Effects of substrate analogues and pH on manganese superoxide dismutases

Biochemistry

Volumn 45, Issue 6, 2006, Pages 1919-1929

  Tabares, Leandro C ^a,b   Cortez, Néstor ^b   Hiraoka, B Yukihiro ^c   Yamakura, Fumiyuki ^d   Un, Sun ^a  

^a CNRS   (France)

^b UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

^c MATSUMOTO DENTAL UNIVERSITY   (Japan)

^d JUNTENDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONS; ESCHERICHIA COLI; PARAMAGNETIC RESONANCE; PH EFFECTS; PROTEINS; SPECTROSCOPIC ANALYSIS;

ANALOGUES AZIDE; CAMBIALISTIC SOD; MANGANESE SUPEROXIDE DISMUTASES; RHODOBACTER CAPSULATUS;

MANGANESE COMPOUNDS;

AZIDE; FLUORIDE; GLYCINE; IRON SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; TYROSINE;

ARTICLE; BINDING SITE; ELECTRON SPIN RESONANCE; ENZYME BINDING; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PH; PORPHYROMONAS GINGIVALIS; PRIORITY JOURNAL; RHODOBACTER CAPSULATUS; SPECTROSCOPY;

AZIDES; BINDING SITES; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; FLUORIDES; GLYCINE; HYDROGEN-ION CONCENTRATION; IRON; MANGANESE; MODELS, MOLECULAR; MUTATION; PORPHYROMONAS GINGIVALIS; PROTEIN CONFORMATION; RHODOBACTER CAPSULATUS; STRUCTURE-ACTIVITY RELATIONSHIP; SUPEROXIDE DISMUTASE; THREONINE; TYROSINE;

ESCHERICHIA COLI; PORPHYROMONAS GINGIVALIS; RHODOBACTER CAPSULATUS;

EID: 32344438011     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051947m     Document Type: Article

References (58)

