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Biochemistry. 2003 Feb 25;42(7):1985-94.

Kinetic and docking studies of the interaction of quinones with the quinone reductase active site.

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Department of Chemistry, Lebanon Valley College, Annville, Pennsylvania 17003, USA.


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.

[Indexed for MEDLINE]

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