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.
http://www.ncbi.nlm.nih.gov/corehtml...PubMedLink.gif 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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