Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties

Protein Science

Volumn 13, Issue 5, 2004, Pages 1347-1355

  De Beus, Mitchel D ^a   Chung, Jinhyuk ^a   Colón, Wilfredo ^a  

^a Research Rensselaer Polytechnic Institute   (United States)

Author keywords

ALS; Copper; Cu Zn superoxide dismutase; Cysteine modification; Oxidative damage; Persulfide; SOD

Indexed keywords

COPPER; CYSTEINE 111; CYSTEINE DERIVATIVE; GLUTARALDEHYDE; HYDROGEN PEROXIDE; POTASSIUM CYANIDE; SODIUM SULFIDE; SULFIDE; SUPEROXIDE DISMUTASE; TRYPSIN; UNCLASSIFIED DRUG; ZINC;

ACIDITY; ADDITION REACTION; ARTICLE; BIOPHYSICS; CHEMICAL BOND; CHEMICAL MODIFICATION; CROSS LINKING; GEL ELECTROPHORESIS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; MOLECULAR WEIGHT; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN LOCALIZATION; REACTION ANALYSIS;

CYSTEINE; OXIDATION-REDUCTION; PEPTIDE MAPPING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS; SULFIDES; SUPEROXIDE DISMUTASE;

EID: 1942441011     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03576904     Document Type: Article

References (34)

