Article
Stabilization and spectroscopic characterization of the dioxygen complex of wild-type cytochrome P4502B4 (CYP2B4) and its distal side E301Q, T302A and proximal side F429H mutants at subzero temperatures.
Biochimica et biophysica acta - 1 Jan 2011
Perera Roshan, Sono Masanori, Kinloch Ryan, Zhang Haoming, Tarasev Michael, Im Sang-Choul, Waskell Lucy, Dawson John H
Abstract excerpt
Mammalian cytochrome P450 2B4 (CYP2B4) is a phenobarbital-inducible rabbit hepatic monooxygenase that catalyzes the N-demethylation of benzphetamine and metabolism of numerous other compounds. To probe the interactions of the heme environment and bound benzphetamine with the dioxygen (O₂) complex of CYP2B4, homogeneous O₂ complexes of the wild-type enzyme and three mutants at sites of conserved amino acids, two...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.