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Volumn 275, Issue 21, 2008, Pages 5355-5366

Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O

Author keywords

Electron microscopy; H2O producing; Hexameric ring structure; NADH oxidase; Thermophilic archaeon

Indexed keywords

CYSTEINE; FLAVINE ADENINE NUCLEOTIDE; HYDROGEN PEROXIDE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; WATER;

EID: 53849112300     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06665.x     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S Imanaka T (2005) Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res 15, 352 363.
    • (2005) Genome Res , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 2
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney FE Jr., Verhagen MF, Cui X Adams MW (1999) Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286, 306 309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney Jr., F.E.1    Verhagen, M.F.2    Cui, X.3    Adams, M.W.4
  • 4
    • 10644295071 scopus 로고    scopus 로고
    • Flavoprotein disulfide reductases: Advances in chemistry and function
    • Argyrou A Blanchard JS (2004) Flavoprotein disulfide reductases: advances in chemistry and function. Prog Nucleic Acid Res Mol Biol 78, 89 142.
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 89-142
    • Argyrou, A.1    Blanchard, J.S.2
  • 5
    • 0039011740 scopus 로고    scopus 로고
    • A NAD(P)H oxidase isolated from the archaeon Sulfolobus solfataricus is not homologous with another NADH oxidase present in the same microorganism
    • Arcari P, Masullo L, Masullo M, Catanzano F Bocchini V (2000) A NAD(P)H oxidase isolated from the archaeon Sulfolobus solfataricus is not homologous with another NADH oxidase present in the same microorganism. J Biol Chem 275, 895 900.
    • (2000) J Biol Chem , vol.275 , pp. 895-900
    • Arcari, P.1    Masullo, L.2    Masullo, M.3    Catanzano, F.4    Bocchini, V.5
  • 6
    • 1842637847 scopus 로고    scopus 로고
    • 2O-forming NADH oxidase from Clostridium aminovalericum: Existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria
    • 2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. Arch Microbiol 181, 324 330.
    • (2004) Arch Microbiol , vol.181 , pp. 324-330
    • Kawasaki, S.1    Ishikura, J.2    Chiba, D.3    Nishino, T.4    Niimura, Y.5
  • 7
    • 0035209047 scopus 로고    scopus 로고
    • 2-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus
    • 2-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus. J Bacteriol 183, 7007 7016.
    • (2001) J Bacteriol , vol.183 , pp. 7007-7016
    • Reed, D.W.1    Millstein, J.2    Hartzell, P.L.3
  • 8
    • 0033811613 scopus 로고    scopus 로고
    • Hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus
    • Niimura Y, Nishiyama Y, Saito D, Tsuji H, Hidaka M, Miyaji T, Watanabe T Massey V (2000) Hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanus. J Bacteriol 182, 5046 5051.
    • (2000) J Bacteriol , vol.182 , pp. 5046-5051
    • Niimura, Y.1    Nishiyama, Y.2    Saito, D.3    Tsuji, H.4    Hidaka, M.5    Miyaji, T.6    Watanabe, T.7    Massey, V.8
  • 10
    • 34247863804 scopus 로고    scopus 로고
    • Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima
    • Yang X Ma K (2007) Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 189, 3312 3317.
    • (2007) J Bacteriol , vol.189 , pp. 3312-3317
    • Yang, X.1    Ma, K.2
  • 14
    • 0027288794 scopus 로고
    • Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI
    • Franklund CV, Baron SF Hylemon PB (1993) Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI. J Bacteriol 175, 3002 3012.
    • (1993) J Bacteriol , vol.175 , pp. 3002-3012
    • Franklund, C.V.1    Baron, S.F.2    Hylemon, P.B.3
  • 15
    • 0026641959 scopus 로고
    • A thermostable NADH oxidase from anaerobic extreme thermophiles
