Thermal unfolding studies of a phytocyanin

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 12, 2008, Pages 1997-2003

  Guzzi, Rita ^a   Sportelli, Luigi ^a   Sato, Katsuko ^b   Cannistraro, Salvatore ^c   Dennison, Christopher ^b  

^a UNIVERSITY OF CALABRIA   (Italy)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c CNISM   (Italy)

Author keywords

Calorimetry; Fluorescence; Lumry Eyring model; Thermal unfolding; Umecyanin

Indexed keywords

COPPER PROTEIN; UMECYANIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

ABSORPTION SPECTROSCOPY; ALKALINITY; ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE SPECTROSCOPY; HORSERADISH; PH; PLANT ROOT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING;

ARMORACIA; CALORIMETRY, DIFFERENTIAL SCANNING; ENTROPY; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; METALLOPROTEINS; MODELS, MOLECULAR; PLANT PROTEINS; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

ARMORACIA RUSTICANA;

EID: 54949145315     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.07.005     Document Type: Article

References (41)

1. Nersissian A.M., and Shipp S.L. Blue copper-binding domain. Adv. Prot. Chem. 60 (2002) 271-340
2. Dennison C. Investigating the structure and function of cupredoxins. Coord. Chem. Rev. 24 (2005) 3025-3054
3. Hart P.J., Nersissian A.M., Herrmann R.G., Nalbandya R.M., Valentine J.S., and Eisenberg D.A. Missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 angstrom resolution. Protein Sci. 5 (1996) 2175-2181
4. Guss J.M., Merritt E.A., Phizackerely R.P., and Freeman H.C. The structure of a phytocyanin, the basic blue copper from cucumber refined at 1.8 angstrom resolution. J. Mol. Biol. 262 (1996) 686-705
5. Koch M., Velarde M., Harrison M.D., Echt S., Fisher M., Messerschmidt A., and Dennison C. Crystal structures of oxidized and reduced stellacyanin from horseradish root. J. Am. Chem. Soc. 127 (2005) 158-166
6. Nersissian A.M., Immoos C., Hill M.G., Hart P.J., Williams G., Herrmann R.G., and Valentine J.S. Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins. Protein Sci. 7 (1998) 915-1929
7. Sato K., Crowley P.B., and Dennison C. Transient protein interactions between cytochrome f and the phytocyanin umecyanin. ChemBioChem. 8 (2007) 732-735
8. Fernandez C.O., Sannazzaro A.I., and Vila A.J. Alkaline transition of Rhus vernicifera stellacyanin, un unusual blue copper protein. Biochemistry 36 (1997) 10566-10570
9. Dennison C., and Lawler A.T. Investigation of the alkaline and acid transition of umecyanin, a stellacyanin from horseradish roots. Biochemistry 40 (2001) 3158-3166
10. Dennison C., Harrison M.D., and Lawler A.T. Alkaline transition of phytocyanins: a comparison of stellacyanin and umecyanin. Biochem. J. 371 (2003) 377-383
11. Harrison M.D., Yanagisawa S., and Dennison C. Investigating the cause of the alkaline transition of phytocyanins. Biochemistry 44 (2005) 3056-3064
12. Dennison C., and Harrison M.D. The active-site structure of umecyanin, the stellacyanin from horseradish roots. J. Am. Chem. Soc. 126 (2004) 2481-2489
13. Delfino I., Sato K., Harrison M.D., Andolfi L., Bizzarri A.R., Dennison C., and Cannistraro S. Optical investigation of the alkaline transition in umecyanin from horseradish root. Biochemistry 44 (2005) 16090-16097
14. Thomann H., Bernardo M., Baldwin M.J., Lowery M.D., and Solomon E.I. Pulsed ENDOR study of the native and high perturbed forms of the blue copper site in stellacyanin. J. Am. Chem. Soc. 113 (1991) 5911-5913
15. Fields B.A., Guss J.M., and Freeman H.C. Three-dimensional model for stellacyanin, a "blue" copper-protein. J. Mol. Biol. 222 (1991) 1053-1065
16. van de Kamp M., Canters G.W., Andrew C.R., Sanders-Loehr J., Bender C.J., and Peisach J. Effect of lysine ionization on the structure and electrochemical behaviour of the Met44→Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa. Eur. J. Biochem. 218 (1993) 229-238
17. Dennison C., Van Driessche G., Van Beeumen J., McFarlane W., and Sykes A.G. Electron-transfer properties and active-site structure of the type 1 (blue) copper protein umecyanin. Chem. Eur. J. 1 (1996) 104-109
18. Battistuzzi G., Bellei M., Dennison C., Di Rocco G., Sato K., Sola M., and Yanagisawa S. Thermodynamics of the alkaline transition in phytocyanins. J. Biol. Inorg. Chem. 12 (2007) 895-900
