7,8-benzoflavone binding to human cytochrome P450 3A4 reveals complex fluorescence quenching, suggesting binding at multiple protein sites-Reference-Cited by-同舟云学术

7,8-benzoflavone binding to human cytochrome P450 3A4 reveals complex fluorescence quenching, suggesting binding at multiple protein sites

Published:2017-03-20 Issue:4 Volume:36 Page:841-860
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Marsch Glenn A.¹,Carlson Benjamin T.¹,Guengerich F. Peter²

Affiliation:

1. Physics Department, Grove City College, Grove City, PA, 16127-2104, USA

2. Department of Biochemistry, Vanderbilt University School of Medicine, 638B Robinson Research Building, 2200 Pierce Avenue, Nashville, TN, 37232-0146, USA

Funder

National Institutes of Health

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2017.1301270

Reference64 articles.

1. Implications of the allosteric kinetics of cytochrome P450s

2. Tryptophan Fluorescence Shifts in Proteins from Hybrid Simulations: An Electrostatic Approach

3. Quantitative Prediction of Fluorescence Quantum Yields for Tryptophan in Proteins

4. Cantor, C. R. & Schimmel, P. R. (1980). Fluorescence spectroscopy, in Biophysical Chemistry. Part II: Techniques for the Study of Biological Structure and Function (1st ed., pp. 433–455). New York, NY: W. H. Freeman.

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