19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenase.
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.
LEDSS, Bâtiment Chimie Recherche, Université Joseph Fourier, Grenoble, France.
S
S
Hamman
M
M
Atta
A
A
Ehrenberg
P
P
Wilkins
H
H
Dalton
C
C
Béguin
M
M
Fontecave
D001665:Binding Sites; D005459:Fluorides / Q000378:metabolism*; D005461:Fluorine; D007700:Kinetics; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008345:Manganese / Q000378:metabolism; D010105:Oxygenases / Q000378:metabolism*; D012264:Ribonucleotide Reductases / Q000378:metabolism*
D046911:Macromolecular Substances; D005461:Fluorine; D008345:Manganese; D010105:Oxygenases; C021555:methane monooxygenase; D012264:Ribonucleotide Reductases; D005459:Fluorides