Synthesis, Spectroscopic, and X-Ray Structural Characterization of Methylmercury-D,L-Selenocysteinate Monohydrate, a Key Model for the Methylmercnry(II)-Selenoprotein Interaction
Carty, AJ and Malone, SF and Taylor, NJ and Canty, AJ (1983) Synthesis, Spectroscopic, and X-Ray Structural Characterization of Methylmercury-D,L-Selenocysteinate Monohydrate, a Key Model for the Methylmercnry(II)-Selenoprotein Interaction. Journal of Inorganic Biochemistry, 18 (4). pp. 291-300.
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Official URL: http://dx.doi.org/10.1016/0162-0134(83)85044-2
Methylmercury-D.L-selenocysteinate monohydrate complex, a key model for the methylmercury(II)-selenoprotein interaction in vivo, has been prepared via the reaction of seleno-D,L-cysteine (from prior reduction of seleno-D,L-cystine) with methylmercury(II) hydroxide and characterized by single-crystal X-ray diffractometry. The selenoamino acid is coordinated to mercury via a deprotonated selenohydryl group [Hg-Se 2.469(4)A]. A very weak intramolecular Hg...O interaction [2.93(2)A] to a carboxylate group, and a similarly weak intermolecular Hg...Se interaction [3.737(4)A] to the adjacent selenocysteine moiety, are present. Individual molecules of the complex are linked by hydrogen bonds to solvent water molecules. Infrared and Raman spectra are reported; 1H and I99Hg nuclear magnetic resonance data, together with the structural data, support the view that the selenacysteinate group interacts more strongly with CH3Hg+ than the sulfur analogue. Strong Hg-Se bonding to selenocysteinate residues may play an important role in selenium protection in biology.
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|Deposited By:||Prof Allan J Canty|
|Deposited On:||18 Feb 2008 14:54|
|Last Modified:||18 Jul 2008 20:35|
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