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ABDUCTION OF IRON(III) FROM THE SOLUBLE METHANE MONOOXYGENASE HYDROXYLASE AND RECONSTITUTION OF THE BINUCLEAR SITE WITH IRON AND MANGANESE
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UNSPECIFIED (1993) ABDUCTION OF IRON(III) FROM THE SOLUBLE METHANE MONOOXYGENASE HYDROXYLASE AND RECONSTITUTION OF THE BINUCLEAR SITE WITH IRON AND MANGANESE. EUROPEAN JOURNAL OF BIOCHEMISTRY, 217 (1). pp. 217-223. ISSN 0014-2956
Full text not available from this repository.Abstract
The apo-form of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) was prepared via chelation of iron(III) with 3,4-dihydroxybenzaldehyde. The apohydroxylase was reconstituted by the anaerobic addition of Fe(II) followed by air oxidation. The enzyme thus prepared regained 85-90% of its original catalytic activity. The incorporation of two manganese(II) ions/mol of apohydroxylase was monitored by EPR spectroscopy. The Mn(II) ions occupy the native diiron active site and remain in the +2 oxidation state. The EPR data suggest strong coupling between the two Mn(II) ions and retention of the mu-hydroxo (alkoxo) bridge. The results of this study indicate that the M. capsulatus (Bath) hydroxylase contains a single diiron site.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Journal or Publication Title: | EUROPEAN JOURNAL OF BIOCHEMISTRY |
| Publisher: | SPRINGER VERLAG |
| ISSN: | 0014-2956 |
| Date: | 1 October 1993 |
| Volume: | 217 |
| Number: | 1 |
| Number of Pages: | 7 |
| Page Range: | pp. 217-223 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/21042 |
Data sourced from Thomson Reuters' Web of Knowledge
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