    • Maeda K, Truscott K, Liu XL Scopes RK (1992) A thermostable NADH oxidase from anaerobic extreme thermophiles. Biochem J 284, 551 555.
    • (1992) Biochem J , vol.284 , pp. 551-555
    • Maeda, K.1    Truscott, K.2    Liu, X.L.3    Scopes, R.K.4
  • 16
    • 0036278156 scopus 로고    scopus 로고
    • Purification and characterization of an NADH oxidase from Eubacterium ramulus
    • Herles C, Braune A Blaut M (2002) Purification and characterization of an NADH oxidase from Eubacterium ramulus. Arch Microbiol 178, 71 74.
    • (2002) Arch Microbiol , vol.178 , pp. 71-74
    • Herles, C.1    Braune, A.2    Blaut, M.3
  • 18
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym O Eisenberg D (2001) Sequence-structure analysis of FAD-containing proteins. Protein Sci 10, 1712 1728.
    • (2001) Protein Sci , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 19
    • 0026795398 scopus 로고
    • Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1
    • Ross RP Claiborne A (1992) Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. J Mol Biol 227, 658 671.
    • (1992) J Mol Biol , vol.227 , pp. 658-671
    • Ross, R.P.1    Claiborne, A.2
  • 20
    • 0026059349 scopus 로고
    • Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1
    • Ross RP Claiborne A (1991) Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. J Mol Biol 221, 857 871.
    • (1991) J Mol Biol , vol.221 , pp. 857-871
    • Ross, R.P.1    Claiborne, A.2
  • 21
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: A novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
    • Lopez de Felipe F, Kleerebezem M, de Vos WM Hugenholtz J (1998) Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J Bacteriol 180, 3804 3808.
    • (1998) J Bacteriol , vol.180 , pp. 3804-3808
    • Lopez De Felipe, F.1    Kleerebezem, M.2    De Vos, W.M.3    Hugenholtz, J.4
  • 22
    • 33745104824 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis
    • Kuzu M, Niefind K, Hummel W Schomburg D (2005) Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis. Acta Crystallogr Sect F Struct Biol Cryst Commun 61, 528 530.
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , pp. 528-530
    • Kuzu, M.1    Niefind, K.2    Hummel, W.3    Schomburg, D.4
  • 24
    • 0036295232 scopus 로고    scopus 로고
    • Electron cryo-microscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum
    • Rockel B, Jakana J, Chiu W Baumeister W (2002) Electron cryo-microscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum. J Mol Biol 317, 673 681.
    • (2002) J Mol Biol , vol.317 , pp. 673-681
    • Rockel, B.1    Jakana, J.2    Chiu, W.3    Baumeister, W.4
  • 26
    • 0242267926 scopus 로고    scopus 로고
    • Deflavination and reconstitution of flavoproteins
    • Hefti MH, Vervoort J van Berkel WJ (2003) Deflavination and reconstitution of flavoproteins. Eur J Biochem 270, 4227 4242.
    • (2003) Eur J Biochem , vol.270 , pp. 4227-4242
    • Hefti, M.H.1    Vervoort, J.2    Van Berkel, W.J.3
  • 27
    • 0024257933 scopus 로고
    • Large-scale preparation and reconstitution of apo-flavoproteins with special reference to butyryl-CoA dehydrogenase from Megasphaera elsdenii. Hydrophobic-interaction chromatography
    • Van Berkel WJ, Van den Berg WA Muller F (1988) Large-scale preparation and reconstitution of apo-flavoproteins with special reference to butyryl-CoA dehydrogenase from Megasphaera elsdenii. Hydrophobic-interaction chromatography. Eur J Biochem 178, 197 207.
    • (1988) Eur J Biochem , vol.178 , pp. 197-207
    • Van Berkel, W.J.1    Van Den Berg, W.A.2    Muller, F.3
  • 28
    • 0032537559 scopus 로고    scopus 로고
    • Oxygen reactivity of an NADH oxidase C42S mutant: Evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change
    • Mallett TC 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, 8790 8802.
