2-Oxoquinoline 8-monooxygenase oxygenase component: Active site modulation by Rieske-[2Fe-2S] center oxidation/reduction

Structure

Volumn 13, Issue 5, 2005, Pages 817-824

  Martins, Berta Maria ^a   Svetlitchnaia, Tatiana ^a   Dobbek, Holger ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOQUINOLINE 8 MONOOXYGENASE; HISTIDINE; IRON; IRON SULFUR PROTEIN; MONOMER; OXYGEN; OXYGENASE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; SOIL MICROFLORA;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT COMPLEX III; IRON-SULFUR PROTEINS; MIXED FUNCTION OXYGENASES; OXIDATION-REDUCTION; OXYGEN; PROTEIN CONFORMATION; PSEUDOMONAS PUTIDA;

BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 18944405592     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.03.008     Document Type: Article

References (31)

1. Z.M. Beharry, D.M. Eby, E.D. Coulter, R. Viswanathan, E.L. Neidle, R.S. Phillips, and D.M. Kurtz Jr. Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase Biochemistry 42 2003 13625 13636
2. I. Bonin, B.M. Martins, V. Puranov, S. Fetzner, R. Huber, and H. Dobbek Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase Structure 12 2004 1425 1435
3. A.T. Brünger, P.D. Adams, G.M. Clore, W.L. Delano, P. Gros, R.W. Grosse Kunstleve, J.S. Jiang, J. Kuszewski, M. Nilges, and N.S. Pannu Crystallography and NMR system: a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54 1998 905 921
4. E. Carredano, A. Karlsson, B. Kauppi, D. Choudhury, R.E. Parales, J.V. Parales, K. Lee, D.T. Gibson, H. Eklund, and S. Ramaswamy Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding J. Mol. Biol. 296 2000 701 712
5. CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
6. N.J. Cosper, D.M. Eby, A. Kounosu, N. Kurosawa, E.L. Neidle, D.M. Kurtz Jr., T. Iwasaki, and R.A. Scott Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters Protein Sci. 11 2002 2969 2973
7. E. De La Fortelle, J.J. Irwin, and G. Bricogne SHARP: a maximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods Crystallographic Computing 7 1997 1 9
8. W.L. DeLano The PyMOL User's Manual 2002 DeLano Scientific San Carlos, CA
9. R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comp. Chem. 19 1998 319 333
10. D.T. Gibson, and R.E. Parales Aromatic hydrocarbon dioxygenases in environmental biotechnology Curr. Opin. Biotechnol. 11 2000 236 243
11. H.Y. Jiang, R.E. Parales, N.A. Lynch, and D.T. Gibson Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites J. Bacteriol. 178 1996 3133 3139
12. A. Karlsson, J.V. Parales, R.E. Parales, D.T. Gibson, H. Eklund, and S. Ramaswamy The reduction of the Rieske iron-sulfur cluster in naphthalene dioxygenase by X-rays J. Inorg. Biochem. 78 2000 83 87
13. A. Karlsson, J.V. Parales, R.E. Parales, D.T. Gibson, H. Eklund, and S. Ramaswamy Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron Science 299 2003 1039 1042
14. B. Kauppi, K. Lee, E. Carredano, R.E. Parales, D.T. Gibson, H. Eklund, and S. Ramaswamy Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase Structure 6 1998 571 586
15. G.J. Kleywegt, and R.J. Read Not your average density Structure 5 1997 1557 1569
16. a values of Rieske iron-sulfur proteins Biochemistry 43 2004 12383 12389
17. S.J. Lange, and L. Que Jr. Oxygen activating nonheme iron enzymes Curr. Opin. Chem. Biol. 2 1998 159 172
18. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26 1993 283 291
19. R.E. Parales, J.V. Parales, and D.T. Gibson Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity J. Bacteriol. 181 1999 1831 1837
20. L. Que Jr., and R.Y. Ho Dioxygen activation by enzymes with mononuclear non-heme iron active sites Chem. Rev. 96 1996 2607 2624
21. B. Rosche, S. Fetzner, F. Lingens, W. Nitschke, and A. Riedel The 2Fe2S centres of the 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy Biochim. Biophys. Acta 1252 1995 177 179
22. B. Rosche, B. Tshisuaka, S. Fetzner, and F. Lingens 2-Oxo-1,2- dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 86 J. Biol. Chem. 270 1995 17836 17842
23. B. Tshisuaka, R. Kappl, J. Huttermann, and F. Lingens Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy Biochemistry 32 1993 12928 12934
24. D. Turk Weiterentwicklung eines Programms für Molekülgraphik und Elektronendichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklärungen 1992 TU München. Munich, Germany
25. G.M. Ullmann, L. Noodleman, and D.A. Case Density functional calculation of p K(a) values and redox potentials in the bovine Rieske iron-sulfur protein J. Biol. Inorg. Chem. 7 2002 632 639
26. M.D. Wolfe, J.V. Parales, D.T. Gibson, and J.D. Lipscomb Single turnover chemistry and regulation of O-2 activation by the oxygenase component of naphthalene 1,2-dioxygenase J. Biol. Chem. 276 2001 1945 1953
27. M.D. Wolfe, D.J. Altier, A. Stubna, C.V. Popescu, E. Munck, and J.D. Lipscomb Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase Biochemistry 41 2002 9611 9626
28. T.C. Yang, M.D. Wolfe, M.B. Neibergall, Y. Mekmouche, J.D. Lipscomb, and B.M. Hoffman Modulation of substrate binding to naphthalene 1,2-dioxygenase by Rieske cluster reduction/oxidation J. Am. Chem. Soc. 125 2003 2034 2035
29. T.C. Yang, M.D. Wolfe, M.B. Neibergall, Y. Mekmouche, J.D. Lipscomb, and B.M. Hoffman Substrate binding to NO-ferro-naphthalene 1,2-dioxygenase studied by high-resolution Q-band pulsed H-2-ENDOR spectroscopy J. Am. Chem. Soc. 125 2003 7056 7066
30. Y. Zu, J.A. Fee, and J. Hirst Complete thermodynamic characterization of reduction and protonation of the bc(1)-type Rieske [2Fe-2S] center of Thermus thermophilus J. Am. Chem. Soc. 123 2001 9906 9907
31. Y. Zu, M.M. Couture, D.R. Kolling, A.R. Crofts, L.D. Eltis, J.A. Fee, and J. Hirst Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state Biochemistry 42 2003 12400 12408