Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb

Biophysical Journal

Volumn 95, Issue 7, 2008, Pages 3419-3428

  Jensen, Karina Tveen ^a   Strambini, Giovanni ^b   Gonnelli, Margherita ^b   Broos, Jaap ^c   Jackson, J Baz ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b CNR Consiglio Nazionale delle Ricerche   (Italy)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; ENZYMOLOGY; FLUORESCENCE; GENETICS; METABOLISM; MUTATION; RHODOSPIRILLUM RUBRUM; SPECTROFLUOROMETRY; TIME;

AMINO ACID SUBSTITUTION; FLUORESCENCE; MUTANT PROTEINS; MUTATION; NADP TRANSHYDROGENASE; RHODOSPIRILLUM RUBRUM; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; TRYPTOPHAN;

EID: 55949123441     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.134650     Document Type: Article

References (39)

1. b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278:113-150.
2. Fender, B. J., K. W. Short, D. K. Hahn, and P. K. Callis. 1999. Vibrational assignments for indole with the aid of phosphorescence spectra. Int. J. Quantum Chem. 72:347-356.
3. Vivian, J. T., and P. R. Callis. 2001. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80:2093-2109.
4. Scott, T. W., B. F. Cambell, R. L. Cone, and J. M. Friedman. 1989. Line narrowing and site selectivity in tryptophan fluorescence from proteins and glasses: cryogenic studies of conformational disorder and dynamics. Chem. Phys. 131:63-79.
5. 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.
6. Hansen, J. E., J. W. Longworth, and G. R. Fleming. 1990. Photophysics of metalloazurins. Biochemistry. 29:7329-7338.
7. Strambini, G. B., and E. Gabellieri. 1991. Phosphorescence from Trp-48 in azurin: influence of Cu(II), Cu(I), Ag(I) and Cd(II) at the coordination site. J. Phys. Chem. 95:4352-4356.
8. Jackson, J. B. 2003. Proton translocation by transhydrogenase. FEBS Lett. 545:18-24.
9. Jackson, J. B., S. A. White, T. H. C. Brondijk, and M. Wikstrom. 2005. Hydride transfer and proton translocation by nicotinamide nucleotide transhydrogenase. In Biophysical and Structural Aspects of Bioenergetics. Royal Society of Chemistry, Cambridge, United Kingdom. 376-393.
10. Diggle, C., M. Hutton, G. R. Jones, C. M. Thomas, and J. B. Jackson. 1995. Properties of the soluble polypeptide of the proton-translocating transhydrogenase from Rhodospirillum rubrum obtained by expression in Escherichia coli. Eur. J. Biochem. 228:719-726.
11. 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.
12. Mei, G., G. Gilardi, M. Venazi, N. Rosato, G. W. Canters, and A. Finazzi Agro. 1996. Probing the structure and mobility of Pseudomonas aeruginosa azurin by circular dichroismand dynamic fluorescence anisotropy. Protein Sci. 5:2248-2254.
13. Eftink, M. R. 1991. Fluorescence techniques for studying protein structure. Methods Biochem. Anal. 35:127-205.
14. Lakowicz, J. R. 1999. Principles of Fluorescence Spectroscopy. Kluwer Academic Publishers, New York.
15. Broos, J., K. Tveen-Jensen, E. de Waal, B. H. Hesp, J. B. Jackson, G. W. Canters, and P. R. Callis. 2007. The emitting state of tryptophan in proteins with highly blue-shifted fluorescence. Angew. Chem. Int. Ed. 46:5137-5139.
16. Barik, S. 1995. Site-directed mutagenesis by double polymerase chain reaction. Mol. Biotechnol. 3:1-7.
17. van Boxel, G. I., P. Quirk, N. J. P. Cotton, S. A. White, and J. B. Jackson. 2003. Glutamine-132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer. Biochemistry. 42:1217-1226.
18. Obiozo, U. M., T. H. C. Brondijk, A. J. White, G. I. van Boxel, T. R. Dafforn, S. A. White, and J. B. Jackson. 2007. Substitution of tyrosine-146 in the dI component of proton-translocating transhydrogenase leads to reversible dissociation of the active dimer into inactive monomers. J. Biol. Chem. 282:36434-36443.