1. Fridovich, I. (1995) Superoxide radical and superoxide dismutases, Annu. Rev. Biochem. 64, 97-112.
2. Touati, D. (1997) Superoxide dismutases in bacteria and pathogen protists, in Oxidative Stress and the Molecular Biology of Antioxidant Defenses (Scandalios, J. G., Ed.) pp 447-493, Cold Spring Harbor, New York.
3. Bull, C., and Fee, J. A. (1985) Steady-state kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli, J. Am. Chem. Soc. 107, 3295-3304.
4. Lavelle, F., McAdam, M. E., Fielden, E, M., and Roberts, P. B. (1977) A pulse-radiolysis study of the catalytic mechanism of the iron-containing superoxide dismutase from Photobacterium leiognathi, Biochem. J. 161, 3-11.
5. Klug-Roth, D., Fridovich, I., and Rabani, J. (1973) Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase, J. Am. Chem. Soc. 95, 2786-2790.
6. Kim, E. J., Chung, H. J., Suh, B., Hah, Y. C., and Roe, J. H. (1998) Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller, Mol. Microbiol 27, 187-195.
7. Kim, F. J., Kim, H. P., Hah, Y. C., and Roe, J. H. (1996) Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor, Eur. J. Biochem. 241, 178-185.
8. Stroupe, M. E., DiDonato, M., and Tainer, J. A. (2001) in Handbook of Metalloproteins (Messerschmidt, A., Huber, R., Wieghardt, K., and Paulos, T., Eds.) pp 941-951, Wiley and Sons, Chichester, U.K.
9. Miller, A.-F. (2001) in Handbook of Metalloproteins (Messerschmidt, A., Huber, R., Wieghardt, K., and Paulos, T., Eds.) pp 668-682, Wiley and Sons, Chichester, U.K.
10. Sugio, S., Hiraoka, B. Y., and Yamakura, F. (2000) Crystal structure of cambialistic superoxide dismutase from Porphyromonas gingivalis, Eur. J. Biochem. 267, 3487-3495.
11. Schmidt, B., Meier, B., and Parak, F. (1996) X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn, J. Biol. Inorg. Chem. 1, 532-541.
12. Ose, D. E., and Fridovich, I. (1976) Superoxide dismutase. Reversible removal of manganese and its substitution by cobalt, nickel or zinc, J. Biol. Chem. 251, 1217-1218.
13. Yamakura, F. (1980) Cadmium, chromium, and manganese replacement for iron in iron-superoxide dismutase from Pseudomonas ovalis, J. Biochem. (Tokyo) 88, 191-196.
14. Meier, B., Barra, D., Bossa, F., Calabrese, L., and Rotilio, G. (1982) Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied, J. Biol. Chem. 257, 13977-13980.
15. Amano, A., Shizukuishi, S., Tamagawa, H., Iwakura, K., Tsunasawa, S., and Tsunemitsu, A. (1990) Characterization of superoxide dismutase purified from either anaerobically maintained or aerated Bacteroides gingivalis, J. Bacteriol. 172, 1457-1463.
16. Martin, M. E., Byers, E. B. R., Olson, M. O. J., Salin, M. L., Arceneaux, J. E. L., and Tolbert, C. (1986) A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor, J. Biol. Chem. 261, 9361-9367.
17. 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis, Arch. Biochem. Biophys. 238, 83-89.
18. Tabares, L. C., Bittel, C., Carrillo, N., Bortolotti, A., and Cortez, N. (2003) The single superoxide dismutase of Rhodobacter capsulatus is a cambialistic, manganese-containing enzyme, J. Bacteriol. 185, 3223-3227.
19. Fee, J. A., McClune, G. J., O'Neill, P., and Fielden, E. M. (1981) Saturation behavior of superoxide dismutation catalyzed by the iron containing superoxide dismutase of E. coli B, Biochem. Biophys. Res. Commun. 100, 377-384.
20. Tierney, D. L., Fee, J. A., Ludwig, M. L., and Penner-Hahn, J. E. (1995) X-ray absorption spectroscopy of the iron site in Escherichia call Fe(III) superoxide dismutase, Biochemistry 34, 1661-1668.
21. Sorkin, D. L., Duong, D. K., and Miller, A. F. (1997) Mutation of tyrosine 34 to phenylalanine eliminates the active site pK of reduced iron-containing superoxide dismutase, Biochemistry 36, 8202-8208.
22. Sorkin, D. L., and Miller, A. F. (1997) Spectroscopic measurement of a long-predicted active site pK in iron-superoxide dismutase from Escherichia coli, Biochemistry 36, 4916-4924.
23. Jackson, T. A., Xie, J., Yikilmaz, E., Miller, A. F., and Brunold, T. C. (2002) Spectroscopic and computational studies on iron and manganese superoxide dismutases: Nature of the chemical events associated with active-site pKs, J. Am Chem. Soc. 124, 10833-10845.
24. Terech, A., Pucheault, J., and Ferradini, C. (1983) Saturation behavior of the manganese-containing superoxide dismutase from Paracoccus denitrificans, Biochem. Biophys. Res. Commun. 113, 114-20.
25. Hsu, J. L., Hsieh, Y., Tu, C, O'Connor, D., Nick, H. S., and Silverman, D. N. (1996) Catalytic properties of human manganese superoxide dismutase, J. Biol. Chem. 271, 17687-17691.
26. Borgstahl, G. E. O., Pokross, M., Chehab, R., Sekher, A., and Snell, E. H. (2000) Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase, J. Mol. Biol. 296, 951-959.
27. Whittaker, M. M., and Whittaker, J. W. (1997) Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase, Biochemistry 36, 8923-8931.
28. Guan, Y., Hickey, M. J., Borgstahl, G. E. O., Hallewell, R. A., Lepock, J. R., O'Conner, D., Hsieh, Y., Nick, H. S., Silvermann, D. N., and Tainer, J. A. (1998) Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34, Biochemistry 37, 4722-4730.
