메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Catalytic properties of the isolated diaphorase fragment of the NAD +-reducing [NiFe]-hydrogenase from Ralstonia eutropha

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; FLAVINE MONONUCLEOTIDE; NICKEL IRON HYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SOLUBLE DEHYDROGENASE; UNCLASSIFIED DRUG; HYDROGENASE; NICKEL-IRON HYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 80053898681     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025939     Document Type: Article
Times cited : (42)

References (60)
  • 1
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory Complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich T, Scheide D, (2000) The respiratory Complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett 479: 1-5.
    • (2000) FEBS Lett , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 2
    • 0037422404 scopus 로고    scopus 로고
    • Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups
    • Albracht SPJ, van der Linden E, Faber BW, (2003) Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups. Biochim Biophys Acta 1557: 41-49.
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 41-49
    • Albracht, S.P.J.1    van der Linden, E.2    Faber, B.W.3
  • 3
    • 55249110895 scopus 로고    scopus 로고
    • Genomic view of energy metabolism in Ralstonia eutropha H16
    • Cramm R, (2009) Genomic view of energy metabolism in Ralstonia eutropha H16. J Mol Microbiol Biotechnol 16: 38-52.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 38-52
    • Cramm, R.1
  • 4
    • 33744503148 scopus 로고    scopus 로고
    • [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation
    • Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, et al. (2005) [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation. J Mol Microbiol Biotechnol 10: 181-196.
    • (2005) J Mol Microbiol Biotechnol , vol.10 , pp. 181-196
    • Burgdorf, T.1    Lenz, O.2    Buhrke, T.3    van der Linden, E.4    Jones, A.K.5
  • 5
    • 19944431547 scopus 로고    scopus 로고
    • Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy
    • Burgdorf T, Löscher S, Liebisch P, van der Linden E, Galander M, et al. (2005) Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy. J Am Chem Soc 127: 576-592.
    • (2005) J Am Chem Soc , vol.127 , pp. 576-592
    • Burgdorf, T.1    Löscher, S.2    Liebisch, P.3    van der Linden, E.4    Galander, M.5
  • 6
    • 20244376022 scopus 로고    scopus 로고
    • The soluble NAD+-reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH
    • Burgdorf T, van der Linden E, Bernhard M, Yin QY, Back JW, et al. (2005) The soluble NAD+-reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH. J Bacteriol 187: 3122-3132.
    • (2005) J Bacteriol , vol.187 , pp. 3122-3132
    • Burgdorf, T.1    van der Linden, E.2    Bernhard, M.3    Yin, Q.Y.4    Back, J.W.5
  • 7
    • 0017110320 scopus 로고
    • Purification and properties of Soluble Hydrogenase from Alcaligenes eutrophus H16
    • Schneider K, Schlegel HG, (1976) Purification and properties of Soluble Hydrogenase from Alcaligenes eutrophus H16. Biochim Biophys Acta 452: 66-80.
    • (1976) Biochim Biophys Acta , vol.452 , pp. 66-80
    • Schneider, K.1    Schlegel, H.G.2
  • 8
    • 32444440595 scopus 로고    scopus 로고
    • An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties
    • van der Linden E, Burgdorf T, de Lacey AL, Buhrke T, Scholte M, et al. (2006) An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties. J Biol Inorg Chem 11: 247-260.
    • (2006) J Biol Inorg Chem , vol.11 , pp. 247-260
    • van der Linden, E.1    Burgdorf, T.2    de Lacey, A.L.3    Buhrke, T.4    Scholte, M.5
  • 9
    • 0021173250 scopus 로고
    • Hydrogen evolution by strictly aerobic hydrogen bacteria under anaerobic conditions
    • Kuhn M, Steinbüchel A, Schlegel HG, (1984) Hydrogen evolution by strictly aerobic hydrogen bacteria under anaerobic conditions. J Bacteriol 159: 633-639.
