Prepration of Dimethyldithiocarbamate(DMC) by Reductive Disulfide Bond Breaking of Tetramethylthiuram(TMT) Disulfide in Presence of Mg++
Keywords:
DMC, TMC, LigandAbstract
The Mg(II) complex [Mg2(DMC)2((DMC)2] has been synthesized directly from thiram ligand, containing a disulfide bond and characterized by elemental analysis and spectroscopic methods. Surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with Zn2+ in methanolic media to give the Mg complex. The crystal structure of Mg++ complex has been determined by single crystal X-ray diffraction. Mg is +2 coordinate, with four nearly identical tetrahedral bonds and a longer fifth bond being similar to some reported [Mg(dtc)2(L)] complexes. The crystal structure of this complex is built up of dimeric units, [Mg(dmdtc)(dmdtc)2], so that each unit has two thiocarbamate groups, one wholly bound to a zinc atom as a bidentate ligand and the other in a bridging coordination mode between the two Mg++ atoms. This structure clearly shows scission of the disulfide bond in the thiram ligand to give two dimethyldithiocarbamate ligands coordinated to the Mg(II) ion.
References
Bednar RA. Reactivity and pH-dependence of thiol conjugation to N-ethylmaleimide -Detection of a conformational change in chalcone isomerase. Biochemistry. 1990;29:3684–3690. [PubMed] [Google Scholar]
Nagy P. Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways. Antioxid Redox Signal. 2013 [PMC free article] [PubMed] [Google Scholar]
Nelson JW, Creighton TE. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry. 1994;33:5974–5983. [PubMed] [Google Scholar]
Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, Gul S, Bokth A, Naeem A, Patel H, Thomas EW, Sreedharan SK, Verma C, Brocklehurst K. A classical enzyme active center motif lacks catalytic competence until modulated electrostatically. Biochemistry. 1997;36:9968–9982. [PubMed] [Google Scholar]
Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol. 1990;63:69–172. [PubMed] [Google Scholar]
Hansen RE, Ostergaard H, Winther JR. Increasing the reactivity of an artificial dithiol-disulfide pair through modification of the electrostatic milieu. Biochemistry. 2005;44:5899–5906. [PubMed] [Google Scholar]
Roos G, Foloppe N, Messens J. Understanding the pKa of redox cysteines: The key role of hydrogen bonding. Antioxid Redox Signal. 2013;18:94–127. [PubMed] [Google Scholar]
Bulaj G, Kortemme T, Goldenberg DP. Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry. 1998;37:8965–8972. [PubMed] [Google Scholar]
March J. Advanced Organic Chemistry. John Wiley. New York: 1985. [Google Scholar]
Shaked Z, Szajewski RP, Whitesides GM. Rates of thiol-disulfide interchange reactions involving proteins and kinetic measurements of thiol pKa values. Biochemistry. 1980;19:4156–4166. [PubMed] [Google Scholar]
Iversen R, Andersen PA, Jensen KS, Winther JR, Sigurskjold BW. Thiol-disulfide exchange between glutaredoxin and glutathione. Biochemistry. 2010;49:810–820. [PubMed] [Google Scholar]
Houk J, Whitesides GM. Structure reactivity relations for thiol disulfide interchange. J Am Chem Soc. 1987.109:6825–6836. [Google Scholar]
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2024 Dr. Pramod Kumar
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.