    • (1998) Biochemistry , vol.37 , pp. 8790-8802
    • Mallett, T.C.1    Claiborne, A.2
  • 29
    • 0025996658 scopus 로고
    • Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 Å resolution
    • Stehle T, Ahmed SA, Claiborne A Schulz GE (1991) Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 Å resolution. J Mol Biol 221, 1325 1344.
    • (1991) J Mol Biol , vol.221 , pp. 1325-1344
    • Stehle, T.1    Ahmed, S.A.2    Claiborne, A.3    Schulz, G.E.4
  • 30
    • 0033986479 scopus 로고    scopus 로고
    • Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes
    • Gibson CM, Mallett TC, Claiborne A Caparon MG (2000) Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes. J Bacteriol 182, 448 455.
    • (2000) J Bacteriol , vol.182 , pp. 448-455
    • Gibson, C.M.1    Mallett, T.C.2    Claiborne, A.3    Caparon, M.G.4
  • 31
    • 0027197351 scopus 로고
    • Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas
    • Chen L, Liu MY, Legall J, Fareleira P, Santos H Xavier AV (1993) Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas. Eur J Biochem 216, 443 448.
    • (1993) Eur J Biochem , vol.216 , pp. 443-448
    • Chen, L.1    Liu, M.Y.2    Legall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 32
    • 0035319360 scopus 로고    scopus 로고
    • Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus
    • Sakuraba H, Takamatsu Y, Satomura T, Kawakami R Ohshima T (2001) Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus. Appl Environ Microbiol 67, 1470 1475.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1470-1475
    • Sakuraba, H.1    Takamatsu, Y.2    Satomura, T.3    Kawakami, R.4    Ohshima, T.5
  • 33
    • 22544440279 scopus 로고    scopus 로고
    • Thiol-disulphide interchange in tubulin: Kinetics and the effects on polymerization
    • Britto PJ, Knipling L, McPhie P Wolff J (2005) Thiol-disulphide interchange in tubulin: kinetics and the effects on polymerization. Biochem J 389, 549 558.
    • (2005) Biochem J , vol.389 , pp. 549-558
    • Britto, P.J.1    Knipling, L.2    McPhie, P.3    Wolff, J.4
  • 34
    • 0018650401 scopus 로고
    • Digital image processing: The Semper system
    • Saxton WO, Pitt TJ Horner M (1979) Digital image processing: the Semper system. Ultramicroscopy 4, 343 354.
    • (1979) Ultramicroscopy , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Horner, M.3
  • 35
    • 0029879294 scopus 로고    scopus 로고
    • The EM program package: A platform for image processing in biological electron microscopy
    • Hegerl R (1996) The EM program package: a platform for image processing in biological electron microscopy. J Struct Biol 116, 30 34.
    • (1996) J Struct Biol , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 37
    • 0034634334 scopus 로고    scopus 로고
    • Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
    • Kim KI, Cheong GW, Park SC, Ha JS, Woo KM, Choi SJ Chung CH (2000) Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. J Mol Biol 303, 655 666.
    • (2000) J Mol Biol , vol.303 , pp. 655-666
    • Kim, K.I.1    Cheong, G.W.2    Park, S.C.3    Ha, J.S.4    Woo, K.M.5    Choi, S.J.6    Chung, C.H.7
  • 39
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analyzing the images of biological macromolecules
    • Van Heel M Frank J (1981) Use of multivariate statistics in analyzing the images of biological macromolecules. Ultramicroscopy 6, 187 194.
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • Van Heel, M.1    Frank, J.2
  • 40
    • 0026261932 scopus 로고
    • Displacement field analysis: Calculation of distortion measures from displacement maps
    • Dürr R (1991) Displacement field analysis: calculation of distortion measures from displacement maps. Ultramicroscopy 38, 135 141.
    • (1991) Ultramicroscopy , vol.38 , pp. 135-141
    • Dürr, R.1


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