Kinetic and docking studies of the interaction of quinones with the quinone reductase active site.
Publication/Presentation Date
2-25-2003
Abstract
NAD(P)H/quinone acceptor oxidoreductase type 1 (QR1) protects cells from cytotoxic and neoplastic effects of quinones though two-electron reduction. Kinetic experiments, docking, and binding affinity calculations were performed on a series of structurally varied quinone substrates. A good correlation between calculated and measured binding affinities from kinetic determinations was obtained. The experimental and theoretical studies independently support a model in which quinones (with one to three fused aromatic rings) bind in the QR1 active site utilizing a pi-stacking interaction with the isoalloxazine ring of the FAD cofactor.
Volume
42
Issue
7
First Page
1985
Last Page
1994
ISSN
0006-2960
Published In/Presented At
Zhou, Z., Fisher, D., Spidel, J., Greenfield, J., Patson, B., Fazal, A., Wigal, C., Moe, O. A., & Madura, J. D. (2003). Kinetic and docking studies of the interaction of quinones with the quinone reductase active site. Biochemistry, 42(7), 1985–1994. https://doi.org/10.1021/bi026518s
Disciplines
Medicine and Health Sciences
PubMedID
12590585
Department(s)
Department of Medicine
Document Type
Article