    • (1984) J Bacteriol , vol.159 , pp. 633-639
    • Kuhn, M.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 10
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis
    • Appel J, Phunpruch S, Steinmüller K, Schulz R, (2000) The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis. Arch Microbiol 173: 333-338.
    • (2000) Arch Microbiol , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 11
    • 28044470050 scopus 로고    scopus 로고
    • Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels
    • Vincent KA, Cracknell JA, Lenz O, Zebger I, Friedrich B, et al. (2005) Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. Proc Natl Acad Sci USA 102: 16951-16954.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16951-16954
    • Vincent, K.A.1    Cracknell, J.A.2    Lenz, O.3    Zebger, I.4    Friedrich, B.5
  • 12
    • 77952566611 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance
    • Pandelia ME, Fourmond V, Tron-Infossi P, Lojou E, Bertrand P, et al. (2010) Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance. J Am Chem Soc 132: 6991-7004.
    • (2010) J Am Chem Soc , vol.132 , pp. 6991-7004
    • Pandelia, M.E.1    Fourmond, V.2    Tron-Infossi, P.3    Lojou, E.4    Bertrand, P.5
  • 13
    • 77950503486 scopus 로고    scopus 로고
    • How Escherichia coli is equipped to oxidize hydrogen under different redox conditions
    • Lukey MJ, Parkin A, Roessler MM, Murphy BJ, Harmer J, et al. (2010) How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. J Biol Chem 285: 3928-3938.
    • (2010) J Biol Chem , vol.285 , pp. 3928-3938
    • Lukey, M.J.1    Parkin, A.2    Roessler, M.M.3    Murphy, B.J.4    Harmer, J.5
  • 14
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus
    • Sazanov LA, Hinchliffe P, (2006) Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus. Science 311: 1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 15
    • 1342343929 scopus 로고    scopus 로고
    • Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha
    • van der Linden E, Faber BW, Bleijlevens B, Burgdorf T, Bernhard M, et al. (2004) Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha. Eur J Biochem 271: 801-808.
    • (2004) Eur J Biochem , vol.271 , pp. 801-808
    • van der Linden, E.1    Faber, B.W.2    Bleijlevens, B.3    Burgdorf, T.4    Bernhard, M.5
  • 16
    • 79951900196 scopus 로고    scopus 로고
    • The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha- insights into catalysis and redox interconversions
    • Lauterbach L, Liu JA, Horch M, Hummel P, Schwarze A, et al. (2011) The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha- insights into catalysis and redox interconversions. Eur J Inorg Chem 2011: 1067-1079.
    • (2011) Eur J Inorg Chem , vol.2011 , pp. 1067-1079
    • Lauterbach, L.1    Liu, J.A.2    Horch, M.3    Hummel, P.4    Schwarze, A.5
  • 17
    • 0021753750 scopus 로고
    • Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b
    • Schneider K, Cammack R, Schlegel HG, (1984) Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b. Eur J Biochem 142: 75-84.
    • (1984) Eur J Biochem , vol.142 , pp. 75-84
    • Schneider, K.1    Cammack, R.2    Schlegel, H.G.3
  • 18
    • 0021381108 scopus 로고
    • Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1b
    • Schneider K, Schlegel HG, Jochim K, (1984) Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1b. Eur J Biochem 138: 533-541.
    • (1984) Eur J Biochem , vol.138 , pp. 533-541
    • Schneider, K.1    Schlegel, H.G.2    Jochim, K.3
  • 19
    • 0026011904 scopus 로고
    • Structural aspects of the soluble NAD-Dependent hydrogenase isolated from Alcaligenes eutrophus H16 and from Nocardia opaca 1b
    • Johannssen W, Gerberding H, Rohde M, Zaborosch C, Mayer F, (1991) Structural aspects of the soluble NAD-Dependent hydrogenase isolated from Alcaligenes eutrophus H16 and from Nocardia opaca 1b. Arch Microbiol 155: 303-308.
