• 1
    Claiborne, A., Yeh, J.I., Mallett, T.C., Luba, J., Crane, E.J. III, Charrier, V., Parsonage, D. (1999) Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38, 1540715416DOI: 10.1021/bi992025k
  • 2
    Brown, D.M., Upcroft, J.A., Upcroft, P. (1996) A H2O producing NADH oxidase from the protozoan parasite Giardia duodenalis. Eur. J. Biochem. 241, 155161
  • 3
    Kawarabayasi, Y., Sawada, M., Horikawa, H., Haikawa, Y., Hino, Y., Yamamoto, S., Sekine, M., Baba, S., Kosugi, H., Hosoyama, A. , et al. (1998) Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5, 5576
  • 4
    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. , et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390, 364370
  • 5
    Bult, C.J., White, O., Olsen, G.J., Zhou, L., Fleischmann, R.D., Sutton, G.G., Blake, J.A., FitzGerald, L.M., Clayton, R.A., Gocayne, J.D. , et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 10581073
  • 6
    Nelson, K.E., Clayton, R.A., Gill, S.R., Gwinn, M.L., Dodson, R.J., Haft, D.H., Hickey, E.K., Peterson, J.D., Nelson, W.C., Ketchum, K.A. , et al. (1999) Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature 399, 323329
  • 7
    Hecht, H.J., Erdmann, H., Park, H.J., Sprinzl, M., Schmid, R.D. (1995) Crystal structure of NADH oxidase from Thermus thermophilus. Nature Struct. Biol. 2, 11091114
  • 8
    Gomes, C.M. & Teixeira, M. (1998) The NADH oxidase from the thermoacidophilic archaea Acidianus ambivalens: isolation and physicochemical characterisation. Biochem. Biophys. Res. Commun. 243, 412415
  • 9
    Liu, X. & Scopes, R. (1993) Cloning, sequencing and expression of the gene encoding NADH oxidase from the extreme anaerobic thermophile Thermoanaerobium brockii. Biochim. Biophys. Acta 1174, 187190
  • 10
    Crane, E., Ward, D., van der Oost, J., She, Q., Garrett, R. (1999) Sequence analysis and overexpression of putative NADH oxidases from the hyperthermophilic archaeons Sulfolobus solfataricus and Pyrococcus horikoshii. In Flavins and Flavoproteins (Ghisla S., Macheroux P.K.P. & Sund H., eds), pp. 281284. Rudolf Weber, Berlin
  • 11
    Jenney, F., Verhagen, M., Cui, X., Adams, M. (1999) Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286, 306309
  • 12
    Ward, D.K.S., van der Oost, J., de Vos, W. (2000) Purification and characterization of the alanine aminotransferase from the hyperthermophilic archaeon Pyrococcus furiosus and its role in alanine Production. J. Bacteriol. 182, 25592566
  • 13
    Makinen, K. & Tenovuo, J. (1982) Observations on the use of guaicol and 2,2′-azino-di(3-ethylbenzthiazoline-6-sulfonic acid) as peroxidse substrates. Anal. Biochem. 126, 100108
  • 14
    Ahmed, S.A. & Claiborne, A. (1989) The Streptococcal flavoprotein NADH oxidase I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers. J. Biol. Chem. 264, 1985619863
  • 15
    Crane, E., Parsonage, D., Poole, L., Claiborne, A. (1995) Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms. Biochemistry. 34, 1411414124
  • 16
    Dai, L. & Klibanov, A. (1999) Striking activation of oxidative enzymes suspended in nonaqueous media. Proc. Natl Acad. Sci. USA 96, 94759478
  • 17
    Klibanov, A. (2001) Improving enzymes by using them in organic solvents. Nature 409, 241256DOI: 10.1038/35051719
  • 18
    Luba, J., Charrier, V., Claiborne, A. (1999) Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry 38, 27252737
  • 19
    Mallett, T.C., Parsonage, D., Claiborne, A. (1999) Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center. Biochemistry 38, 30003011.
  • 20
    Jeffers, C. & Tu, S. (2001) Differential transfers of reduced flavin cofactor and product by bacterial flavin reductase to luciferase. Biochemistry 40, 17491754DOI: 10.1021/bi0024310
  • 21
    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
  • 22
    Poole, L. & Ellis, H. (1996) Flavin-dependent hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35, 5664
  • 23
    Niimura, Y., Nishiyama, Y., Saito, D., Tsuji, H., Hidaka, M., Miyaji, T., Watanabem, T., Massey, V. (2000) A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus. J. Bacteriol. 182, 50465051
  • 24
    Poole, L.B. & Claiborne, A. (1989) The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J. Biol. Chem. 264, 1233012338
  • 25
    Ahmed, S.A. & Claiborne, A. (1989) The streptococcal flavoprotein NADH oxidase. II. Interactions of pyridine nucleotides with reduced and oxidized enzyme forms. J. Biol. Chem. 264, 1986319870
  • 26
    Crane, E.J., III, Vervoort, J., Claiborne, A. (1997) 13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase. Biochemistry 36, 86118618
  • 27
    Parsonage, D. & Claiborne, A. (1995) Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center. Biochemistry 34, 435441
  • 28
    Chae, H., Robison, K., Poole, L., Church, G., Storz, G., Rhee, S. (1994) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA. 91, 70177021
  • 29
    Kang, S.W., Baines, I.C., Rhee, S.G. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273, 63036311
  • 30
    Poole, L.B., Reynolds, C.M., Wood, Z.A., Karplus, P.A., Ellis, H.R., Li Calzi, M. (2000) AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur. J. Biochem. 267, 61266133
  • 31
    Montemartini, M., Nogoceke, E., Singh, M., Steinert, P., Flohe, L., Kalisz, H.M. (1998) Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J. Biol. Chem. 273, 48644871DOI: 10.1074/jbc.273.9.4864