Article
Intramolecular heme ligation of the cytochrome P450 2C9 R108H mutant demonstrates pronounced conformational flexibility of the B-C loop region: implications for substrate binding.
Biochemistry - 12 Oct 2010
Roberts Arthur G, Cheesman Matthew J, Primak Andrew, Bowman Michael K, Atkins William M, Rettie Allan E
Abstract excerpt
A previous study [Dickmann, L., et al. (2004) Mol. Pharmacol. 65, 842-850] revealed some unusual properties of the R108H mutant of cytochrome P450 2C9 (CYP2C9), including elevated thermostability relative to that of CYP2C9, as well as a UV-visible absorbance spectrum that was indicative of nitrogenous ligation to the heme iron. In our study, size-exclusion chromatography and UV-visible absorbance spectroscopy of...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.