CO binding studies of engineered cytochrome P-450ds: effects of mutations at putative distal sites in the presence of polycyclic hydrocarbons.

doi:10.1021/bi00233a004

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Article

CO binding studies of engineered cytochrome P-450ds: effects of mutations at putative distal sites in the presence of polycyclic hydrocarbons.

Biochemistry - 14 May 1991

Shimizu T, Ito O, Hatano M, Fujii-Kuriyama Y

Abstract excerpt

The kinetic parameters of CO binding to genetically engineered cytochrome P-450d (P-450d) and two putative distal mutants, Glu318Asp and Thr322Ala, have been evaluated in the presence and absence of polycyclic hydrocarbons. The dissociation constant (Kd) of CO from wild-type P-450d was decreased...

Topics

Animals
Carbon Monoxide
Cytochrome P-450 Enzyme System
Horses
Kinetics
Mutation
Myoglobin
Photochemistry
Polycyclic Compounds
Spectrum Analysis
Structure-Activity Relationship

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