Spectroscopic investigations to reveal the nature of interactions between the haem protein myoglobin and the dye rhodamine 6G

Luminescence

Volumn 27, Issue 4, 2012, Pages 285-291

  Mandal, Paulami ^a   Bardhan, Munmun ^a   Ganguly, Tapan ^a  

^a DEPARTMENT OF MATERIALS SCIENCE   (India)

Author keywords

circular dichroism; hydrogen bonding; myoglobin; rhodamine6G; static fluorescence quenching; van der Waals' force

Indexed keywords

BINDING ENERGY; BINDING SITES; DIAGNOSIS; DICHROISM; ENERGY TRANSFER; FLUORESCENCE QUENCHING; GROUND STATE; HYDROGEN; PROTEINS; VAN DER WAALS FORCES;

FLUORESCENCE QUENCHING; MYOGLOBIN; RHODAMINE; RHODAMINE 6G; SPECTROSCOPIC INVESTIGATIONS; STATIC FLUORESCENCE QUENCHING; STEADY STATE; THERMODYNAMIC PARAMETER; TIME-RESOLVED FLUORESCENCE; VAN DER WAALS' FORCES;

HYDROGEN BONDS;

FLUORESCENT DYE; MYOGLOBIN; RHODAMINE; RHODAMINE 6G;

ARTICLE; CHEMISTRY; EVALUATION; KINETICS; METHODOLOGY; PROTEIN BINDING; SPECTROSCOPY;

FLUORESCENT DYES; KINETICS; MYOGLOBIN; PROTEIN BINDING; RHODAMINES; SPECTRUM ANALYSIS;

EID: 84865071595     PISSN: 15227235     EISSN: 15227243     Source Type: Journal    
DOI: 10.1002/bio.1348     Document Type: Article

References (47)

