Implication of a critical residue (Glu175) in structure and function of bacterial luciferase

FEBS Letters

Volumn 579, Issue 21, 2005, Pages 4701-4706

  Madvar, Ali Riahi ^a   Hosseinkhani, Saman ^a   Khajeh, Khosro ^a   Ranjbar, Bijan ^a   Asoodeh, Ahmad ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

8 Anilino 1 naphthalene sulphonic acid; Bacterial luciferase; Circular dichroism; Decay rate; Fluorescence quenching; Intrinsic fluorescence; Random mutagenesis

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; BACTERIAL ENZYME; GLUTAMIC ACID; LUCIFERASE; TRYPTOPHAN;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; EXPOSURE; FLUORESCENCE; HYDROPHOBICITY; LUMINESCENCE; MUTAGENESIS; MUTATION; NONHUMAN; PHOTORHABDUS LUMINESCENS; PRIORITY JOURNAL; RANDOMIZATION; TURNOVER TIME; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CIRCULAR DICHROISM; GLUTAMIC ACID; LUCIFERASES, BACTERIAL; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY;

PHOTORHABDUS LUMINESCENS;

EID: 24044451239     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.07.040     Document Type: Article

References (26)

1. J.W. Hastings, and Q.H. Gibson Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide J. Biol. Chem. 238 1963 2537 2554
2. Q.H. Gibson, and J.W. Hastings The oxidation of reduced flavin mononucleotide by molecular oxygen J. Biochem. 83 1962 368 377
3. A.J. Fisher, T.B. Thopmpson, J.B. Thoden, T.O. Baldwin, and I. Rayment The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions J. Biol. Chem. 271 1996 21956 21968
4. N.K. AbouKhair, M.M. Ziegler, and T.O. Baldwin Bacterial luciferase: demonstration of a catalytically competent altered conformational state following a single turnover Biochemistry 24 1985 3942 3947
5. K.H. Nealson Isolation, identification and manipulation of luminos bacteria Methods Enzymol. 57 1978 153 166
6. K.H. Nealson, and J.W. Hastings Bacterial bioluminescence: its control and ecological significance Microbiol. Rev. 43 1979 496 518
7. R. Szittner, and E. Meighen Nucleotide sequence, expression, and properties of luciferase coded by lux genes from a terrestrial bacterium J. Biol. Chem. 265 1990 16581 16587
8. E.A. Meighen, and J.W. Hastings Binding site determination from kinetic data. Reduced flavin mononucleotide binding to bacterial luciferase J. Biol. Chem. 246 1971 7666 7674
9. T.W. Cline, and J.W. Hastings Mutated luciferases with altered bioluminescence emission spectra J. Biol. Chem. 249 1974 4668 4669
10. N. Valkova, R. Szittner, and E.A. Meighen Control of luminescence decay and flavin binding by the LuxA carboxyl-terminal regions in chimaeric bacterial luciferases Biochemistry 38 1999 13820 13828
11. S. Hosseinkhani, R. Szittner, and E. Meighen Random mutagenesis of bacterial luciferase: critical role of Glu175 in control of luminescence decay Biochem. J. 385 2005 575 580
12. L.Y. Lin, T. Sulea, R. Szittner, V. Vassilyev, E.O. Purisima, and E. Meighen Modeling of bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data Protein Sci. 10 2001 1563 1571
13. Z. Li, and E.A. Meighen Trytophan 250 on the α subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W → Y mutations on catalytic function J. Biol. Chem. 34 1995 15084 15090
14. A.J. Fisher, F.M. Raushel, T.O. Baldwin, and I. Rayment Three dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution Biochemistry 34 1995 6581 6586
15. A. Gunsalus-Miguel, E.A. Meighen, M.Z. Nicoli, K.H. Nealson, and J.W. Hastings Purification and properties of bacterial luciferases J. Biol. Chem. 247 1972 398 404
16. M.M. Bradford A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
17. S. Hosseinkhani, B. Ranjbar, H. Naderi-Manesh, and M. Nemat-Gorgani Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure FEBS Lett. 561 2004 213 216
18. M.R. Eftink, and C.A. Ghiron Exposure of tryptophanyl residues and protein dynamics Biochemistry 16 1977 5546 5551
19. N. Wellner, P.S. Belton, and A.S. Tatham Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of ω-gliadins Biochem. J. 319 1996 741 747
20. I. Protasevich, B. Ranjbar, V. Lobachov, A. Markov, D. Gilli, D. Briand, J. Lafitte, and R. Haiech Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutation Biochemistry 36 1997 2017 2024
21. S. Hosseinkhani, R. Szittner, M. Nemat-Gorgani, and E.A. Meighen Adsorptive immobilization of bacterial luciferase on alkyl-substituted Sepharose 4B Enzyme Microb. Technol. 32 2003 186 193
22. S.D. Amico, J.C. Marx, C. Gerday, and G. Feller Activity-stability relationships in extremophilic enzymes J. Biol. Chem. 278 2003 7891 7896
23. Z. Li, and E.A. Meighen Steady-state fluorescence and phosphorescence spectroscopic studies of bacterial luciferase tryptophan mutants J. Fluoresc. 4 1994 209 216
24. X. Xu, Q. Liu, Y. Liu, and Y. Xie Terbium (III) fluorescence probe studies on metal ion-binding sites in anticoagulation factor I from Agkistrodon acutus venom J. Protein. Chem. 21 2002 123 129
25. K. Boren, P. Anderson, M. Larsson, and U. Carlsson Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum Biochim. Biophys. Acta 1430 1999 111 118
26. 8 barrel structure of the bacterial luciferase α subunit Biochemistry 40 2001 15436 15443