Nanosecond fluorometry of the single tryptophan in cytochrome P-450e (P450IIB2)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. Cytochrome P-450,1985
2. Oxygen Activation by Cytochrome P-4501
3. TIME-RESOLVED FLUORESCENCE OF PROTEINS
4. THE PHOTOPHYSICS AND PHOTOCHEMISTRY OF THE NEAR-UV ABSORBING AMINO ACIDS-I. TRYPTOPHAN AND ITS SIMPLE DERIVATIVES
5. Nanosecond pulse fluorometry of conformational change in phenylalanine hydroxylase associated with activation
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1. Dynamic Ligation Properties of the Escherichia coli Heme Chaperone CcmE to Non-covalently Bound Heme;Journal of Biological Chemistry;2006-03
2. Steady-State and Picosecond-Time-Resolved Fluorenscence Studies on the Recombinant Heme Domain of Bacillus megaterium Cytochrome P-450;European Journal of Biochemistry;1997-03
3. Interaction of Tryptophan Residues of Cytochrome P450scc with a Highly Specific Fluorescence Quencher, a Substrate Analogue, Compared to Acrylamide and Iodide;European Journal of Biochemistry;1994-12
4. Cytochromes P450: Their Active-Site Structure and Mechanism of Oxidation;Drug Metabolism Reviews;1993-01
5. Nanosecond fluorescence of tryptophans in cytochrome P-450scc (CYP11A1): Effect of substrate binding;Biochemical and Biophysical Research Communications;1991-12
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