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

Biochemistry (2003-02-20)
Zhigang Zhou, Derek Fisher, Jared Spidel, Jodi Greenfield, Brian Patson, Aleem Fazal, Carl Wigal, Owen A Moe, Jeffry D Madura
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Duroquinone, 97%
Supelco
Duroquinone, Standard for quantitative NMR, TraceCERT®