Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.

Article

Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.

The Journal of biological chemistry - 5 Apr 1990

Di Primo C, Hui Bon Hoa G, Douzou P, Sligar S

Abstract excerpt

Cytochrome P-450cam, a monoxygenase responsible for the regiospecific hydroxylation of camphor, binds its substrate through complimentary van der Waals contacts and the formation of a single hydrogen bond between tyrosine 96 and the ketone group of camphor. Substrate association is positively reg...

Topics

Camphor
Camphor 5-Monooxygenase
Cations, Monovalent
Chemical Phenomena
Chemistry, Physical
Cytochrome P-450 Enzyme System
Heme
Hydrogen Bonding
Mixed Function Oxygenases
Mutation
Thermodynamics
Tyrosine

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