Fe3+-η2-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii

Biophysical Chemistry

Volumn 119, Issue 1, 2006, Pages 38-48

  Mathé, Christelle ^a,b   Nivière, Vincent ^b   Houée Levin, Chantal ^c   Mattioli, Tony A ^a  

^a CEA SACLAY   (France)

^b UNIV GRENOBLE ALPES   (France)

^c UNIVERSITÉ PARIS SUD   (France)

Author keywords

Desulfoarculus baarsii; Desulfoferrodoxin; Ferricyanide; Hydrogen peroxide; Iron peroxo intermediate; Neelaredoxin; Oxidative stress; Pulse radiolysis; Resonance Raman; Superoxide reductase SOR; Treponema pallidum

Indexed keywords

OXIDOREDUCTASE; SUPEROXIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CHEMICAL REACTION; CONTROLLED STUDY; CORRELATION ANALYSIS; DESULFOARCULUS; DETOXIFICATION; NONHUMAN; PRIORITY JOURNAL; RAMAN SPECTROMETRY; SPECIES DIFFERENTIATION; TREPONEMA PALLIDUM;

BINDING SITES; CATALYSIS; CATIONS; CYSTEINE; DESULFOVIBRIO; ELECTRON SPIN RESONANCE SPECTROSCOPY; FERRIC COMPOUNDS; HYDROGEN PEROXIDE; IRON; LIGANDS; OXIDOREDUCTASES; SPECTRUM ANALYSIS, RAMAN; SULFUR; TEMPERATURE; TREPONEMA PALLIDUM;

DESULFOARCULUS; DESULFOVIBRIO BAARSII; TREPONEMA PALLIDUM;

EID: 29344444990     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.06.013     Document Type: Article

References (35)

