Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase

Journal of Bacteriology

Volumn 186, Issue 23, 2004, Pages 7888-7895

  Weinberg, Michael V ^a   Jenney Jr , Francis E ^a   Cui, Xiaoyuan ^a,b   Adams, Michael W W ^a  

^a University of Georgia ^*  (United States)

^b NATIONAL STARCH AND CHEMICAL COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; IRON; OXIDOREDUCTASE; PEROXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RUBREDOXIN; RUBRERYTHRIN; UNCLASSIFIED DRUG;

ANAEROBIC METABOLISM; ANTIOXIDANT ACTIVITY; ARTICLE; BACTERIAL METABOLISM; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PURIFICATION; ESCHERICHIA COLI; NONHUMAN; OXIDATIVE STRESS; PHYLOGENETIC TREE; PRIORITY JOURNAL; PYROCOCCUS FURIOSUS;

BACTERIAL PROTEINS; CATALYSIS; FERREDOXINS; NAD; PEROXIDASES; PYROCOCCUS FURIOSUS; RECOMBINANT PROTEINS; RUBREDOXINS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PYROCOCCUS FURIOSUS;

EID: 9244263012     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.23.7888-7895.2004     Document Type: Article

References (47)

1. Adams, M. W. W., F. E. Jenney, M. D. Clay, and M. K. Johnson. 2002. Superoxide reductase: fact or fiction? J. Biol. Inorg. Chem. 7:647-652.
2. Alban, P. S., and N. R. Krieg. 1998. A hydrogen peroxide resistant mutant of Spirillum volutans has NADH peroxidase activity but no increased oxygen tolerance. Can. J. Microbiol. 44:87-91.
3. 2-terminal sequencing. J. Appl. Microbiol. 85:875-882.
4. Bonomi, F., D. M. Kurtz, and X. Y. Cui. 1996. Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin. J. Biol. Inorg. Chem. 1:67-72.
5. Brown-Peterson, N. J., and M. L. Salin. 1993. Purification of a catalase-peroxidase from Halobacterium halobium: characterization of some unique properties of the halophilic enzyme. J. Bacteriol. 175:4197-4202.
6. Bryant, F. O., and M. W. W. Adams. 1989. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264:5070-5079.
7. Coulter, E. D., and D. M. Kurtz. 2001. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch. Biochem. Biophys. 394:76-86.
8. Coulter, E. D., N. V. Shenvi, Z. M. Beharry, J. J. Smith, B. C. Prickril, and D. M. Kurtz. 2000. Rubrerythrin-catalyzed substrate oxidation by dioxygen and hydrogen peroxide. Inorg. Chim. Acta 297:231-241.
9. Coulter, E. D., N. V. Shenvi, and D. M. Kurtz. 1999. NADH peroxidase activity of rubrerythrin. Biochem. Biophys. Res. Commun. 255:317-323.
10. Das, A., E. D. Coulter, D. M. Kurtz, and L. G. Ljungdahl. 2001. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin. J. Bacteriol. 183:1560-1567.
11. Dawson, R. M. C., D. C. Elliot, W. H. Elliot, and K. M. Jones. 1986. Data for biochemical research, 3rd ed., vol. 1. Clarendon Press, Oxford, England.
12. deMare, F., D. M. Kurtz, and P. Nordlund. 1996. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat. Struct. Biol. 3:539-546.
13. Eidsness, M., S. O'Dell, D. Kurtz, Jr., R. Robson, and R. Scott. 1992. Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin. Protein Eng. 5:367-371.
14. Felsenstein, J. 1996. Inferring phytogenies from protein sequences by parsimony, distance and likelihood methods. Methods Enzymol. 266:418-427.
15. Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp-nov represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
16. Geissmann, T. A., M. Teuber, and L. Meile. 1999. Transcriptional analysis of the rubrerythrin and Superoxide dismutase genes of Clostridium perfringens. J. Bacteriol. 181:7136-7139.
17. Gudelj, M., G. O. Fruhwirth, A. Paar, F. Lottspeich, K. H. Robra, A. Cavaco-Paulo, and G. M. Gubitz. 2001. A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents. Extremophiles 5:423-429.
18. Gupta, N., F. Bonomi, D. M. Kurtz, N. Ravi, D. L. Wang, and B. H. Huynh. 1995. Recombinant Desulfovibrio vulgaris rubrerythrin-isolation and characterization of the diiron domain. Biochemistry 34:3310-3318.
19. Heinonen, J. K., and R. J. Lahti. 1981. A new and convenient colorimetric determination of inorganic ortho-phosphate and its application to the assay of inorganic pyrophosphatase. Anal. Biochem. 113:313-317.
20. http://www.secsg.org.
21. http://www.tigr.org.
22. Jenney, F. E., and M. W. W. Adams. 2001. Rubredoxin from Pyrococcus furiosus. Methods Enzymol. 334:45-55.
