733 KB

Evidence for the involvement of cytochro

Evidence for the involvement of cytochrome P-450 in tiaramide N-oxide reduction

✍ Masahiko Sugiura; Kazuhide Iwasaki; Hideyo Noguchi; Ryuichi Kato 📂 Article 📅 1974 🏛 Elsevier Science 🌐 English ⚖ 340 KB

Multiplicity of n-heptane oxidation path

Multiplicity of n-heptane oxidation pathways catalyzed by cytochrome P450

✍ Mirosław M. Szutowski; Joseph S. Rakoto 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 155 KB

## Abstract Modeling, mutagenesis, and kinetic studies have demonstrated that the substrate‐binding site of cytochrome P450 is composed of multiple interactive regions that are capable of simultaneously binding two or more xenobiotics. Substrate molecules can interact with each other after docking.