1. Keener J, Sneyd J,. Mathematical physiology. New York: Springer, 1998.
2. Boyer R,. Interactive concepts in biochemistry. Chichester: Wiley, 2002; sections 4.5 and 5.5.
3. Rosette M, Malone R,. Bioinorganic chemistry: a short course. New York: Wiley, 2002; 348.
4. Bordbar AK, Mooasavi-Movahedi AA,. Binding data analysis of the interaction bovine hemoglobin with dodecyltrimethylammonium bromide. Bull Chem Soc Japan 1996; 69: 2231-4.
5. Mooasavi-Movahedi AA, Jones MN, Plicher G,. Thermodynamics of the interaction of sodium n-dodecyl sulphate with Aspergillus niger catalase in low ionic strength aqueous solutions. Int J Biol Macromol 1988; 10: 75-8.
6. Nizomov N, Ismailov ZF, Kurtaliev AN, Nizamov SN, Khodzhaev G, Patsenker LD,. Luminescent spectral properties of rohdamine derivatives while binding to serum albumin. J Appl Spec 2006; 73: 432-6.
7. Jisha VS, Arun KT, Hariharan M, Ramaiah D,. Site-selective interactions: squaraine dye-serum albumin complexes with enhanced fluorescence and triplet yields. J Phys Chem B 2010; 11: 5912-19.
8. Varlan A, Hillebrand M,. Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy. Molecules 2010; 15: 3905-19.
9. Vaiana AC, Neuweiler H, Schulz A, Wolfrum J, Sauer M, Smith JC,. Fluorescence quenching of dyes by tryptophan: interactions at atomic detail from combination of experiment and computer simulation. J Am Chem Soc 2003; 125: 14564-72.
10. (a), Jones G, Lu LN, Vullev V, Gosztola DJ, Greenfield SR, Wasielewski MR,. Photoinduced electron transfer for pyrenesulfonamide conjugates of tryptophan-containing peptides. Mitigation of fluoroprobe behavior in N-terminal labeling experiments. Bioor Med Chem Lett 1995; 5 (20): 2385-90.
11. Tatikolov AS, Costa SMB,. Energy transfer and fluorescence quenching in complexes of polymethine dyes with human serum albumin. Photochem Photobiol 2004; 80: 250-56.
12. Neuweiler H, Schulz A, Vaiana AC, Smith JC, Kaul S, Wolfrum J, Sauer M,. Detection of individual p53-autoantibodies by using quenched peptide-based molecular probes. Angew Chem Int Ed 2002; 41: 4769-73.
13. Knemeyer JP, Marme N, Sauer M,. Probes for detection of specific DNA sequences at the single-molecule level. Anal Chem 2000; 72: 3717-24.
14. Neuweiler H, Böhmer M, Enderlein J, Sauer M,. Measurement of submicrosecond intramolecular contact formation in peptides at the single-molecule level. J Am Chem Soc 2003; 125: 5324-30.
15. Brown JP, Roehm GW, Brown RJ,. Mutagenicity testing of certified food colors and related azo, xanthene and triphenylmethane dyes with the Salmonella/microsome system. Mutat Res 1978; 56: 249-71.
16. International Agency for Research on Cancer. Rhodamine B. IARC Monogr. 1978; 16: 221.
17. Magde D, Rojas GE, Seybold PG,. Solvent dependence of the fluorescence lifetimes of xanthene dyes. Photochem Photobiol 1999; 70: 737-44.
18. Mandal P, Bardhan M, Ganguly T,. A detailed spectroscopic study on the interaction of rhodamine 6 G with human hemoglobin. J Photochem Photobiol B Biol 2010; 99: 78-86.
19. Parker CA,. Photoluminescence of solutions. New York: Elsevier, New York, 1968; 220.
20. Sinha S, De R, Ganguly T,. Investigations of excited state quenching reactions between p-toluidine, its N,N-dimethyl derivative and the acceptor dimethylterephthalate at different temperatures. J Photochem Photobiol A Chem 1998; 112: 13-20.
21. Stern O, Volmer M,. On the quenching-time of fluorescence. Phys Z 1919; 20: 183-8.
22. Bevington PR,. Data reduction error analysis for the physical sciences. New York: McGraw-Hill, 1969.
23. Lakowicz JR,. Principles of fluorescence spectroscopy, 2nd edn. New York: Plenum, 1999; 242.
24. Albani JR,. Structure and dynamics of macromolecules: absorption and fluorescence studies. Amsterdam, The Netherlands: Elsevier, 2004; 154.
25. Maruthamuthu M, Selvakumar G,. Selective quenching of tryptophanyl fluorescence in bovine serum albumin by the iodide ion. Proc Indian Acad Sci Chem Sci 1996; 107: 79-86.
26. 2+ antagonist, to serum albumin: A Fluorescence study. J Pharm Sci 1994; 83: 674-6.
27. Lehrer SS,. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 1971; 10: 3254-63.
28. Saikh SMT, Seetharamappa J, Kandagal PB, Manjunatha DH, Ashoka S,. Spectroscopic investigations on the mechanism of interaction of bioactive dye with bovine serum albumin. Dyes Pigments 2007; 74: 665-71.
29. Liu JQ, Tian JN, Zhang JY,. Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study. Anal Bioanal Chem 2003; 376: 864-7.
30. Tian JN, Liu JQ, Zhang JY,. Fluorescence studies on the interactions of barbaloin with bovine serum albumin. Chem Pharm Bull 2003; 51: 579-82.
31. Marty A, Boiret M, Deumie M,. How to illustrate ligand-protein binding in a class experiment. J Chem Educ 1986; 63: 365-6.
32. Gao H, Lei L, Qin K, Chen X, Hu Z,. The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectroscopic methods. J Photochem Photobiol A 2004; 167: 213-21.
33. Hu YJ, Liu Y, Shen XS, Fang XY, Qu SS,. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Mol Struct 2005; 738: 143-7.
34. Ross PD, Subramanian S,. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981; 20: 3096-102.
35. Tian JN, Liu JQ, He WY, Hu ZD, Yao XJ, Chen XG,. Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules 2004; 5: 1956-61.
36. Tofani L, Feis A, Snoke RE, Berti D, Baglioni P, Smulevich G,. Spectroscopic and interfacial properties of myoglobin/surfactant complexes. Biophys J 2004; 87: 186-95.
37. Song S, Hou X, Wu Y, Shang S, Yang C, Inoue Y, Dong C,. Study on the interaction between methyl blue and human serum albumin by fluorescence spectrometry. J Lumin 2009; 129: 169-75.
38. Bi S, Song D, Tian Y,. Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochim Acta A Mol Biomol Spectrosc 2005; 61: 629-36.
39. He W, Li Y, Xue C, Chen X, Sheng F,. Effect of Chinese medicine alpinetin on the structure of human serum albumin. Bioorg Med Chem 2005; 13: 1837-45.
40. Valeur B,. Molecular fluorescence: principles and applications. New York: Wiley, 2001.
41. Shrivastava HY, Kanthimathi M, Nair BU,. Interaction of Schiff base with bovine serum albumin: site-specific photocleavage. Biochem Biophys Res Commun 1999; 265: 311-14.
42. Kamat BP, Seetharamappa J,. Mechanism of interaction of vincristine sulphate and rifampicin with bovine serum albumin: a spectroscopic study. J Chem Sci 2005; 117: 649-55.
43. Li R, Nagai Y, Nagai M,. Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near- and far-UV circular dichroism of isolated chains and recombined hemoglobin. J Inorg Biochem 2000; 82: 93-101.
44. Jin Y, Sakurai H, Nagai Y, Nagai M,. Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding: a study of mutants at α42, α140, β145 tyrosine or β37 tryptophan. Biopolymers 2004; 74: 60-63.
45. Perutz MF, Ladner JE, Simon SR, Ho C,. Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry 1974; 13: 2163-73.
46. Shimizu H, Kaito A, Hatano M,. Induced circular dichroism of β-cyclodextrin complexes with azanaphthalenes-polarization directions of the π π transitions in azanaphthalenes. J Am Chem Soc 1982; 104: 7059-65.
47. 19 F-NMR and induced CD spectral studies. FEBS Lett 1983; 160: 182-6.