Bicarbonate is required for the peroxidase function of Cu,Zn-superoxide dismutase at physiological pH

Journal of Biological Chemistry

Volumn 274, Issue 3, 1999, Pages 1226-1232

  Sankarapandi, Sornampillai ^a   Zweier, Jay L ^a,b  

^a DEPARTMENT OF PATHOLOGY   (United States)

^b JOHNS HOPKINS ASTHMA AND ALLERGY CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BICARBONATE; COPPER ZINC SUPEROXIDE DISMUTASE; PEROXIDASE;

ARTICLE; CATTLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ERYTHROCYTE; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PH; PRIORITY JOURNAL;

ANIMALS; BICARBONATES; BINDING SITES; CATTLE; COPPER; CYCLIC N-OXIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; OXIDATION-REDUCTION; PEROXIDASE; SUPEROXIDE DISMUTASE;

BOS TAURUS;

EID: 0033555968     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.3.1226     Document Type: Article

References (51)

1. McCord, J. M., and Fridovich, I. (1969) J. Biol. Chem. 244, 6049-6055
2. Bannister J. V., Bannister, W. H., and Rotilio, G. (1987) CRC Crit. Rev. Biochem. 22, 111-180
3. Symonyan, M. A., and Nalbandyan, R. M. (1972) FEBS Lett. 28, 22-34
4. Bray, R. C., Cockle, S. H., Fielden, E. M., Roberts, P. B., Rotilio, G., and Calabrese, L. (1974) Biochem. J. 139, 43-48
5. Hodgson, E. K., and Fridovich, I. (1975)Biochemistry 14, 5294-5299
6. Blech, D. M., and Borders, C. L., Jr. (1983) Arch. Biochem. Biophys. 224, 579-586
7. Borders, C. L., Jr., and Fridovich, I. (1985) Arch. Biochem. Biophys. 241, 472-476
8. Salo, D. C., Pacifici, R. E., Lin, S. W., Giulivi, C., and Davies, K J. A. (1990) J. Biol. Chem. 265, 11919-11927
9. Sato, K., Akaike, T., Kohno, M., Ando, M., and Maeda, H. (1992) J. Biol. Chem. 267, 25371-25377
10. Yim, M. B., Chock, P. B., and Stadtman, E. R. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 5006-5010
11. Yim, M. B., Chock, P. B., and Stadtman, E. R. (1993) J. Biol. Chem. 268, 4099-4105
12. Cabelli, D. E., Allen, D., Bielski, B. H. J., and Holcman, J. (1989) J. Biol. Chem. 264, 9967-9971
13. Uchida, K., and Kawakishi, S. (1994) J. Biol. Chem. 269, 2405-2410
14. Hodgson, E. K., and Fridovich, I. (1975) Biochemistry 14, 5299-5303
15. Fridovich, I. (1995) Annu. Rev. Biochem. 64, 97-112
16. Fuchs, H. J. R., and Borders, C. L., Jr. (1983) Biochem. Biophys. Res. Commun. 241, 472-476
17. Viglino, P., Scarpa, M., Rotilio, G., and Rigo, A. (1988) Biochim. Biophys. Acta 962, 77-82
18. Sinet, P.-M., and Garber, P. (1981) Arch. Biochem. Biophys. 212, 411-416
19. Wiedau-Pazos, M, Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., and Bredesen, D. E. (1996) Science 271, 515-518
20. Yim, H. -S., Kang, J. -H., Chock, P. B., Stadtman, E. R., and Yim, M. B. (1997) J. Biol. Chem. 272, 8861-8863
21. Beauchamp, C., and Fridovich, I. (1971) Anal. Biochem. 44, 276-287
22. Aisen, P., Liebman, A., and Zweier, J. L. (1990) J. Biol. Chem. 253, 1930-1937
23. Kuppusamy, P., and Zweier, J. L. (1992) Appl. Rad. Isotop. 44, 367-372
24. Zweier, J. L. (1988) J. Biol. Chem. 263, 1353-1357
25. Zweier, J. L., Kuppusamy, P., and Lutty, G. A. (1988) Proc. Natl. Acad. Sci. U. S. A. 86, 4046-4050
26. Rigo, A., Stevanato, R., Viglino, P., and Rotilio, G. (1977) Biochem. Biophys. Res. Commun. 79, 776-783
27. Fee, J. A., and Gaber, B. P. (1972) J. Biol. Chem. 247, 60-65
28. Djinovic-Carugo, K., Polticelli, F., Desideri, A., Rotilio, G., Wilson, K. S., and Bolognesi, M. (1994) J. Mol. Biol. 240, 179183
29. Rotilio, G., Morpurgo, L., Giovagnoli, C., Calabrese, L., and Mondovi, B. (1972) Biochemistry 11, 2187-2192
30. Strothkamp, K. G., and Lippard, S. J. (1981) Biochemistry 20, 7488-7493
31. Cocco, D., Rossi, L., Barraa, D., Bossa, F., and Rotilio, G. (1982) FEBS Lett. 150, 303-306
32. Mota de Freitas, D., and Valentine, J. S. (1984) Biochemistry 23, 2079-2082
33. Bertini, I., Lanini, G., Luchinat, C., Messori, L., Monnanni, R., and Scozzafava, A. (1985) J. Am. Chem. Soc. 107, 4391-4396
34. Valentine, J. S., and Mota de Freitas D., (1986) in Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine (Rotilio, G., ed), pp. 149, Elsevier, Amsterdam
35. Sette, M., Paci, M., Desideri, A., and Rotilio, G. (1992) Biochemistry 31, 12410-12415
36. Fee, J. A., Peisach, J., and Mims, W. B. (1981) J. Biol. Chem. 256, 1910-1914
37. Getzoff, E. D., Tainer, J. A., Weiner, P. K., Kollman, P. A., Richardson, J. S., Richardson, D. C. (1983) Nature 306, 287-290
38. Mottley, C., Mason, R. P., Chignell, C. F., Sivarajah, K., and Eling, T. E. (1982) J. Biol. Chem. 257, 5050-5055
39. Childs, R. E., and Bardsley, W. G. (1975) Biochem. J. 145, 93-103
40. Fridovich, I. (1978) Science 201, 875-880
41. Zweier, J. L., Flaherty, J. T., and Weisfeldt, M. L. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 1404-1407
42. Elroy-Stein, O., and Groner, Y. (1988) Cell 52, 259-267
43. Scott, M. D., Meshnick, S. R., and Eaton, J. W. (1989) J. Biol. Chem. 264, 2498-2501
44. Rosen, D. R., et al. (1993) Nature 362, 59-62
45. Siddique, T. and Deng, HX (1996) Hum. Mol. Genet. 5, 1465-1470
46. Banci, L., Bertini, I., Luchinat, C., and Scozzafava, A. (1989) J. Biol. Chem. 264, 9742-9744
47. Segel, I. H. (1993) Enzyme Kinetics, John Wiley & Sons, New York, pp. 250-258
48. Zweier, J. L., Aisen, P., Peisach, J., and Mims, W. B. (1979) J. Biol. Chem. 254, 3512-3515
49. Zweier, J. L., Wooten, J. B., and Cohen, J. S. (1981) Biochemistry 20, 3505-3510
50. Smith, C. A., Anderson, B. F., Baker, H. M., Baker, E. N. (1992) Biochemistry 31, 4527-4533
51. Zweier, J. L., Wang, P., Samuilov, A., and Kuppusamy, P. (1995) Nat. Med. 1, 804-809