1. Andersen, P.M., Sims, K.B., Xin, W.W., Kiely, R., O'Neill, G., Ravits, J., Pioro, E., Harati, Y., Brower, R.D., Levine, J.S., et al. 2003. Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: A decade of discoveries, defects and disputes. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 4: 62-67.
2. Andrus, P.K., Fleck, T.J., Gurney, M.E., and Hall, E.D. 1998. Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Neurochem. 71: 2041-2048.
3. Barrett, W.C., DeGnore, J.P., Konig, S., Fales, H.M., Keng, Y.F., Zhang, Z.Y., Yim, M.B. and Chock, P.B. 1999. Regulation of PTP1B via glutathionylation of the active site cysteine 125. Biochemistry 38: 6699-6705.
4. Battistoni, A., Folcarelli, S., Cervoni, L., Polizio, F., and Desideri, A. 1998. Role of the dimeric structure in the Cu, Zn superoxide dismutase. J. Biol. Chem. 273: 5655-5661.
5. Berni, R., Musci, G., Pallini, R., and Cannella, C. 1991. Chemical modification of rhodanese with sulphite. Free Radic. Res. Commun. 15: 203-209.
6. Bowling, A.C., Barkowski, E.E., McKenna-Yasek, D., Sapp, P., Horvitz, H.R., Beal, M.F. and Brown, R.H. 1995. Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis. J. Neurochem. 64: 2366-2369.
7. Briggs, R.G. and Fee, J.A. 1978. Sulfhydryl reactivity of human erythrocyte superoxide dismutase. On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin. Biochim. Biophys. Acta 537: 100-109.
8. Bush, A.I. 2002. Is ALS caused by an altered oxidative activity of mutant superoxide dismutase? Nat. Neurosci. 5: 919.
9. Calabrese, L., Federici, G., Bannister, W.H., Bannister, J.V., Rotilio, G., and Finazzi-Agro, A. 1975. Labile sulfur in human superoxide dismutase. Eur. J. Biochem. 56: 305-309.
10. Carrico, R.J. and Deutsch, H.F. 1969. Isolation of human hepatocuprein and cerebrocuprein. Their identity with erythrocuprein. J. Biol. Chem. 244: 6087-6093.
11. Chung, J., Yang, H., de Beus, M.D., Ryu, C.Y., Cho, K., and Colón, W. 2003. Cu/Zn superoxide dismutase can form pore-like structures. Biochem. Biophys. Commun. 312: 873-876.
12. Cleveland, D.W. and Rothstein, J.D. 2001. From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2: 806-819.
13. Crow, J.P., Sampson, J.B., Zhuang, Y., Thompson, J.A., and Beckman, J.S. 1997. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69: 1936-1944.
14. Gergel, D. and Cederbaum, A.I. 1996. Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc. Biochemistry 35: 16186-16194.
15. Gurney, M.E., Pu, H., Chiu, A.Y., Dal Canto, M.C., Polchow, C.Y., Alexander, D.D., Caliendo, C., Hentati, A., Kwon, Y.W., Deng, H., et al. 1994. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 264: 1772-1775.
16. Hallewell, R.A., Imlay, K.C., Lee, P., Fong, N.M., Gallegos, C., Getzoff, E.D., Tainer, J.A., Cabelli, D.E., Tekamp-Olson, P., Mullenbach, G.T., et al. 1991. Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines. Biochem. Biophys. Commun. 181: 474-480.
17. Jaswal, S.S., Sohl, J.L., Davis, J.H., and Agard, D.A. 2002. Energetic landscape of α-lytic protease optimizes longevitiy through kinetic stability. Nature 415: 343-346.
18. Khossravi, M., Shire, S.J., and Borchardt, R.T. 2000. Evidence of the involvement of histidine A(12) in the aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation. Biochemistry 39: 5876-5885.
19. Lashuel, H.A., Hartley, D., Petre, B.M., Walz, T., and Lansbury, Jr., P.T. 2002. Neurodegenerative disease: Amyloid pores from pathogenic mutations. Nature 418: 291.
20. Liu, H., Zhu, H., Eggers, D., Nersissian, A., Faull, K., Goto, J., Ai, J., Sanders-Loehr, J., Gralla, E., and Valentine, J. 2000. Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry 39: 8125-8132.
21. Mach, H., Dong, Z., Middaugh, C.R., and Lewis, R.V. 1991. Conformational stability of Cu,Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives: Second-derivative spectroscopy of phenylalanine and tyrosine residues. Arch. Biochem. Biophys. 287: 41-47.
22. McCord, J.M. and Fridovich, I. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049-6055.
23. Nebot, C., Moutet, M., Huet, P., Xu, J.-Z., Yadan, J.-C., and Chaudiere, J. 1993. Spectrophotometric assay of superoxide dismutase activity based on the activated autooxidation of a tetracyclic cathecol. Anal. Biochem. 214: 442-451.
24. Panda, M. and Horowitz, P.M. 2000. Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese. J. Protein Chem. 19: 399-409.
25. Parge, H.E., Hallewell, R.A., and Tainer, J.A. 1992. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. 89: 6109-6113.
26. Rakhit, R., Cunningham, P., Furtos-Matei, A., Dahan, S., Qi, X.F., Crow, J.P., Cashman, N.R., Kondejewski, L.H., and Chakrabartty, A. 2002. Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. J. Biol. Chem. 277: 47551-47556.
27. Reaume, A.G., Elliot, J.L., Hoffman, E.K., Kowall, N.W., Ferrante, R.J., Siwek, D.F., Wilcox, H.M., Flood, D.G., Beal, M.F., Brown, Jr., R.H., et al. 1996. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axotomy. Nat. Genet. 13: 43-47.
28. Ripps, M.E., Huntley, G.W., Hof, P.R., Morrison, J.H., and Gordon, J.W. 1995. Transgenic mice expressing an altered murine superoxide-dismutase gene provide an animal-model of amyotrophic-lateral-sclerosis. Proc. Natl. Acad. Sci. 92: 689-693.
29. Rotilio, G., Calabrese, L., Bossa, F., Barra, D., Agro, A.F., and Mondovi, B. 1972. Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase. Biochemistry 11: 2182-2187.
30. Simon, D.I., Mullins, M.E., Jia, L., Gaston, B., Singel, D.J., and Stamler, J.S. 1996. Polynitrosylated proteins: Characterization, bioactivity, and functional consequences. Proc. Natl. Acad. Sci. 93: 4736-4741.
31. Stadtman, E.R. and Berlett, B.S. 1997. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10: 485-494.
32. Turnbull, S., Tabner, B.J., Brown, D.R., and Allsop, D. 2003. Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. Neurosci. Lett. 336: 159-162.
33. Valentine, J.S. and Hart, P.J. 2003. Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. 100: 3617-3622.
34. Wong, P.C., Pardo, C.A., Borchelt, D.R., Lee, M.K., Copeland, N.G., Jenkins, N.A., Sisodia, S.S., Cleveland, D.W., and Price, D.L. 1995. An adverse property of a familial ALS-linked SODI mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14: 1105-1116.