SEARCH

SEARCH BY CITATION

References

  • 1
    Stetter, K.O. (1988) Archaeoglobus fulgidus gen. nov., sp. nov. a new taxon of extremely thermophilic archaebacteria. Syst. Appl. Microbiol. 10, 1721720.
  • 2
    Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A., Dodson, R.J., Gwinn, M., Hickey, E.K., Peterson, J.D., Richardson, D.L., Kerlavage, A.R., Graham, D.E., Kyrpides, N.C., Fleischmann, R.D., Quackenbush, J., Lee, N.H., Sutton, G.G., Gill, S., Kirkness, E.F., Dougherty, B.A., McKenney, K., Adams, M.D., Loftus, B. & Venter, J.C. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390, 364370.
  • 3
    Ross, R.P. & Claiborne, A. (1992) Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. J. Mol. Biol. 227, 658671.
  • 4
    Ross, R.P. & Claiborne, A. (1991) Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases. J. Mol. Biol. 221, 857887.
  • 5
    Del Cardayre, S.B., Stock, K.P., Newton, G.L., Fahey, R.C. & Davies, J.E. (1998) Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme. J. Biol. Chem. 273, 57445751.
  • 6
    Maeda, K., Truscott, K., Liu, X.L. & Scopes, R.K. (1992) A thermostable NADH oxidase from anaerobic extreme thermophiles. Biochem. J. 284, 551555.
  • 7
    Liu, X.L. & Scopes, R.K. (1993) Cloning, sequencing and expression of the gene encoding NADH oxidase from the extreme anaerobic thermophile Thermoanaerobium brockii. Biochim. Biophys. Acta 1174, 187190.
  • 8
    Park, H.J., Kreutzer, R., Reiser, C.O. & Sprinzl, M. (1992) Molecular cloning and nucleotide sequence of the gene encoding a H2O2-forming NADH oxidase from the extreme thermophilic Thermus thermophilus HB8 and its expression in Escherichia coli. Eur. J. Biochem. 205, 875879.
  • 9
    Reed, D.W., Millstein, J. & Hartzell, P.L. (2001) H2O2-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus. J. Bacteriol. 183, 70077016.
  • 10
    Ward, D.E., Donnelly, C.J., Mullendore, M.E., van der Oost, J., de Vos, W.M. & Crane, E.J. III (2001) The NADH oxidase from Pyrococcus furiosus. Eur. J. Biochem. 268, 58165823.
  • 11
    Liu, Z., Niwa, O., Horiuchi, T., Kurita, R. & Torimitsu, K. (1999) NADH and glutamate on-line sensors using Os-gel-HRP/GC electrodes modifed with NADH oxidase and glutamate dehydrogenase. Biosens. Bioelectron. 14, 631638.
  • 12
    Jaenicke, R. (1991) Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715728.
  • 13
    Leuschner, C. & Antranikian, G. (1995) Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms. World. J. Microbiol. Biotechnol. 11, 95114.
  • 14
    Blumentals, I.I., Itoh, M., Olson, G.J. & Kelly, R.M. (1990) Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl. Environ. Microbiol. 56, 12551262.
  • 15
    Sambrook, J., Fritsch, E.F. & Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring. Harbor Laboratory Press, Cold Spring Harbor, NY.
  • 16
    Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.
  • 17
    Bergmeyer, H.U. & Gawehn, K. (1978) Principles of Enzymatic Analysis. Verlag Chemie, New York, Weinheim.
  • 18
    Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248254.
  • 19
    Weiss, R. (1970) The solubility of nitrogen, oxygen and neon in seawater. Deep-Sea Res. 17, 721735.
  • 20
    Higgins, D.G. & Sharp, P.M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73, 237244.
  • 21
    Matsumoto, J., Higuchi, M., Shimada, M., Yamamoto, Y. & Kamio, Y. (1996) Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans. Biosci. Biotechnol. Biochem. 60, 3943.
  • 22
    Mallett, T.C. & Claiborne, A. (1998) Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C (4a)-peroxyflavin intermediate and a rate-limiting conformational change. Biochemistry 37, 87908802.
  • 23
    Rohdich, F., Wiese, A., Feicht, R., Simon, H. & Bacher, A. (2001) Enoate reductases of Clostridia. Cloning, sequencing and expression. J. Biol. Chem. 276, 57795787.
  • 24
    He, X.Y., Yang, S.Y. & Schultz, H. (1997) Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur. J. Biochem. 248, 516520.
  • 25
    Franklund, C.V., Baron, S.F. & Hylemon, P.B. (1993) Characterization of the baiH gene encoding a bile acid-inducible NADH: flavin oxidoreductase from Eubacterium sp. Strain VPI 12708. J. Bacteriol. 175, 30023012.
  • 26
    Stanton, T.B. & Jensen, N.S. (1993) Purification and characterization of NADH oxidase from Serpulina (Treponema) hyodysenteria. J. Bacteriol. 175, 29802987.
  • 27
    Toomey, D. & Mayhew, S.G. (1998) Purification and characterisation of NADH oxidase from Thermus aquaticus YT-1 and evidence that it functions in a peroxide-reduction system. Eur. J. Biochem. 251, 935945.
  • 28
    Ma, K. & Adams, M.W.W. (1994) Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J. Bacteriol. 176, 65096517.
  • 29
    Kunow, J., Linder, D., Stetter, K.O. & Thauer, R.K. (1994) F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters. Eur. J. Biochem. 223, 503511.
  • 30
    Pagala, V.R., Park, J., Reed, D.W. & Hartzell, P.L. (2002) Cellular localization of d-lactate dehydrogenase and NADH oxidase from Archaeoglobus fulgidus. Archaea 1, 95104.
  • 31
    Tindall, B.J., Stetter, K.O. & Collins, M.D. (1989) A novel, fully saturated menaquinone from the thermophilic, sulphate-reducing archaebacterium Archaeoglobus fulgidus. J. General Microbiol. 135, 693696.
  • 32
    Schut, G.J., Zhou, J. & Adams, M.W.W. (2001) DNA microarray analysis of the hyperthermophilic archaeon Pyrococcus furiosus: evidence for an new type of sulfur-reducing enzyme complex. J. Bacteriol. 183, 70277036.
  • 33
    Kengen, S.W.M., Bikker, F.J., Hagen, W.R., de Vos, W.M. & van der Oost, J. (2001) Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus. Extremophiles 5, 323332.
  • 34
    Abreu, I.A., Saraiva, L.M., Carita, J., Huber, H., Stetter, K.O., Cabelli, D. & Teixeira, M. (2000) Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by Neelaredoxin. Mol. Microbiol. 38, 322334.
  • 35
    Chen, L., Liu, M.Y., Legall, J., Fareleira, P., Santos, H. & Xavier, A.V. (1993) Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas. Eur. J. Biochem. 216, 443448.
  • 36
    Snel, B., Lehmann, G., Bork, P. & Huynen, M.A. (2000) STRING: a web-server to retrieve and display the repeatedly occurring neighbourhood of a gene. Nucleic Acids Res. 28, 34423444.
  • 37
    Park, H.J., Reiser, C.O.A., Kondruweit, S., Erdmann, H., Schmid, R.D. & Sprinzl, M. (1992) Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus. Eur. J. Biochem. 205, 881885.