Nanosecond fluorometry of the single tryptophan in cytochrome P-450e (P450IIB2).
Properties of the single tryptophan residue in rat liver microsomal phenobarbital-inducible cytochrome P-450e (P450IIB2) were studied by the nanosecond time-resolved fluorometry. The tryptophan fluorescence decay time was found to be 3.6 ns and it was not affected by the addition of substrate (perhydrophenanthrene). This result strongly indicates that the tryptophan residue is not a part of the substrate-binding site.
Department of Biochemistry, Charles University, Prague, Czechoslovakia.
P
P
Anzenbacher
J
J
Hudecek
S
S
Vajda
V
V
Fidler
D000818:Animals; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism* / Q000648:ultrastructure; D004790:Enzyme Induction / Q000187:drug effects; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology; D010634:Phenobarbital / Q000494:pharmacology; D011487:Protein Conformation; D051381:Rats; D012997:Solvents; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D014364:Tryptophan
D012997:Solvents; D014364:Tryptophan; D003577:Cytochrome P-450 Enzyme System; D010634:Phenobarbital