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Bibliography on structural studies of intradiol aromatic­ring­cleavage dioxygenases

  1. Benvenuti, M., Briganti, F., Scozzafava, A., Golovleva, L., Travkin, V.M. and Mangani, S. (1999) Crystallization and preliminary crystallographic analysis of the hydroxyquinol 1,2­dioxygenase from Nocardioides simplex 3E: a novel dioxygenase involved in the biodegradation of polychlorinated aromatic compounds. Acta Crystallogr. D55, 901-903.
  2. Broderick, J.B. and O'Halloran, T.V. (1991) Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non­heme iron dioxygenase with broad substrate tolerance. Biochemistry 30, 7349-7358.
  3. Broderick, J.B., Natan, M.J., O'Halloran, T.V. and van Duyne, R.P. (1993) Evidence for retention of biological activity of a non­heme iron enzyme adsorbed on a silver colloid: A surface­enhanced resonance Raman scattering study. Biochemistry 32, 13771-13776.
  4. Bull, C. and Ballou, D.P. (1981) Purification and properties of protocatechuate 3,4­dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry. J. Biol. Chem. 256, 12673-12680.
  5. Bull, C., Ballou, D.P. and Otsuka, S. (1981) The reaction of oxygen with protocatechuate 3,4­dioxygenase from Pseudomonas putida. Characterization of a new oxygenated intermediate. J. Biol. Chem. 256, 12681-12686.
  6. Earhart, C.A., Radhakrishnan, R., Orville, A.M., Lipscomb, J.D. and Ohlendorf, D.H. (1994a) Preliminary crystallographic study of protocatechuate 3,4­dioxygenase from Brevibacterium fuscum. J. Mol. Biol. 236, 374-376.
  7. Earhart, C.A., Hall, M.D., Michaud­Soret, I., Que, L., Jr. and Ohlendorf, D.H. (1994b) Crystallization of catechol­1,2 dioxygenase from Pseudomonas arvilla C­1. J. Mol. Biol. 236, 377-378.
  8. Elgren, T.E., Orville, A.M., Kelly, K.A., Lipscomb, J.D., Ohlendorf, D.H. and Que, L., Jr. (1997) Crystal structure and resonance Raman studies of protocatechuate 3,4­dioxygenase complexed with 3,4­dihydroxyphenylacetate. Biochemistry 36, 11504-11513.
  9. Frazee, R.W., Orville, A.M., Dolbeare, K.B., Yu, H., Ohlendorf, D.H. and Lipscomb, J.D. (1998) The axial tyrosinate Fe3+ ligand in protocatechuate 3,4­dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. Biochemistry 37, 2131-2144.
  10. Hou, C.T. (1975) Circular dichroism of holo­ and apoprotocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa. Biochemistry 14, 3899-3902.
  11. Hou, C.T. (1978) Iron­binding ligands in the catalytic site of protocatechuate 3,4­dioxygenase. Bioinorg. Chem. 8, 237-243.
  12. Keyes, W.E. and Loehr, T.M. (1978) Raman spectral evidence for tyrosine coordination of iron in protocatechuate 3,4­dioxygenase. Biochem. Biophys. Res. Commun. 83, 941-945.
  13. Ludwig, M.L., Weber, L.D. and Ballou, D.P. (1984) Characterization of crystals of protocatechuate 3,4­dioxygenase from Pseudomonas cepacia. J. Biol. Chem. 259, 14840-14842.
  14. Ohlendorf, D.H., Weber, P.C. and Lipscomb, J.D. (1987) Determination of the quaternary structure of protocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa. J. Mol. Biol. 195, 225-227.
  15. Ohlendorf, D.H., Lipscomb, J.D. and Weber, P.C. (1988) Structure and assembly of protocatechuate 3,4­dioxygenase. Nature 336, 403-405.
  16. Ohlendorf, D.H., Orville, A.M. and Lipscomb, J.D. (1994) Structure of protocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution. J. Mol. Biol. 244, 586-608.
