| pubmed-article:8373399 | pubmed:abstractText | 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. | lld:pubmed |
