Abstract
Disulfide-containing proteins offer unique advantages for mechanistic studies of the formation of native three-dimensional structure from unordered, reduced precursors. The main advantage is that covalent intermediates are formed; by characterizing these intermediates, one obtains substantial information about the reaction pathway. Thiol- disulfide interchange is a major component of most oxidative mechanisms carrying thiol to disulfide; thus, it required some attention in its own right. Anfinsen’s descriptions of a “shuffle-ase” enzyme led us to examine the rates of the uncatalyzed exchange under physiologically plausible conditions. Somewhat surprisingly, we found that the rates for formation of several native proteins in uncatalyzed systems containing GSSG and GSH are as great as with the “shuffle-ase” enzyme, suggesting that a substantial portion of biological thiol oxidations proceed by uncatalyzed exchange. While thiol-disulfide exchange of course results in no net change in the oxidation level of a system, catalytic linkage of thiol or disulfide to other redox systems provides a mechanism for achieving net changes.
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References
Ahmed, A. K., Schaffer, S. W. and Wetlaufer, D. B. (1975). Non-enzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by gluathione oxido-reduction buffers. J. Biol. Chem. 250, 8477–82.
Anderson, W. L. and Wetlaufer, D. B. (1976). The folding pathway of reduced lysozyme. J. Biol. Chem. 251, 3147–53.
Anfinsen, C. B. (1967). The formation of the tertiary structure of proteins. The Harvey Lectures 61, 95–116.
Bernheim, F. and Bernheim, M. L. C. (1938). The effects of various metals and metal complexes on the oxidation of sulfhydryl groups. Cold Spring Harbor Sympos. on Quant. Biol. 7, 174–183.
Birkett, D. J. (1973). Mechanism of inactivation of rabbit muscle glyceraldehyde 3-phosphate dehydrogenase by ethacrynic acid. Mol. Pharmacol. 9, 209–218.
Black, S. and Colman, R. F. (1963). The biochemistry of sulfur-containing compounds. Ann. Rev. Biochem. 32, 399–418.
Bloksma, A. H. (1971) in Pomeranz, Y. ed. “Wheat Chemistry and Technology.” Amer. Assn. of Cereal Chemists, St. Paul, 1971, pp. 523–584.
Bradshaw, R. A., Kanarek, L. and Hill, R. L. (1967). The preparation, properties, and reactivation of the mixed disulfide derivative of egg white lysozyme and L-crystine. J. Biol. Chem. 242, 3789–3798.
Creighton, T. E. (1975). The two-disulfide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor. J. Mol. Biol. 95, 167–99.
DeLorenzo, F. and Molea, G. (1967). Relative levels of the disulfide-interchange enzyme in the microsomes of bovine tissues. Biochem. Biophys. Acta 146, 593–595.
Eldjarn, L. and Pihl, A. (1957). On the mode of action of X-ray protective agents II. The interaction between biologically important thiols and disulfides. J. Biol. Chem. 225, 499–510.
Eldjarn, L. and Pihl, A. (1957). On the mode of action of X-ray protective agents III. The enzymatic reduction of disulfides. J. Biol. Chem. 227, 339–345.
Epstein, C. J. (1970) in Anfinsen, C. B. ed. “Aspects of Protein Biosynthesis.” Part A, Acad. Press, N.Y. pp. 367–431.
Ernest, M. J. and Kim, K. (1973). Regulation of rat liver glycogen synthetase; reversible inactivation of glycogen synthetase D by sulfhydryl-disulfide exchange. J. Biol. Chem. 248, 1550–1555.
Fahey, R. C., Brody, S. and Mikolajczyk, S. D. (1975). Change in the glutathione thiol-disulfide status of Neurospora crassa conidia during germination and aging. J. Bacteriol. 121, 144–51.
Frankfater, A. and Fridovich, I. (1970). The purification and properties of oxidized derivatives of L-histidine ammonia-lyase. Biochem. Biophys. Acta 206, 457–472.
Givol, D., DeLorenzo, F., Goldberger, R. F., and Anfinsen, C. B. (1965). Disulfide interchange and the three dimensional structure of proteins. Proc. Nat’1 Acad. Sci. U.S. 53, 676–684.