23. Jenney, F. E., M. F. J. M. Verhagen, X. Y. Cui, and M. W. W. Adams. 1999. Anaerobic microbes: Oxygen detoxification without Superoxide dismutase. Science 286:306-309.
24. 2-induced peptides in an obligatory anaerobe, Clostridium acetobutylicum. FEBS Lett. 571:21-25.
25. Kengen, S. W., F. J. Bikker, W. R. Hagen, W. M. de Vos, and J. Van Der Oost. 2001. Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus. Extremophiles 5:323-332.
26. Kumar, S., K. Tamura, and M. Nei. 2004. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Briefings Bioinformatics 5:150-163.
27. Legall, J., B. C. Prickril, I. Moura, A. V. Xavier, J. J. G. Moura, and B. H. Huynh. 1988. Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster. Biochemistry 27:1636-1642.
28. Lehmann, Y., L. Meile, and M. Teuber. 1996. Rubrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its Superoxide dismutase function. J. Bacteriol. 178:7152-7158.
29. Li, M., M. Y. Liu, J. Le Gall, L. L. Gui, J. Liao, T. Jiang, J. Zhang, D. Liang, and W. Chang. 2003. Crystal structure studies on rubrerythrin: Enzymatic activity in relation to the zinc movement. J. Biol. Inorg. Chem. 8:149-155.
30. Liu, M. Y., and J. Legall. 1990. Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris-rubrerythrin and a new, highly-active, enzyme. Biochem. Biophys. Res. Commun. 171:313-318.
31. Lovenberg, W., J. C. Rabinowitz, and B. B. Buchanan. 1963. Studies on chemical nature of clostridial ferredoxin. J. Biol. Chem. 238:3899-3913.
32. Ma, K., and M. W. W. Adams. 1999. A hyperactive NAD(P)H: rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 181:5530-5533.
33. Mccord, J. M., and I. Fridovic. 1969. Superoxide dismutase-an enzymic function for erythrocuprein. J. Biol. Chem. 244:6049-6055.
34. Pierik, A. J., R. B. G. Wolbert, G. L. Portier, M. F. J. M. Vertagen, and W. R. Hagen. 1993. Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters. Eur. J. Biochem. 212:237-245.
35. Ravi, N., B. C. Prickril, D. M. Kurtz, and B. H. Huynh. 1993. Spectroscopic characterization of Fe-57-reconstituted rubrerythrin, a nonheme iron protein with structural analogies to ribonucleotide reductase. Biochemistry 32:8487-8491.
36. Robb, F. T., D. L. Maeder, J. R. Brown, J. DiRuggiero, M. D. Stump, R. K. Yeh, R. B. Weiss, and D. M. Dunn. 2001. Genomic sequence of hyperthermophile, Pyrococcus furiosus: Implications for physiology and enzymology. Methods Enzymol. 330:134-157.
37. Rzhetsky, A., and M. Nei. 1993. Theoretical foundation of the minimum-evolution method of phylogenetic inference. Mol. Biol. Evol. 10:1073-1095.
38. Saitou, N., and M. Nei. 1987. The neighbor-joining method-a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
39. Sambrook, J., and D. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
40. Schut, G. J., S. D. Brehm, S. Datta, and M. W. W. Adams. 2003. Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides. J. Bacteriol. 185:3935-3947.
41. Sieker, L. C., M. Holmes, I. Le Trong, S. Turley, M. Y. Liu, J. LeGall, and R. E. Stenkamp. 2000. The 1.9 angstrom crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: some surprising results. J. Biol. Inorg. Chem. 5:505-513.
42. Sieker, L. C., M. Holmes, I. Le Trong, S. Turley, B. D. Santarsiero, M. Y. Liu, J. LeGall, and R. E. Stenkamp. 1999. Alternative metal-binding sites in rubrerythrin. Nat. Struct. Biol. 6:308-309.
43. Sztukowska, M., M. Bugno, J. Potempa, J. Travis, and D. M. Kurtz. 2002. Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis. Mol. Microbiol. 44:479-488.
44. Tempel, W., Z. J. Liu, F. D. Schubot, M. V. Weinberg, F. E. Jenney, Jr., M. W. W. Adams, J. P. Rose, and B. C. Wang. Structural genomics of Pyrococcus furiosus: X-ray crystallography reveals 3D domain swapping in rubrerythrin. Proteins Struct. Funct. Genet., in press.
45. Thompson, V. S., K. D. Schaller, and W. A. Apel. 2003. Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus. Biotechnol. Prog. 19:1292-1299.
46. Van Beeumen, J. J., G. Van Driessche, M. Y. Liu, and J. LeGall. 1991. The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris-comparison with hemerythrin and rubre-doxin. J. Biol. Chem. 266:20645-20653.
47. Wakagi, T. 2003. Sulerythrin, the smallest member of the rubrerythrin family, from the strictly aerobic and thermoacidophilic archaeon, Sulfolobus tokodaii strain 7. FEMS Microbiol. Lett. 222:33-37.