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J Am Chem Soc. 2010 Dec 8;132(48):17080-3. doi: 10.1021/ja1077574. Epub 2010 Nov 15.

Crystal structures of urate bound form of xanthine oxidoreductase: substrate orientation and structure of the key reaction intermediate.

Author information

1
Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyou-ku, Tokyo 113-8602, Japan.

Abstract

Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 Å and of the reduced bovine milk enzyme at 2.1 Å, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine.

PMID:
21077683
DOI:
10.1021/ja1077574
[Indexed for MEDLINE]

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