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Default 19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and me

19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenase.

Related Articles 19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenase.

Biochem Biophys Res Commun. 1993 Sep 15;195(2):594-9

Authors: Hamman S, Atta M, Ehrenberg A, Wilkins P, Dalton H, Béguin C, Fontecave M

The relaxation rates of fluoride, determined by 19F NMR spectroscopy, were greatly increased in the presence of protein Mn-A, the manganese form of the hydroxylase component of methane monooxygenase. This demonstrates that F- interacts with the manganese center of protein Mn-A. On the contrary, protein Mn-R2, the manganese form of the small subunit of ribonucleotide reductase, had no effect on the relaxation rate of F-. This reflects differences between the two proteins in terms of the accessibility of the metal ion sites, despite the strong similarities of these sites.

PMID: 8373399 [PubMed - indexed for MEDLINE]



Source: PubMed
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