Thiodiglycol, the hydrolysis product of sulfur mustard: Analysis of in vitro biotransformation by mammalian alcohol dehydrogenases using nuclear magnetic resonance

Toxicology and Applied Pharmacology

Volumn 213, Issue 3, 2006, Pages 207-215

  Brimfield, A A ^a   Novak, Mark J ^b   Hodgson, Ernest ^c  

^a US ARMY MEDICAL RESEARCH INSTITUTE OF CHEMICAL DEFENSE   (United States)

^b Florida Institute of Technology   (United States)

^c NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Alcohol dehydrogenase; In vitro metabolism; NMR; Sulfur mustard; Thiodiglycol

Indexed keywords

1,4 OXATHIAN 2 OL; 2 HYDROXYETHYLTHIOACETALDEHYDE; 2 HYDROXYETHYLTHIOACETALDEHYDE HYDRATE; 2 HYDROXYETHYLTHIOACETIC ACID; ACETIC ACID DERIVATIVE; ALCOHOL DEHYDROGENASE; ALCOHOL DERIVATIVE; ALDEHYDE DERIVATIVE; MUSTARD GAS; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXATHIIN DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIODIGLYCOL; UNCLASSIFIED DRUG; VASOPRESSIN; 2,2'-THIODIETHANOL; ISOENZYME; THIOL DERIVATIVE;

AEROBIC METABOLISM; ARTICLE; BIOTRANSFORMATION; ENZYME METABOLISM; IN VITRO STUDY; MAMMAL; NUCLEAR MAGNETIC RESONANCE; PROTON NUCLEAR MAGNETIC RESONANCE; SPECTROPHOTOMETRY; SYNTHESIS; ANIMAL; ENZYMOLOGY; HORSE; HUMAN; HYDROLYSIS; LIVER; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

MAMMALIA;

ALCOHOL DEHYDROGENASE; ANIMALS; BIOTRANSFORMATION; HORSES; HUMANS; HYDROLYSIS; ISOENZYMES; LIVER; MAGNETIC RESONANCE SPECTROSCOPY; MUSTARD GAS; SULFHYDRYL COMPOUNDS;

EID: 33745934918     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2005.11.009     Document Type: Article

References (26)

1. Abeles R.H., and Lee H.A. The dismutation of formaldehyde by alcohol dehydrogenase. J. Biol. Chem. 274 (1960) 7106-7107
2. Bartlett P.D., and Swain C.G. Kinetics of hydrolysis and displacement reactions of β,β′-dichlorodiethyl sulfide (mustard gas) and of β-chloro-β′-hydroxydiethyl sulfide (mustard chlorohydrin). J. Am. Chem. Soc. 71 (1949) 1406-1415
3. Bell R.P., and Evans P.G. Kinetics of the dehydration of methylene glycol in aqueous medium. Proc. R. Soc. London, Ser. A 291 (1966) 297-323
4. Besseman S.P., and McCabe III E.R.B. 1,4-Butanediol-A substrate for rat liver and horse liver alcohol dehydrogenases. Biochem. Pharmacol. 21 (1972) 1135-1142
5. Black R.M., Brewster K., Clark R.J., Hambrook J.L., Harrison J.M., and Howells D.J. Metabolism of thiodiglycol (2,2′-thiobis-ethanol): isolation and identification of urinary metabolites following intraperitoneal administration to rat. Xenobiotica 23 (1993) 473-481
6. Brimfield A.A. Possible protein phosphatase inhibition by bis(hydroxy ethyl)sulfide a hydrolysis product of mustard gas. Toxicol. Lett. 78 (1995) 43-48
7. Brimfield A.A., Zweig L.M., Novak M.J., and Maxwell D.M. In vitro oxidation of the hydrolysis product of sulfur mustard, 2,2′-thiobis-ethanol, by mammalian alcohol dehydrogenases. J. Biochem. Mol. Toxicol. 12 (1998) 361-369
8. Corey E.J., and Schmidt G. Useful procedures for the oxidation of alcohols involving pyridinium dichromate in aprotic media. Tetrahedron. Lett. 5 (1979) 399-402
9. Choi J., Rose R.L., and Hodgson E. In vitro human metabolism of permethrin: the role of human alcohol and aldehyde dehydrogenases. Pestic. Biochem. Physiol. 73 (2002) 117-128
10. Dalziel K., and Dickerson F.M. Aldehyde mutase. Nature 206 (1965) 255-257
11. Davison C., Rozman R.S., and Smith P.K. Metabolism of bis-β-chloroethyl sulfide (sulfur mustard gas). Biochem. Pharmacol. 7 (1961) 65-74
12. Dudley B.F., Brimfield A.A., and Winston G.W. Oxidation of 2,2′-thiodiethanol by alcohol dehydrogenase: comparison of human isozymes. J. Biochem. Mol. Toxicol. 14 (2000) 244-251
13. Frey W.A., and Vallee B.L. Human liver alcohol dehydrogenase. An enzyme essential to the metabolism of digitalis. Biochem. Biophys. Res. Commun. 91 (1979) 1543-1548
14. Henehan G.T.M., Kenyon G.L., and Oppenheimer N.J. Oxidation of aldehydes by horse liver alcohol dehydrogenase. Adv. Exp. Biol. Med. 370 (1993) 481-491
15. Henehan G.T.M., and Oppenheimer N.J. Horse liver alcohol dehydrogenase-catalyzed oxidation of aldehydes: dismutation precedes net production of reduced nicotinamide adenine dinucleotide. Biochemistry 32 (1993) 735-738
16. Henehan G.T.M., Chang S.H., and Oppenheimer N.J. Aldehyde dehydrogenase activity of Drosophila melanogaster alcohol dehydrogenase: burst kinetics at high pH and aldehyde dismutase activity at physiological pH. Biochemistry 34 (1995) 12294-12301
17. Hinson J.A., and Neal R.A. An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase. Biochim. Biophys. Acta 384 (1975) 1-11
18. Hore P.J. Nuclear magnetic resonance. Solvent suppression. Methods Enzymol. 176 (1989) 64-77
19. Li Y.-M., and Casida J.E. Cantharidin-binding protein: identification as protein phosphatase 2A. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 11867-11870
20. McComb R.B., Bond L.W., Burnette R.W., Keech R.C., and Bowers G.N. Determination of the molar absorbtivity of NADH. Clin. Chem. 22 (1976) 141-150
21. Menon K.I., Feldwick M.G., Noaks P.S., and Mead R.J. The mode of toxification of the pesticide Gliftor: the metabolism of 1,3-difluoroacetone to (-)-erythro-fluorocitrate. J. Biochem. Mol. Toxicol. 15 (2001) 47-54
22. Oppenheimer N.J., and Henehan G.T.M. Horse liver alcohol dehydrogenase-catalyzed aldehyde oxidation. Adv. Exp. Biol. Med. 372 (1995) 407-415
23. Reddy, G., Major, M.A., Leach, G.J., in press. Toxicity assessment of thiodiglycol. Int. J. Toxicol.
24. Serafini-Cessi F. Conversion of allyl alcohol into acrolein by rat liver. Biochem. J. 128 (1972) 1103-1107
25. Velonia K., and Smonou I. Dismutation of aldehydes by alcohol dehydrogenases. J. Chem. Soc., Perkin Trans. 1 (2000) 2283-2287
26. Yang Y.-C., Szanfraniec L.L., Beaudry W.T., and Ward J.R. Kinetics and mechanisms of hydrolysis of 2-chloroethyl sulfides. J. Org. Chem. 53 (1988) 3293-3297