19. Thorolfsson M., Ibarra-Molero B., Fojan P., Petersen S.B., Sanchez-Ruiz J.M., and Martinez A. l-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry 41 (2002) 7573-7585
20. Dzwolak W., Ravindra R., and Winter R. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 42 (2003) 11347-11355
21. Sandberg A., Harrison D.J., and Karlsson B.G. Thermal denaturation of spinach plastocyanin: effect of copper oxidation state and molecular oxygen. Biochemistry 42 (2003) 10301-10310
22. Quesada-Soriano I., Garcia-Maroto F., and Garcia-Fuentes L. Kinetic study on the irreversible thermal denaturation of Schistisoma japonicum glutathione s-transferase. Biochim. Biophys. Acta 1764 (2006) 979-984
23. Feio M.J., Diaz-Quintana A., Navarro J.A., and De la Rosa M.A. Thermal unfolding of plastocyanin from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and comparison with its thermophilic counterpart from Phormidium laminosum. Biochemistry 45 (2006) 4900-4906
24. Guzzi R., Sportelli L., La Rosa C., Milardi D., Grasso D., Verbeet M.Ph., and Canters G.W. A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant. Biophys. J. 77 (1999) 1052-1063
25. Ma J.K., Bishop G.R., and Davidson V.L. The ligand geometry of copper determines the stability of amicyanin. Arch. Biophys. Biochem. 444 (2005) 27-33
26. Fitzsimons S.M., Mulvihill D.M., and Morris E.R. Denaturation and aggregation process in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocoll. 21 (2007) 638-644
27. Guzzi R., Andolfi L., Cannistraro S., Verbeet M.Ph., Canters G.W., and Sportelli L. Thermal stability of wild type and disulfide bridge containing mutant of poplar plastocyanin. Biophys. Chem. 112 (2004) 35-43
28. Shosheva A., Donchev A., Dimitrov M., Kostov G., Toromanov G., Getov V., and Alexov E. Comparative study of the stability of poplar plastocyanin isoforms. Biochem. Biophys. Acta 1748 (2005) 116-127
29. Einsle O., Mehrabian Z., Nalbandyan R., and Messerschmidt A. Crystal structure of plantacyanin, a basic blue cupredoxin from spinach. J. Biol. Inorg. Chem. 5 (2000) 666-672
30. Rodriguez-Larrea D., Ibarra-Molero B., de Maria L., Borchert T.V., and Sanchez-Ruiz J.M. Beyond Lumry-Eyring: an unexpected pattern of operational reversibility/irreversibility in protein denaturation. Proteins 70 (2008) 19-24
31. Lepock J.R., Frey H.E., and Hallewell R.A. Contribution of conformational stability and reversibility of unfolding to the increased thermostability of human and bovine superoxide dismutase mutated at free cysteines. J. Biol. Chem. 265 (1990) 21612-21618
32. Sandberg A., Leckner J., Shi Y., Schwarz F.P., and Karlsson B.G. Effects of metal ligation and oxygen on the reversibility of the thermal denaturation of Pseudomonas aeruginosa azurin. Biochemistry 41 (2002) 1060-1069
33. Tigerstrom A., Schwarz F.P., Karlsson B.G., Okvist M., Alvarez-Rua C., Maeder D., Robb F.T., and Sjolin L. Effects of a novel disulfide bond and engineered electrostatic interactions on the thermostability of azurin. Biochemistry 43 (2004) 12563-12574
34. Jacob C., Holme A.L., and Fry F.H. The sulfinic acid switch in proteins. Org. Biomol. Chem. 2 (2004) 1953-1956
35. Stirpe A., Sportelli L., and Guzzi R. A comparative investigation of the thermal unfolding of pseudoazurin in the Cu(II)-holo and apo form. Biopolymers 83 (2006) 487-497
36. Espina M., Ausar S.F., Middaugh R., Picking W.D., and Picking W.L. Spectroscopic and calorimetric analyses of invasion plasmid antigen D (IpaD) from Shigella flexneri reveal the presence of two structural domains. Biochemistry 45 (2006) 9219-9227
37. Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biochemistry (Moscow) 63 (1998) 276-284
38. Privalov P.L. Physical basis of the stability of the folded conformations of proteins. In: Creighton T.E. (Ed). Protein Folding (1992), W. H. Freeman and Co, New York 83-126
39. Freire E. The thermodynamic linkage between protein structure, stability and function. Methods in Mol. Biol. 168 (2001) 37-68
40. Murphy P.K., and Gill S.J. Solid model compounds and the thermodynamics of protein folding. J. Mol. Biol. 22 (1991) 699-709
41. Milardi D., La Rosa C., Fasone S., and Grasso D. An alternative approach in the structure-based prediction of the thermodynamics of protein unfolding. Biophys. Chem. 69 (1997) 43-51