Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocols

Biophysical Journal

Volumn 87, Issue 3, 2004, Pages 1873-1880

  Fuentes, Lymari ^a   Oyola, Jessica ^a   Fernândez, Mónica ^a   Quiñones, Edwin ^a  

^a UNIVERSITY OF PUERTO RICO   (Puerto Rico)

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLAMIDE; APOAZURIN; AZURIN; COPPER; GADOLINIUM; GADOLINIUM AZURIN; LIGAND; METAL; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; FLUORESCENCE; MACROMOLECULE; PHOTOCHEMICAL QUENCHING; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN IMMOBILIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA; SOLVATION;

BACTERIA (MICROORGANISMS); LUCIA LIMBARIA; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 4444289990     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.042580     Document Type: Article

References (28)

1. Baker, E. N. 1988. Structure of azurin from Alcaligenes denitrificans refinement at 1.8 A resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203:1071-1095.
2. Bonander, N., J. Leckner, H. Guo, B. G. Karlsson, and L. Sjölin. 2000. Crystal structure of the disulfite bond-deficient azurin mutant C3A/C26A. How important is the S-S bond for folding and stability? Eur. J. Biochem. 267:4511-4519.
3. Burstein, E. A., E. A. Permyakov, V. A. Yashin, S. A. Burkhanov, and A. Finazzi-Agro. 1977. The fine structure of luminescence spectra of azurin. Biochim. Biophys. Acta. 491:155-159.
4. Eggers, D. K., and J. S. Valentine. 2001. Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci. 10:250-261.
5. El Baraka, M., R. Garcia, and E. Quinones. 1994. A study of the inclusion complexes of beta-cyclodextrin with three electronic states of 4-(N,N-dimethylamino)benzonitrile. J. Photochem. Photobiol. A-Chem. 79:181-187.
6. Gilardi, G., G. Mei, N. Rosato, G. W. Canters, and A. Finazzi-Agro. 1994, Unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy. Biochemistry. 33:1425-1432.
7. Gottfried, D. S., A. Kagan, B. M. Hoffman, and J. M. Friedman. 1999. Impeded rotation of a protein in a sol-gel matrix. J. Phys. Chem. B. 103:2803-2807.
8. Guzzi, R., L. Sportelli, C. La Rosa, D. Milardi, D. Grasso, M. P. Verbeet, and G. W. Canters. 1999. A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant. Biophys. J. 77:1052-1063.
9. Hansen, J. E., J. W. Longworth, and G. R. Fleming. 1990. Photophysics of metalloazurins. Biochemistry. 29:7329-7338.
10. Hutnik, C. M., and A. G. Szabo. 1989a. Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity. Biochemistry. 28:3923-3934.
11. Hutnik, C. M., and A. G. Szabo. 1989b. A time-resolved fluorescence study of azurin and metalloazurin derivatives. Biochemistry. 28:3935-3939.
12. Juszczak, L. J., and J. M. Friedman. 1999. UV resonance raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin. J. Biol. Chem. 274:30357-30360.
13. Khan, I., C. F. Shannon, D. Dantsker, A. J. Friedman, J. Perez-Gonzalez-de-Apodaca, and J. M. Friedman. 2000. Sol-gel trapping of functional intermediates of hemoglobin: geminate and bimolecular recombination studies. Biochemistry. 39:16099-16109.
14. Kroes, S. J., G. W. Canters, G. Gilardi, A. van Hoek, and A. J. W. G. Visser. 1998. Time-resolved fluorescence study of azurin variants: conformational hetorogeneity and tryptophan mobility. Biophys. J. 75: 2441-2450.
15. La Rosa, C., D. Milardi, D. Grasso, R. Guzzi, and L. Sportelli. 1995. Thermodynamics of the thermal unfolding of azurin. J. Phys. Chem. A. 99:14864-14870.
16. Leckner, J., N. Bonander, P. Wittung-Stafshede, B. G. Malmstrom, and B. G. Karlsson. 1997. The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc and apoprotein. Biochem. Biophys. Acta. 1342:19-27.
17. Mei, G., A. Di Venre, F. Malvezzi, G. Gilardi, N. Rosato, F. De Matteis, and A. Finnazzi-Agro. 1999. The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core. Eur. J. Biochem. 265:619-626.
18. Nar, H., A. Messerschmidt, R. Huber, M. van de Kamp, and G. W. Canters. 1991. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. J. Mol. Biol. 221:765-772.
19. Naro, F., M. G. Tordi, G. M. Giacometti, F. Tomei, A. M. Timerio, and L. Zolla. 2000. Metal binding to Pseudomonas aeruginosa azurin: a kinetic investigation. Z. Naturforsch. 55:347-354.
20. Nozaki, Y. 1970. The preparation of guanidine hydrochloride. Methods Enzymol. 26:43-50.
21. Pozdnyakova, I., J. Guidry, and P. Wittung-Stafshede. 2001. Copper stabilizes azurin by decreasing the unfolding rate. Arch. Biochem. Biophys. 390:146-148.
22. Pozdnyakova, I., and P. Wittung-Stafshede. 2001. Biological relevance of metal binding before protein folding. J. Am. Chem. Soc. 123:10135-10136.
23. Samuni, U., M. S. Navati, L. J. Juszczak, D. Dantsker, M. Yang, and J. M. Friedman. 2000. Unfolding and refolding of sol-gel encapsulated carbonmonoxymyoglobin: an orchestrated spectroscopic study of intermediates and kinetics? J. Phys. Chem. B. 104:10802-10813.
24. Schellman, J. A. 2003. Protein stability in mixed solvents: a balance of contact interaction and exclude volume. Biophys. J. 85:108-125.
25. Tanford, C. 1970. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1-95.
26. Winkler, J. R., P. Wittung-Stafshede, J. Leckner, B. G. Malmstrom, and H. B. Gray. 1997. Effects of folding on metalloprotein active sites. Proc. Natl. Acad. Sci. USA. 94:4246-4249.
27. Yamada, T., M. Goto, V. Punj, O. Zaborina, M. L. Chen, K. Kimbara, D. Majumdar, E. Cunningham, T. K. Das Gupta, and A. M. Chakrabarty. 2002. Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer. Proc. Natl. Acad. Sci. U.S.A. 99:14098-14103.
28. Zheng, L., W. R. Reid, and J. D. Brenan. 1997. Measurement of fluorescence from tryptophan to protein doped sol-gel-derived glass monoliths. Anal. Chem. 69:3940-3949.