19. Diggle, C., T. Bizouarn, N. P. J. Cotton, and J. B. Jackson. 1996. Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum. Eur. J. Biochem. 241:162-170.
20. Mejbaum-Katzenellenbogen, S., and W. J. Drobryszycka. 1959. New methods for quantitative determination of serum proteins separated by paper chromatography. Clin. Chem. Acta. 4:515-522.
21. Karlsson, B. G., T. Pascher, M. Nordling, R. H. Arvidsson, and L. G. Lundberg. 1989. Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli. FEBS Lett. 246:211-217.
22. Sandberg, A., J. Leckner, and B. G. Karlsson. 2004. Apo-azurin folds via an intermediate that resembles the molten globule. Protein Sci. 13:2628-2638.
23. Venning, J. D., D. J. Rodrigues, C. J. Weston, N. P. J. Cotton, P. G. Quirk, N. Errington, S. Finet, S. A. White, and J. B. Jackson. 2001. The heterotrimer of the membrane-peripheral components of transhydrogenase and the alternating-site mechanism of proton translocation. J. Biol. Chem. 276:30678-30685.
24. D'Auria, S., A. Varriale, M. Gonnelli, M. Saviano, M. Staiano, M. Rossi, and G. B. Strambini. 2007. Tryptophan fluorescence studies of the D-galactose/D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamic features of the protein. J. Proteome Res. 6:1306-1312.
25. Strambini, G. B., B. A. Kerwin, B. D. Mason, and M. Gonelli. 2004. The triplet-state lifetime of indole derivatives in aqueous solution. Photochem. Photobiol. 80:462-470.
26. Yamamoto, Y., and J. Tanaka. 1972. Polarized absorption spectra of crystals of indole and its related compounds. Bull. Chem. Soc. Jpn. 65:1362-1366.
27. b excitation bands. Photochem. Photobiol. 25:441-444.
28. Finazzi Agro, A., C. Giovagnoli, L. Avigliano, G. Rotilio, and V. Mondovi. 1973. Environment of copper in Pseudomonas fluorescens azurin: fluorimetric approach. Eur. J. Biochem. 34:20-24.
29. a fluorescence from jet-cooled 3-methylindole-polar solvent complexes. J. Chem. Phys. 113:5235-5244.
30. Broos, J., E. Gabellieri, G. I. van Boxel, J. B. Jackson, and G. B. Strambini. 2003. Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core. J. Biol. Chem. 278:47578-47584.
31. Gonnelli, M., and G. B. Strambini. 2005. Intramolecular quenching of tryptophan phosphorescence in short peptides and proteins. Photochem. Photobiol. 81:614-622.
32. Strambini, G. B., and M. Gonelli. 1995. Tryptophan phosphorescence in fluid solution. J. Am. Chem. Soc. 117:7646-7651.
33. b coupling in the excited state of 3-methyl indole and its polar clusters. J. Phys. Chem. 98:12834-12843.
34. Carney, J. R., and T. S. Zwier. 1999. Infrared and ultraviolet spectroscopy of water-containing clusters of indole, 1-methylindole and 3-methylindole. J. Phys. Chem. 103:9943-9957.
35. Gregoret, L. M., S. D. Rader, R. J. Fletterick, and F. E. Cohen. 1991. Hydrogen bonds involving sulfur atoms in proteins. Proteins. 9:99-107.
36. Purkey, R. M., and W. C. Galley. 1970. Phosphorescence studies of environmental heterogeneity for tryptophyl residues in proteins. Biochemistry. 9:3569-3575.
37. Hershberger, M. V., A. H. Maki, and W. C. Galley. 1980. Phosphorescence and optically detected magnetic resonance studies of a class of anomalous tryptophan residues in globular proteins. Biochemistry. 19:2204-2209.
38. Zscherp, C., and A. Barth. 2001. What vibrations tell us about proteins. Q. Rev. Biophys. 35:369-430.
39. Callis, P. R., J. T. Vivian, and L. S. Slater. 1995. Ab initio calculations of vibronic spectra for indole. Chem. Phys. Lett. 244:53-58.