Biochemical properties of Cu/Zn-superoxide dismutase from fungal strain Aspergillus niger 26

Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy

Volumn 71, Issue 3, 2008, Pages 975-983

  Dolashki, Aleksandar ^a   Abrashev, Radoslav ^b   Stevanovic, Stefan ^a   Stefanova, Lilyana ^b   Ali, Syed Abid ^c   Velkova, Ludmila ^d   Hristova, Rumyana ^d   Angelova, Maria ^b   Voelter, Wolfgang ^a   Devreese, Bart ^e   Van Beeumen, Jozef ^e   Dolashka Angelova, Pavlina ^d  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b INSTITUTE OF MICROBIOLOGY   (Bulgaria)

^c UNIVERSITY OF KARACHI   (Pakistan)

^d INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

^e GHENT UNIVERSITY   (Belgium)

Author keywords

Aspergillus niger 26; Cu Zn superoxide dismutase; Fluorescence and CD spectroscopy; Mn SOD

Indexed keywords

AMINATION; AMINO ACIDS; BRIDGES; CARBOHYDRATES; ENZYME ACTIVITY; ENZYMES; MANGANESE; MANGANESE COMPOUNDS; ORGANIC ACIDS; ORGANIC COMPOUNDS; OXYGEN; PH EFFECTS;

ASPERGILLUS NIGER 26; CU/ZN-SUPEROXIDE DISMUTASE; FLUORESCENCE AND CD SPECTROSCOPY; MN-SOD;

AMINES;

ISOENZYME; SUPEROXIDE DISMUTASE;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS NIGER; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYMOLOGY; GENETICS; MASS SPECTROMETRY; MOLECULAR GENETICS; MOLECULAR WEIGHT; PH; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; SPECTROFLUOROMETRY; TEMPERATURE; ULTRAVIOLET SPECTROPHOTOMETRY;

AMINO ACID SEQUENCE; ASPERGILLUS NIGER; CATALYTIC DOMAIN; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPEROXIDE DISMUTASE; TEMPERATURE;

EID: 53849137341     PISSN: 13861425     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.saa.2008.02.023     Document Type: Article

References (40)

1. McCord J.M., and Fridovich I. J. Biol. Chem. 244 (1969) 6049-6055
2. Fridovich I. Toxicology 23 (1983) 239-257
3. Valentine J.S., Wertz D.L., Lyons T.J., Liou L., Goto J.J., and Gralla E.B. Curr. Opin. Chem. Biol. 2 (1998) 253-262
4. Fridovich I. J. Biol. Chem. 272 (1997) 18515-18517
5. H.M. Hassan, C.S. Moody, in: G. Rotilio (Ed.), Elsevier Science Publisher, New York, pp. 274-279, 1986.
6. Fridovich I. Annu. Rev. Biochem. 44 (1975) 147-159
7. Fridovich I. Adv. Enzymol. Relat. Areas Mol. Biol. 58 (1986) 61-67
8. Dolashka-Angelova P., Genova L., Stoeva S., Stefanov B., Angelova M., Hristova R., Pashova S., and Voelter W. J. Peptide. Res. 54 (1999) 279-289
9. Dolashka-Angelova P., Angelova M., Genova L., Stoeva S., and Voelter W. Spectrochim. Acta A. Mol. Biomol. Spectrosc. 55A (1999) 2249-2260
10. Wang Z., He Z., Shen Q., Gu Y., Li S., and Yuan Q. J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 826 1-2 (2005) 114-121
11. Yost F.J., and Fridovich I. J. Biol. Chem. 248 (1973) 4905-4908
12. Youn H.D., Kim E.J., Roew J.H., Hah Y.C., and Kang S.O. Biochem. J. 318 (1996) 889-896
13. Fréalle E., Noël C., Viscogliosi E., Camus D., Dei-Cas E., and Delhaes L. FEMS Immunol. Med. Microbiol. 45 (2005) 411-422
14. Haddad N.I., and Yuan Q. J. Chromatogr. B. Anal. Technol. Biomed. Life Sci. 818 (2005) 123-131
15. Kujumdzieva A., Nedeva T., Morfova M., and Savov V. J. Cult. Collections 2 (1997-1998) 44-50
16. Holdom M.D., Hay R.J., and Hamilton A.J. Infect Immun. 64 (1996) 3326-3332
17. Wang Z., He Z., Li S., and Yuan Q. Enzyme Microb. Technol. 36 (2005) 862-869
18. Dolashka-Angelova P., Stevanovic S., Dolashki A., Angelova M., Serkedjieva J., Krumova E., Pashova S., Zacharieva S., and Voelter W. Biochem. Biophys. Res. Commun. 317 (2004) 1006-1016
19. Flückiger S., Mitt P.R.E., Scapozza L., Fijten H., Folkers G., Grütter M.G., Blaser K., and Crameri R. J. Immunol. 168 3 (2002) 1267-1272
20. Parker M.W., and Blake C.C. FEBS Lett. 229 (1988) 337-382
21. Chary P., Dillon D., Schroeder A.L., and Natvig D.O. Genetics 137 (1994) 723-730
22. Díez B., Schleissner C., Moreno M.A., Rodríguez M., Collados A., and Barredo J.L. Curr. Genet. 33 (1998) 387-394
23. Crameri R., Faith A., Hemmann S., Juassi R., Ismail C., Menz G., and Blaser K. J. Exp. Méd. 184 (1996) 265-270
24. Fang G.-C., Hanau R.M., and Vaillancourt L.J. Fungal Genet. Biol. 36 (2002) 155-165
25. Chang E.C., and Kosman D.J. J. Bacteriol. 172 (1990) 1840-1845
26. Chang E.C., Crawford B., Hong Z., Bilinski T., and Kosman D.J. J. Biol. Chem. 266 (1991) 4417-4424
27. Slokoska L., and Angelova M. Z. Naturforsch. 53C (1998) 968-972
28. Angelova M., Dolashka-Angelova P., Ivanova E., Serkedjieva J., Slokoska L., Pashova S., Toshkova R., Vassilev S., Simeonov I., Hartmann H.J., Stoeva S., Weser U., and Voelter W. Microbiology 147 (2001) 1641-1650
29. Abrashev R., Dolashka-Angelova P., Hristova R., Stefanova L., and Angelova M. J. Appl. Microbiol. 99 (2005) 902-905
30. Beauchamp C., and Fridovich I. Anal. Biochem. 44 1 (1971) 276-287
31. Lowry O.H., Rosenbrough H.J., Faar A.L., and Randall R.J. J. Biol. Chem. 193 (1951) 265-275
32. Laemmli U.K. Nature 227 (1970) 680-685
33. Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M., Marmocchi F., Rotilio G., and Bolognesi M. J. Mol. Biol. 225 (1992) 791-809
34. Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., Shindyalov I.N., and Bourne P.E. The Protein Data Bank Nucl. Acids Res. 28 (2000) 235-242
35. Šali A., and Blundell T.L. J. Mol. Biol. 2 (1990) 403-428
36. Šali A., and Blundell T.L. J. Mol. Biol. 234 (1993) 779-815
37. Hooft R.W.W., Sander C., and Vriend G. Proteins 26 (1996) 363-376
38. Laskowski R.A., McArthur M.W., Moss D.S., and Thornton J.M. J. Appl. Crystallogr. 26 (1993) 283-291
39. Lehrer S.S. Biochemistry 10 (1971) 3254-3263
40. Krumova E., Dolashka-Angelova P., Pashova S., Stefanova L., Van Beeumen J., Vassilev S., and Angelova M. Enzyme Microb. Technol. 404 (2007) 524-532