29. Maliekal, J., Karapetan, A., Vance, C., Yikilmaz, E., Wu, Q., Jackson, T., Brounold, T. C., Spiro, T. G., and Miller, A.-F. (2002) Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase, J. Am. Chem. Soc. 124, 15064-15075.
30. Lah, M. S., Dixon, M. M., Pattridge, K. A., Stallings, W. C., Fee, J. A., and Ludwig, M. L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus, Biochemistry 34, 1646-1660.
31. Ludwig, M. L., Metzger, A. L., Pattridge, K. A., and Stallings, W. C. (1991) Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 Å resolution, J. Mol. Biol. 219, 335-358.
32. Stallings, W. C., Metzger, A. L., Pattridge, K. A., Fee, J. A., and Ludwig, M. L. (1991) Structure-function relationships in iron and manganese superoxide dismutases, Free Radical Res. Commun. 12-13 (Pt. 1), 259-268.
33. Whittaker, M. M., and Whittaker, J. W. (1991) Active site spectral studies on manganese superoxide dismutase, J. Am. Chem. Soc. 113, 5528-5540.
34. Slykhouse, T. O., and Fee, J. A. (1976) Physical and chemical studies on bacterial superoxide dismutases, J. Biol. Chem. 251, 5472-5477.
35. Schmidt, M. (1999) Manipulating the coordination mumber of the ferric iron within the cambialistic superoxide dismutase of Propionibacterium shemanii by changing the pH-value. A crystallographic analysis, Eur. J. Biochem. 262, 117-127.
36. Whittaker, J. W., and Solomon, E. I. (1988) Spectroscopic studies on ferrous non-heme iron active sites: Magnetic circular dichroism of mononuclear Fe sites in superoxide dismutase and lipoxygenase, J. Am. Chem. Soc. 110, 5329-5339.
37. Miller, A. F., Sorkin, D. L., and Padmakumar, K. (2005) Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34, Biochemistry 44, 5969-5981.
38. Whittaker, M. M., and Whittaker, J. W. (1996) Low-temperature thermochromism marks a change in coordination for the metal ion in manganese superoxide dismutase, Biochemistry 35, 6762-6770.
39. Jackson, T. A., Karapetan, A., Miller, A.-F., and Brunold, T. C. (2004) Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: Definitive assignment of the ligand responsible for the low-temperature thermochroism, J. Am. Chem. Soc. 126, 12477-12491.
40. Un, S., Dorlet, P., Voyard, G., Tabares, L. C., and Cortez, N. (2001) High-field EPR characterization of manganese reconstituted superoxide dismutase from Rhodobacter capsulatus, J. Am. Chem. Soc. 123, 10123-10124.
41. Un, S., Tabares, L. C., Cortez, N., Hiraoka, B. Y., and Yamakura, F. (2004) Manganese(II) zero-field interaction in cambialistic and manganese superoxide dismutases and its relationship to the structure of the metal binding site, J. Am. Chem. Soc. 126, 2720-2726.
42. Tabares, L. C., Cortez, N., Agalidis, I., and Un, S. (2005) Temperature-dependent coordination in E. coli manganese superoxide, J. Am. Chem. Soc. 127, 6039-6047.
43. Yamakura, F., Sugio, S., Hiraoka, B. Y., Yokota, T., and Ohmori, D. (2003) Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site, Biochemistry 42, 10790-10799.
44. Cortez, N., Carrillo, N., Pasternak, C., Balzer, A., and Klug, G. (1998) Molecular cloning and expression analysis of the Rhodobacter capsulatus sodB gene, encoding an iron superoxide dismutase, J. Bacteriol. 180, 5413-5420.
45. McCord, J. M., and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J. Biol. Chem. 244, 6049-6055.
46. Un, S., Dorlet, P., and Rutherford, A. W. (2001) A high-field tour of radicals in photosystems I and II, Appl. Magn. Reson. 21, 341-361.
47. Burghaus, O., Plato, M., Rohrer, M., Moebius, K., MacMillan, F., and Lubitz, W. (1993) 3-mm high-field EPR on semiquinone radical anions Q(.-) related to photosynthesis and on the primary donor P(.+) and acceptor QA(.-) in reaction centers of Rhodobacter sphaeroides R-26, J. Phys. Chem. 97, 7639-7647.
48. Markham, G. D., Rao, B. D. N., and Reed, G. H. (1979) Analysis of EPR powder patter lineshapes for Mn(II) including third-order perturbation corrections. Applications to Mn(II) complex with enzymes, J. Magn. Reson. 33, 592-602.
49. Beyer, W. F., Jr., and Fridovich, I. (1987) Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli, Biochemistry 26, 1251-1257.
50. 2 by applied field, Phys. Rev. B: Solid State 13, 2723-2728.
51. 2+ ions, J. Phys. Chem. Solids 34, 1773-1777.
52. 2: Mn crystals, J. Phys. Chem. Solids 54, 315-323.
53. 2:Mn, J. Phys. Chem. Solids 56, 703-714.
54. 2+ with mixed ligands, J. Magn. Reson. 69, 134-143.
55. Newman, D. J., and Urban, W. (1975) Interpretation of S-state ion EPR spectra, Adv. Phys. 24, 793-844.
56. Yamakura, F. (1978) A study on the reconstitution of iron-superoxide dismutase from Pseudomonas ovalis, J. Biochem. 83, 849-857.
57. Vance, C. K., and Miller, A. F. (1998) Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase, Biochemistry 37, 5518-5527.
58. Edwards, R. A., Baker, H. M., Whittaker, M. M., Whittaker, J. W., Jameson, G. B., and Baker, E. N. (1998) Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1 Å resolution, J. Biol. Chem. 3, 161-171.