Rhodanese as a thioredoxin oxidase

International Journal of Biochemistry and Cell Biology

Volumn 32, Issue 4, 2000, Pages 465-473

  Nandi, Dhirendra L ^a   Horowitz, Paul M ^b   Westley, John ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FREE RADICAL; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; THIOREDOXIN; THIOREDOXIN OXIDASE; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; ENZYME STRUCTURE, FUNCTION AND VARIABILITY; LIVER METABOLISM; MITOCHONDRIAL RESPIRATION; NONHUMAN; OXIDATION;

ANIMALS; CATALYSIS; CATTLE; ESCHERICHIA COLI; ISOENZYMES; LIVER; OXIDATION-REDUCTION; REACTIVE OXYGEN SPECIES; RECOMBINANT PROTEINS; THIOREDOXIN; THIOSULFATE SULFURTRANSFERASE;

BOVINAE; MAMMALIA;

EID: 0034174530     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00035-7     Document Type: Article

References (30)

1. Westley J. Rhodanese. Adv. Enzymol. 39:1973;327-368.
2. Sorbo B.H. Metabolism of sulfur compounds. Greenberg D.M. Metabolic pathways, 3rd ed. Vol. 7:1975;433-455 Academic Press, New York.
3. Westley J. Sulfane-transfer catalysis by enzymes. Van Tamelen E.E. Bioorganic Chemistry. Vol. 1:1977;371-390 Academic Press, New York.
4. Finazzi-Agro A., Federici C., Giovagnoli C., Cannella C., Cavallini D. Effect of sulfur binding on rhodanese fluorescence. Eur. J. Biochem. 28:1972;83-93.
5. Lang K. Die Rhodanbildung im Tierkorper. Biochem. Z. 259:1933;243-256.
6. Volini M., Craven D., Ogata K. Rhodanese-iron protein association in bovine liver extracts. Biochem. Biophys. Res. Commun. 79:1977;890-896.
7. Pagani S., Bonomi F., Cerletti P. Sulfide insertion into spinach ferredoxin by rhodanese. Biochim. Biophys. Acta. 700:1982;154-164.
8. Ogata K., Dai X., Volini M. Bovine mitochondrial rhodanese is a phosphoprotein. J. Biol. Chem. 264:1989;2718-2725.
9. Blumenthal K.M., Heinrikson R.L. Structural studies of bovine liver rhodanese. J. Biol. Chem. 246:1971;2430-2437.
10. Cannella C., Costa M., Pensa M.B., Ricci G., Pecci L., Cavallini D. Multiple forms of bovine liver rhodanese. Eur. J. Biochem. 119:1981;491-495.
11. Villarejo M., Westley J. Mechanism of rhodanese catalysis of thiosulfate-lipoate oxidation-reduction. J. Biol. Chem. 238:1963;4016-4020.
12. Volini M., Westley J. The mechanism of rhodanese-catalyzed thiosulfate-lipoate reaction. J. Biol. Chem. 241:1966;5168-5176.
13. Holmgren A. Thioredoxin. Ann. Rev. Biochem. 54:1985;237-271.
14. Silverman R.B., Nandi D.L. Reduced thioredoxin: a possible cofactor for vitamin K epoxide reductase. Further support for an active site disulfide. Biochem. Biophys. Res. Commun. 155:1988;1248-1254.
15. Nandi D.L., Westley J. Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Int. J. Biochem. Cell Biol. 30:1998;973-977.
16. McCord J.M. Free radicals and myocardial ischemia: overview and outlook. Free Rad. Biol. Med. 4:1988;9-14.
17. Mintel R., Westley J. The rhodanese reaction: mechanism of thiosulfate binding. J. Biol. Chem. 241:1966;3381-3385.
18. Westley J., Heyse D. Mechanism of sulfur transfer catalysis: sulfhydryl-catalyzed transfer of thiosulfonate sulfur. J. Biol. Chem. 246:1971;1468-1474.
19. Horowitz P.M. Purification of sulfurtransferase by selective immobilization on blue agarose. Anal. Biochem. 86:1978;751-753.
20. Miller D.M., Delgado R., Chirgwin J.M., Hardies S.C., Horowitz P.M. Expression of cloned bovine adrenal rhodanese. J. Biol. Chem. 266:1991;4686-4691.
21. Sorbo B.H. Crystalline rhodanese 1. Purification and physicochemical examination. Acta Chem. Scand. 7:1953;1129-1136.
22. De Sandro V., Dupuy C., Richert L., Cordier A., Pommier J. A method for measuring hydrogen peroxide based on the potentiation of peroxidative NADPH oxidation by superoxide dismutase and scopoletin. Anal. Biochem. 206:1992;408-413.
23. Westley J. Thiosulfate: cyanide sulfurtransferase (rhodanese). Jakoby W.B. Methods in Enzymology. Vol. 77:1981;285-291 Academic Press, New York.
24. Weng L., Heinrikson R.L., Westley J. Active site cysteinyl and arginyl residues of rhodanese. J. Biol. Chem. 253:1978;8109-8119.
25. Misra H.P. Generation of superoxide free radical during the autooxidation of thiols. J. Biol. Chem. 249:1974;2151-2155.
26. Costa M., Pecci L., Pensa B., Cannella C. Hydrogen peroxide involvement in the rhodanese inactivation by dithiothreitol. Biochem. Biophys. Res. Commun. 78:1978;596-603.
27. Horowitz P.M., Bowman S. Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents. J. Biol. Chem. 262:1987;8728-8733.
28. Horowitz P.M., Criscimagna N.L. Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese. J. Biol. Chem. 263:1988;10278-10283.
29. Horowitz P.M., Bowman S. Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation. J. Biol. Chem. 264:1989;3311-3316.
30. Cannella C., Berni R. Interaction of rhodanese with intermediates of oxygen reduction. FEBS Lett. 162:1983;180-184.