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https://hdl.handle.net/2440/66043
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Type: | Journal article |
Title: | Nature of the catalytically labile oxygen at the active site of xanthine oxidase |
Author: | Doonan, C. Stockert, A. Hille, R. George, G. |
Citation: | Journal of the American Chemical Society, 2005; 127(12):4518-4522 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2005 |
ISSN: | 0002-7863 1520-5126 |
Statement of Responsibility: | Christian J. Doonan, Amy Stockert, Russ Hille, and Graham N. George |
Abstract: | In this paper we report the results of molybdenum K-edge X-ray absorption studies performed on the oxidized active site of xanthine oxidase at pH 6 and 10. These results indicate that the active site possesses one terminal oxygen ligand (Mo=O), two thiolate ligands (Mo-S), one terminal sulfido ligand (Mo=S), and one Mo-OH moiety. EXAFS analysis demonstrates that the Mo-OH bond shortens from 1.97 A at pH 6 to 1.75 A at pH 10, which is consistent with the generation of a Mo-O- moiety. This study provides convincing structural evidence that the catalytic oxygen donor at the oxidized active site of xanthine oxidase is Mo-OH rather than the Mo-OH2 ligation previously suggested by X-ray crystallography. These results support a mechanism initiated by base-assisted nucleophilic attack of the substrate by Mo-OH. |
Keywords: | Oxygen Molybdenum Xanthine Oxidase Spectrometry, X-Ray Emission Binding Sites Catalysis Hydrogen-Ion Concentration |
Rights: | Copyright © 2005 American Chemical Society |
DOI: | 10.1021/ja042500o |
Published version: | http://dx.doi.org/10.1021/ja042500o |
Appears in Collections: | Aurora harvest Chemistry publications Environment Institute publications |
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