Givol, D., Goldberger, R. F., and Anfinsen, C. B. (1963). Oxidation and disulfide interchange in the reactivation of reduced ribonuclease. J. Biol. Chem. 239, 3114–3116.
Goldberger, R. F., Epstein, C. J. and Anfinsen, C. B. (1964). Purification and properties of a microsomal enzyme, system catalyzing the reactivation of reduced ribonuclease and lysozyme. J. Biol. Chem. 239, 1406–1410.
Gregory, E. M. and Fridovich, I. (1973). Oxygen toxicity and superoxide dismutase. J. Bacteriol. 114, 1193–1197.
Habig, W. H., Pabst, M. J. and Jakoby, W. B. (1974). Glutathione S-transferases; the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130–39.
Isaacs, J. T. (1976). Glutathione systems and the control of the protein SS/SH ratio. Fed. Proc. 35, Abstract No. 605.
Jocelyn, P. C. (1967). The standard redox potential of cysteine-cystine from the thiol-disulfide exchange reaction with glutathione and lipoic acid. Eur. J. Biochem. 2, 327–331.
Jocelyn, P. C. (1972). Biochemistry of the SH group. Acad. Press, London, p. 10.
Lamfrom, H. and Nielsen, S. O. (1958). Mercaptolysis of cystine— synthesis of an asmymetric disulfide containing half-cystine. Compt. Rend. Trav. du Lab. Carlsberg, Ser. Chim. 30, 349–359.
Lee, J. H. (1956). The influence of copper deficiency on the fleece of British breeds of sheep. J. Agr. Sci. 47, 218–24.
Liener, I. E. and Hogle, J. (1973). Reduction and reactivation of the Bowman-Birk soybean inhibitor. Canad. J. Biochem. 51, 1014–1020.
Mills, G. C. (1960). Glutathione peroxidase and the destruction of hydrogen peroxide in animal tissues. Arch. Biochem. Biophys. 86, 1–5.
Mize, C. E. Langdon, R. and Thompson, T. E. (1962). Hepatic gutathione reductase II. Physical properties and mechanism of action. J. Biol. Chem. 237, 1596–1600.
Nowak T. and Hirnes, R. H. (1971). Formyltetrahydrofolate synthetase; the role of the sulfhydryl groups. J. Biol. Chem. 246, 1285–1293.
Peterson, J. G. L. and Dorrington, K. J. (1974). An in vitro system for studying the kinetics of interchain disulfide bond formation in immunoglobulin G. J. Biol. Chem. 249, 5633–5641.
Pontremoli, S. and Horecker, B. L. (1970). Current topics in cellular regulation. Acad. Press, N.Y., Vol. 2, 188–195.
Saxena, V. P. and Wetlaufer, D. B. (1970). Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9, 5015–5023.
Sinha, N. K. and Light, A. (1975). Refolding of reduced, denatured trypsinogen and trypsin immobilized on agarose beads. J. Biol. Chem. 250, 8624–8629.
Sumegi, J., Sanner, T. and Pihl, A. (1971). Involvement of Highly reactive sulfhydryl groups in the action of RNA polymerase from E. Coli. FEBS Letters 16, 125.
Teale, J. M. and Benjamin, D. C. (1976). Antibody as an immunological probe for studying the refolding of bovine serum albumin. I. The catalysis of reoxidation of reduced bovine serum albumin by glutathione and a disulfide interchange enzyme. II. Evidence for the independent refolding of the domains of the molecule. J. Biol. Chem. 251, 4603–4608, 4609-4615.
Tietze, F. (1969). Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Bioch. 27, 502–522.
Wang, S. and Volini, M. (1968). Studies on the active side of rhodanase. J. Biol. Chem. 243, 5465–5470.
Wetlaufer, D. B., Johnson, E. R. and Clauss, L. M. (1974) in Osserman, E., Beychok, S. and Canfield R. eds. Lysozyme. Acad. Press, N.Y., pp. 269–280.
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Wetlaufer, D.B. et al. (1977). Protein Thiol-Disulfide Interchange and Interfacing with Biological Systems. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3282-4_3
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DOI: https://doi.org/10.1007/978-1-4684-3282-4_3
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