Copper x-ray absorption spectroscopic studies of the bovine plasma amine oxidase-sulfide complex
Substrate amines react with the organic cofactor of the bovine plasma amine oxidase and are oxidized to aldehydes. This reduces the enzyme by two electrons, and copper is required for the subsequent oxidation of the reduced enzyme by O/sub 2/ producing H/sub 2/O/sub 2/ and releasing NH/sub 3/. HS/su...
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Veröffentlicht in: | Inorg. Chem.; (United States) 1988-10, Vol.27 (21), p.3859-3861 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Substrate amines react with the organic cofactor of the bovine plasma amine oxidase and are oxidized to aldehydes. This reduces the enzyme by two electrons, and copper is required for the subsequent oxidation of the reduced enzyme by O/sub 2/ producing H/sub 2/O/sub 2/ and releasing NH/sub 3/. HS/sup -/ has been proposed to initially bind to the enzyme forming a Cu/sup II/-SH/sup -/ complex, which then undergoes further reaction to eventually produce Cu(I) and the reduced organic cofactor as products. The results of an x-ray absorption spectroscopic study to characterize the structure of the Cu/sup II/-SH/sup -/ complex are reported. 25 references, 2 figures, 1 table. |
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ISSN: | 0020-1669 1520-510X |
DOI: | 10.1021/ic00294a035 |