The "bridging" aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron(II)-mononuclear center

Biochemistry

Volumn 45, Issue 34, 2006, Pages 10208-10216

  Tarasev, Michael ^a   Pinto, Alex ^a   Kim, Duke ^b   Elliott, Sean J ^b   Ballou, David P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b Boston University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CATALYST ACTIVITY; NITROGEN OXIDES; OXIDATION; SOLVENTS;

AEROBIC BREAKDOWN; ELECTRON TRANSFER; PHTHALATE DIOXYGENASE (PDO); RIESKE DIOXYGENASES;

ENZYMES;

ASPARTIC ACID; DIOXYGENASE; IRON; IRON SULFUR PROTEIN; METAL; NITRIC OXIDE; OXIDOREDUCTASE; PHTHALIC ACID; RECOMBINANT ENZYME;

ABSORPTION SPECTROSCOPY; AEROBIC METABOLISM; ARTICLE; BURKHOLDERIA CEPACIA; CHEMICAL STRUCTURE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; NONHUMAN; PLASMID; POTENTIOMETRY; PRIORITY JOURNAL; STEADY STATE;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; BURKHOLDERIA CEPACIA; IRON; MODELS, MOLECULAR; NITRIC OXIDE; OXIDATION-REDUCTION; OXYGENASES; PHTHALIC ACIDS; PROTEIN BINDING;

EID: 33748635618     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060219b     Document Type: Article

References (28)

1. Pinto, A., Tarasev, M., and Ballou, D. P. (2006) Substitutions of the "bridging" aspartate 178 result in the profound changes in the reactivity of the Rieske center of phthalate dioxygenase, Biochemistry (in press).
2. Kauppi, B., Lee, K., Carredano, E., Parales, R. E., Gibson, D. T., Eklund, H., and Ramaswamy, S. (1998) Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase, Structure 6, 571-586.
3. Moser, C. C., Keske, J. M., Warncke, K., Farid, R. S., and Dutton, P. L. (1992) Nature of biological electron transfer, Nature 355, 796-802.
4. Furusawa, Y., Nagarajan, V., Tanokura, M., Masai, E., Fukuda, M., and Senda, T. (2004) Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1, J. Mol. Biol. 342, 1041-1052.
5. Friemann, R., Ivkovic-Jensen, M. M., Lessner, D. J., Yu, C. L., Gibson, D. T., Parales, R. E., Eklund, H., and Ramaswamy, S. (2005) Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase, J. Mol. Biol. 348, 1139-1151.
6. Nojiri, H., Ashikawa, Y., Noguchi, H., Nam, J. W., Urata, M., Fujimoto, Z., Uchimura, H., Terada, T., Nakamura, S., Shimizu, K., Yoshida, T., Habe, H., and Omori, T. (2005) Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase, J. Mol. Biol. 351, 355-370.
7. Dong, X., Fushinobu, S., Fukuda, E., Terada, T., Nakamura, S., Shimizu, K., Nojiri, H., Omori, T., Shoun, H., and Wakagi, T. (2005) Crystal structure of the terminal oxygenase component of cumene dioxygenase from Pseudomonas fluorescens IP01, J. Bacteriol. 187, 2483-2490.
8. Martins, B. M., Svetlitchnaia, T., and Dobbek, H. (2005) 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction, Structure (Cambridge) 13, 817-824.
9. 2 activation by the oxygenase component of naphthalene 1,2-dioxygenase, J. Biol. Chem. 276, 1945-1953.
10. 2H-ENDOR spectroscopy, J. Am. Chem. Soc. 125, 7056-7066.
11. Tarasev, M., and Ballou, D. P. (2005) Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase, Biochemistry 44, 6197-6207.
12. Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., and Ramaswamy, S. (2003) Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron, Science 299, 1039-1042.
13. Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., and Ramaswamy, S. (2005) NO binding to naphthalene dioxygenase, J. Biol. Inorg. Chem. 10, 483-489.
14. Tarasev, M., Rhames, F., and Ballou, D. P. (2004) Rates of the phthalate dioxygenase reaction with oxygen are dramatically increased by interactions with phthalate and phthalate oxygenase reductase, Biochemistry 43, 12799-12808.
15. Gassner, G. T., Ballou, D. P., Landrum, G. A., and Whittaker, J. W. (1993) Magnetic circular dichroism studies on the mononuclear ferrous active site of phthalate dioxygenase from Pseudomonas cepacia show a change of ligation state on substrate binding, Biochemistry 32, 4820-4825.
16. Pavel, E. G., Martins, L. J., Ellis, W. R. J., and Solomon, E. I. (1994) Magnetic circular dichroism studies of exogenous ligand and substrate binding to the non-heme ferrous active site in phthalate dioxygenase, Chem. Biol. 1, 173-183.
17. Bertini, I., Luchinat, C., Mincione, G., Parigi, G., Gassner, G. T., and Ballou, D. P. (1996) NMRD studies on phthalate dioxygenase: evidence for displacement of water on binding substrate, J. Biol. Inorg. Chem., 468-475.
18. Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., and Ramaswamy, S. (2000) The reduction of the Rieske iron-sulfur cluster in naphthalene dioxygenase by X-rays, J. Inorg. Biochem. 78, 83-87.
19. Parales, R. E., Parales, J. V., and Gibson, D. T. (1999) Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity, J. Bacteriol. 181, 1831-1837.
20. Beharry, Z. M., Eby, D. M., Coulter, E. D., Viswanathan, R., Neidle, E. L., Phillips, R. S., and Kurtz, D. M., Jr. (2003) Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase, Biochemistry 42, 13625-13636.
21. Jiang, H., Parales, R. E., Lynch, N. A., and Gibson, D. T. (1996) Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites, J. Bacteriol. 178, 3133-3139.
22. Bevington, P. R. (1996) in Data Reduction and Error Analysis for the Physical Sciences, pp 235-242, McGraw-Hill, New York.
23. Kuila, D., and Fee, J. A. (1986) Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein, J. Biol. Chem. 261, 2768-2771.
24. Yang, T. C., Wolfe, M. D., Neibergall, M. B., Mekmouche, Y., Lipscomb, J. D., and Hoffman, B. M. (2003) Modulation of substrate binding to naphthalene 1,2-dioxygenase by rieske cluster reduction/oxidation, J. Am. Chem. Soc. 125, 2034-2035.
25. Orville, A. M., and Lipscomb, J. D. (1997) Cyanide and nitric oxide binding to reduced protocatechuate 3,4-dioxygenase: insight into the basis for order-dependent ligand binding by intradiol catecholic dioxygenases, Biochemistry 36, 14044-14055.
26. 2+ environment, J. Biol. Chem. 258, 14981-14991.
27. 2+ oxidase with metal coordination sites for small molecules and substrate, J. Biol. Chem. 264, 21677-21681.
28. Wolfe, M. D., Altier, D. J., Stubna, A., Popescu, C. V., Munck, E., and Lipscomb, J. D. (2002) Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase, Biochemistry 41, 9611-9626.