Article
Structural alteration of mouse P450coh by mutation of glycine-207 to proline: spin equilibrium, enzyme kinetics, and heat sensitivity.
The Biochemical journal - 15 Aug 1993
Juvonen R O, Iwasaki M, Sueyoshi T, Negishi M
Abstract excerpt
Mouse cytochrome P450coh is a high-spin haem protein which specifically catalyses coumarin 7-hydroxylase activity. A mutation of Gly-207 to Pro shifts the P450coh completely to the low-spin form, indicating that the sixth axial position of the haem is hexaco-ordinated with a water molecule in the mutant G207P. Moreover, the G207P mutation increases the Km value for coumarin 7-hydroxylase activity 100-fold and the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
