Abstract
Summary The NADPH-supported metabolism of chlorobenzene has been studied with a reconstituted hydroxylation system from rat liver microsomes. The maximal rate of metabolism required the presence of cytochrome P-450, NADPH-cytochrome c reductase, lipid, and cytochrome b 5 . In contrast, cytochrome b 5 was not required for the NADPH-supported cytochrome P-448-dependent hydroxylation of chlorobenzene. Thus, it appears that a conclusion as to whether cytochrome b 5 is or is not involved in NADPH-supported microsomal hydroxylation reactions is dependent not only on the specific reaction studied, but also on the particular hemeprotein catalyzing the reaction.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