    • (1991) Arch Microbiol , vol.155 , pp. 303-308
    • Johannssen, W.1    Gerberding, H.2    Rohde, M.3    Zaborosch, C.4    Mayer, F.5
  • 20
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP, (2009) How mitochondria produce reactive oxygen species. Biochem J 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 21
    • 0019396561 scopus 로고
    • Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16
    • Schneider K, Schlegel HG, (1981) Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16. Biochem J 193: 99-107.
    • (1981) Biochem J , vol.193 , pp. 99-107
    • Schneider, K.1    Schlegel, H.G.2
  • 22
    • 41149100550 scopus 로고    scopus 로고
    • Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria
    • Esterhazy D, King MS, Yakovlev G, Hirst J, (2008) Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria. Biochemistry 47: 3964-3971.
    • (2008) Biochemistry , vol.47 , pp. 3964-3971
    • Esterhazy, D.1    King, M.S.2    Yakovlev, G.3    Hirst, J.4
  • 23
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory Complex I
    • Hinchliffe P, Sazanov LA, (2005) Organization of iron-sulfur clusters in respiratory Complex I. Science 309: 771-774.
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 24
    • 0031886480 scopus 로고    scopus 로고
    • Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Massanz C, Schmidt S, Friedrich B, (1998) Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus. J Bacteriol 180: 1023-1029.
    • (1998) J Bacteriol , vol.180 , pp. 1023-1029
    • Massanz, C.1    Schmidt, S.2    Friedrich, B.3
  • 25
    • 0018137794 scopus 로고
    • Identification and quantitative determination of flavin component of soluble hydrogenase from Alcaligenes eutrophus
    • Schneider K, Schlegel HG, (1978) Identification and quantitative determination of flavin component of soluble hydrogenase from Alcaligenes eutrophus. Biochem Biophys Res Commun 84: 564-571.
    • (1978) Biochem Biophys Res Commun , vol.84 , pp. 564-571
    • Schneider, K.1    Schlegel, H.G.2
  • 26
    • 57449089412 scopus 로고    scopus 로고
    • Heterologous production, isolation, characterization and crystallization of a soluble fragment of the NADH:ubiquinone oxidoreductase (Complex I) from Aquifex aeolicus
    • Kohlstadt M, Dorner K, Labatzke R, Koc C, Hielscher R, et al. (2008) Heterologous production, isolation, characterization and crystallization of a soluble fragment of the NADH:ubiquinone oxidoreductase (Complex I) from Aquifex aeolicus. Biochemistry 47: 13036-13045.
    • (2008) Biochemistry , vol.47 , pp. 13036-13045
    • Kohlstadt, M.1    Dorner, K.2    Labatzke, R.3    Koc, C.4    Hielscher, R.5
  • 27
    • 0035685613 scopus 로고    scopus 로고
    • Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family
    • Zhao T, Cruz F, Ferry JG, (2001) Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family. J Bacteriol 183: 6225-6233.
    • (2001) J Bacteriol , vol.183 , pp. 6225-6233
    • Zhao, T.1    Cruz, F.2    Ferry, J.G.3
  • 28
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (Complex I) from Escherichia coli
    • Braun M, Bungert S, Friedrich T, (1998) Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (Complex I) from Escherichia coli. Biochemistry 37: 1861-1867.
    • (1998) Biochemistry , vol.37 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 30
    • 0020473231 scopus 로고
    • Resolution of mitochondrial NADH dehydrogenase and isolation of 2 iron sulfur proteins
    • Ragan CI, Galante YM, Hatefi Y, Ohnishi T, (1982) Resolution of mitochondrial NADH dehydrogenase and isolation of 2 iron sulfur proteins. Biochemistry 21: 590-594.