1. F.E. Jenney Jr., M.F.J.M. Verhagen, X. Cui, and M.W.W. Adams Anaerobic microbes: oxygen detoxification without superoxide dismutase Science 286 1999 306 309
2. M. Lombard, M. Fontecave, D. Touati, and V. Nivière Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity J. Biol. Chem. 275 2000 115 121
3. V. Nivière, and M. Fontecave Discovery of superoxide reductase: an historical perspective J. Biol. Inorg. Chem. 9 2004 119 123
4. M. Lombard, D. Touati, M. Fontecave, and V. Nivière Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum J. Biol. Chem. 275 2000 27021 27026
5. T. Jovanovic, C. Ascenso, K.R.O. Hazlett, R. Sikkink, C. Krebs, R. Litwiller, L.M. Benson, I. Moura, J.J.G. Moura, J.D. Radolf, B.H. Huynh, S. Naylor, and F. Rusnak Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase J. Biol. Chem. 275 2000 28439 28448
6. I.A. Abreu, L.M. Saraiva, J. Carita, H. Huber, K.O. Stetter, D.E. Cabelli, and M. Teixeira Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin Mol. Microbiol. 38 2000 322 334
7. M.J. Pianzzola, M. Soubes, and D. Touati Overproduction of the rbo gene product from Desulfovibrio species suppresses all deleterious effects of lack of superoxide dismutase in Escherichia coli J. Bacteriol. 178 1996 6736 6742
8. M. Fournier, Y. Zhang, J.D. Wildschut, A. Dolla, J.K. Voordouw, D.C. Schriemer, and G. Voordouw Function of oxygen resistance proteins in the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough J. Bacteriol. 185 2003 71 79
9. 4 centre J. Biol. Inorg. Chem. 2 1997 680 689
10. M.D. Clay, J.P. Emerson, E.D. Coulter, D.M. Kurtz Jr., and M.K. Johnson Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris J. Biol. Inorg. Chem. 8 2003 671 682
11. J.P. Emerson, D.E. Cabelli, and D.M. Kurtz Jr. An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo Proc. Natl. Acad. Sci. U. S. A. 100 2003 3802 3807
12. P.Y. Andrew, Y. Hu, F.E. Jenney Jr., M.W.W. Adams, and D.C. Rees Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states Biochemistry 39 2000 2499 2508
13. M.D. Clay, F.E. Jenney Jr., P.L. Hagedoorn, G.N. George, M.W.W. Adams, and M.K. Johnson Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism J. Am. Chem. Soc. 124 2002 788 805
14. C. Berthomieu, F. Dupeyrat, M. Fontecave, A. Verméglio, and V. Nivière Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study Biochemistry 41 2002 10360 10368
15. J.P. Emerson, E.D. Coulter, R.S. Phillips, and D.M. Kurtz Jr. Kinetics of the superoxide reductase catalytic cycle J. Biol. Chem. 278 2003 39662 39668
16. P. Tavares, N. Ravi, J.J.G. Moura, J. LeGall, Y.H. Huang, B.R. Crouse, M.K. Johnson, B.H. Huynh, and I. Moura Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774) J. Biol. Chem. 269 1994 10504 10510
17. M.F.J.M. Verhagen, W.G.B. Voorhorst, J.A. Kolkman, R.B.G. Wolbert, and W.R. Hagen On the two iron centers of desulfoferrodoxin FEBS Lett. 336 1993 13 18
18. E.D. Coulter, J.P. Emerson, D.M. Kurtz Jr., and D.E. Cabelli Superoxide reactivity of rubredoxin oxidoreductase (Desulfoferrodoxin) from Desulfovibrio vulgaris: a pulse radiolysis study J. Am. Chem. Soc. 122 2000 11555 11556
19. M. Lombard, C. Houée-Levin, D. Touati, M. Fontecave, and V. Nivière Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis Biochemistry 40 2001 5032 5040
20. V. Nivière, M. Lombard, M. Fontecave, and C. Houée-Levin Pulse radiolysis studies on superoxide reductase from Treponema pallidum FEBS Lett. 497 2001 171 173
21. I.A. Abreu, L.M. Saraiva, C.M. Soares, M. Teixeira, and D.E. Cabelli The mechanism of superoxide scavenging by Archaeoglobus fulgidus neelaredoxin J. Biol. Chem. 276 2001 38995 39001
22. J.P. Emerson, E.D. Coulter, D.E. Cabelli, R.S. Phillips, and D.M. Kurtz Jr. Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris Biochemistry 41 2002 4348 4357
23. V. Nivière, M. Asso, C.O. Weill, M. Lombard, B. Guigliarelli, V. Favaudon, and C. Houée-Levin Superoxide reductase from Desulfoarculus baarsii: identification of protonation steps in the enzymatic mechanism Biochemistry 43 2004 808 818
24. C. Mathé, T.A. Mattioli, O. Horner, M. Lombard, J.M. Latour, M. Fontecave, and V. Nivière Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii J. Am. Chem. Soc. 124 2002 4966 4967
25. 3+ species in the active site of superoxide reductase from Desulfoarculus baarsii. Density functional calculations on related models Biochemistry 43 2004 8815 8825
26. 6 Inorg. Chem. 42 2003 938 940
27. M.D. Clay, F.E. Jenney Jr., H.J. Noh, P.L. Hagedoom, G.N. George, M.W.W. Adams, and M.K. Johnson Resonance Raman characterization of the mononuclear iron active-site vibrations and putative electron transport pathways in Pyrococcus furiosus superoxide reductase Biochemistry 41 2002 9833 9841
28. V. Adams, A. Royant, V. Nivière, F.P. Molina-Heredia, and D. Bourgeois Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction Structure 12 2004 1729 1740
29. M.D. Clay, C.A. Cosper, F.E. Jenney Jr., M.W.W. Adams, and M.K. Johnson Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase Proc. Natl. Acad. Sci. U. S. A. 100 2003 3796 3801
30. J.J. Girerd, F. Banse, and A. Simaan Characterization and properties of non-heme iron peroxo complexes Struct. Bond. 97 2000 145 177
31. R. Silaghi-Dumitrescu, I. Silaghi-Dumitrescu, E.D. Coulter, and D.M. Kurtz Jr. Computational study of the non-heme iron active site in superoxide reductase and its reaction with superoxide Inorg. Chem. 42 2003 446 456
32. G. Roelfes, V. Vrajmasu, K. Chen, R.Y.N. Ho, J.-U. Rohde, C. Zondervan, R.M. la Crois, E.P. Schudde, M. Lutz, A.L. Spek, R. Hage, B.L. Feringa, E. Münck, and L. Que Jr. End-on and side-on peroxo derivatives of non-heme iron complexes with pentadentate ligands: models for putative intermediates in biological iron/dioxygen chemistry Inorg. Chem. 42 2003 2639 2653
33. 2 Proc. Natl. Acad. Sci. U. S. A. 100 2003 3635 3640
34. B. Meunier, S.P. de Visser, and S. Shaik Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes Chem. Rev. 104 2004 3947 3980
35. Z. Chen, T.W.B. Ost, and J.P.M. Schelvis Phe393 mutants of cytochrome P450 BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations Biochemistry 43 2004 1798 1808