  17. Orville, A.M. and Lipscomb, J.D. (1989) Binding of isotopically labeled substrates, inhibitors, and cyanide by protocatechuate 3,4­dioxygenase. J. Biol. Chem. 264, 8791-8801.
  18. Orville, A.M. and Lipscomb, J.D. (1993) Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4­dioxygenase. J. Biol. Chem. 268, 8596-8607.
  19. Orville, A.M., Elango, N., Lipscomb, J.D. and Ohlendorf, D.H. (1997a) Structures of competitive inhibitor complexes of protocatechuate 3,4­dioxygenase: Multiple exogenous ligand binding orientations within the active site. Biochemistry 36, 10039-10051.
  20. Orville, A.M., Lipscomb, J.D. and Ohlendorf, D.H. (1997b) Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4­dioxygenase: Endogenous Fe3+ ligand displacement in response to substrate binding. Biochemistry 36, 10052-10066.
  21. Pascal, R.A., Jr. and Huang, D.S. (1986) Reactions of 3­ethylcatechol and 3­(methylthio)catechol with catechol dioxygenases. Arch. Biochem. Biophys. 248, 130-137.
  22. Que, L., Jr., Lipscomb, J.D., Zimmermann, R., Münck, E., Orme­Johnson, N.R. and Orme­Johnson, W.H. (1976) Mössbauer and EPR spectroscopy of protocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 452, 320-334.
  23. Que, L., Jr., Lipscomb, J.D., Münck, E. and Wood, J.M. (1977) Protocatechuate 3,4­dioxygenase. Inhibitor studies and mechanistic implications. Biochim. Biophys. Acta 485, 60-74.
  24. Satyshur, K.A., Rao, S.T., Lipscomb, J.D. and Wood, J.M. (1980) Preliminary crystallographic study of protocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa. J. Biol. Chem. 255, 10015-10016.
  25. Siu, D., Orville, A.M., Lipscomb, J.D., Ohlendorf, D.H. and Que, L., Jr. (1992) Resonance Raman studies of the protocatechuate 3,4­dioxygenase from Brevibacterium fuscum. Biochemistry 31, 10443-10448.
  26. Strachan, P.D., Freer, A.A. and Fewson, C.A. (1998) Purification and characterization of catechol 1,2­dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene. Biochem. J. 333, 741-747.
  27. True, A.E., Orville, A.M., Pearce, L.L., Lipscomb, J.D. and Que, L., Jr. (1990) An EXAFS study of the interaction of substrate with the ferric active site of protocatechuate 3,4­dioxygenase. Biochemistry 29, 10847-10854.
  28. Vetting, M.W., Earhart, C.A. and Ohlendorf, D.H. (1994) Crystallization and preliminary X­ray analysis of protocatechuate 3,4­dioxygenase from Acinetobacter calcoaceticus. J. Mol. Biol. 236, 372-373.
  29. Zaborsky, O.R., Ogletree, J. and Hou, C.T. (1975) Circular dichroism of protocatechuate 3,4­dioxygenase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 386, 18-25.
  30. Whittaker, J.W. and Lipscomb, J.D. (1984a) Transition state analogs for protocatechuate 3,4­dioxygenase. Spectroscopic and kinetic studies of the binding reactions of ketonized substrate analogs. J. Biol. Chem. 259, 4476-4486.
  31. Whittaker, J.W. and Lipscomb, J.D. (1984b) 17O­water and cyanide ligation by the active site iron of protocatechuate 3,4­dioxygenase. Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs. J. Biol. Chem. 259, 4487-4495.
  32. Whittaker, J.W., Lipscomb, J.D., Kent, T.A. and Münck, E. (1984) Brevibacterium fuscum protocatechuate 3,4­dioxygenase. Purification, crystallization, and characterization. J. Biol. Chem. 259, 4466-4475.
Reviews on aromatic­ring­cleavage dioxygenases