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Synthesis, Spectroscopic, and X-Ray Structural Characterization of Methylmercury-D,L-Selenocysteinate Monohydrate, a Key Model for the Methylmercnry(II)-Selenoprotein Interaction

journal contribution
posted on 2023-05-25, 22:42 authored by Carty, AJ, Malone, SF, Taylor, Nicholas J, Canty, AJ
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.

History

Publication title

Journal of Inorganic Biochemistry

Volume

18

Article number

4

Number

4

Pagination

291-300

Publication status

  • Published

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The definitive version is available at http://www.sciencedirect.com

Repository Status

  • Restricted

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