    • (1982) Biochemistry , vol.21 , pp. 590-594
    • Ragan, C.I.1    Galante, Y.M.2    Hatefi, Y.3    Ohnishi, T.4
  • 31
    • 0017148370 scopus 로고
    • Interaction of phenols with old yellow enzyme-physical evidence for charge-transfer complexes
    • Abramovitz AS, Massey V, (1976) Interaction of phenols with old yellow enzyme-physical evidence for charge-transfer complexes. J Biol Chem 251: 5327-5336.
    • (1976) J Biol Chem , vol.251 , pp. 5327-5336
    • Abramovitz, A.S.1    Massey, V.2
  • 32
    • 73149096726 scopus 로고    scopus 로고
    • Kinetic characterization of xenobiotic reductase A from Pseudomonas putida 86
    • Spiegelhauer O, Dickert F, Mende S, Niks D, Hille R, et al. (2009) Kinetic characterization of xenobiotic reductase A from Pseudomonas putida 86. Biochemistry 48: 11412-11420.
    • (2009) Biochemistry , vol.48 , pp. 11412-11420
    • Spiegelhauer, O.1    Dickert, F.2    Mende, S.3    Niks, D.4    Hille, R.5
  • 33
    • 55749110597 scopus 로고    scopus 로고
    • NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • Cotruvo JA, Stubbe J, (2008) NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Proc Natl Acad Sci USA 105: 14383-14388.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14383-14388
    • Cotruvo, J.A.1    Stubbe, J.2
  • 34
    • 58249116720 scopus 로고    scopus 로고
    • Direct observation of a photoinduced radical pair in a cryptochrome blue-light photoreceptor
    • Biskup T, Schleicher E, Okafuji A, Link G, Hitomi K, et al. (2009) Direct observation of a photoinduced radical pair in a cryptochrome blue-light photoreceptor. Angew Chem Int Ed 48: 404-407.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 404-407
    • Biskup, T.1    Schleicher, E.2    Okafuji, A.3    Link, G.4    Hitomi, K.5
  • 35
    • 0013954466 scopus 로고
    • On existence of spectrally distinct classes of flavoprotein semiquinones. A new method for quantitative production of flavoprotein semiquinones
    • Massey V, Palmer G, (1966) On existence of spectrally distinct classes of flavoprotein semiquinones. A new method for quantitative production of flavoprotein semiquinones. Biochemistry 5: 3181-3189.
    • (1966) Biochemistry , vol.5 , pp. 3181-3189
    • Massey, V.1    Palmer, G.2
  • 36
    • 52749089381 scopus 로고    scopus 로고
    • Spectroscopic investigation of flavoproteins: Mechanistic differences between (electro)chemical and photochemical reduction and oxidation
    • Nöll G, (2008) Spectroscopic investigation of flavoproteins: Mechanistic differences between (electro)chemical and photochemical reduction and oxidation. J Photochem Photobiol A: Chem 200: 34-38.
    • (2008) J Photochem Photobiol A: Chem , vol.200 , pp. 34-38
    • Nöll, G.1
  • 37
    • 0015951494 scopus 로고
    • Fluorescence and optical characteristics of reduced flavines and flavoproteins
    • Ghisla S, Massey V, Lhoste JM, Mayhew SG, (1974) Fluorescence and optical characteristics of reduced flavines and flavoproteins. Biochemistry 13: 589-597.
    • (1974) Biochemistry , vol.13 , pp. 589-597
    • Ghisla, S.1    Massey, V.2    Lhoste, J.M.3    Mayhew, S.G.4
  • 39
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett BD, Kimball EH, Gao M, Osterhout R, Van Dien SJ, et al. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5: 593-599.
    • (2009) Nat Chem Biol , vol.5 , pp. 593-599
    • Bennett, B.D.1    Kimball, E.H.2    Gao, M.3    Osterhout, R.4    van Dien, S.J.5
  • 41
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory Complex I
    • Berrisford JM, Sazanov LA, (2009) Structural basis for the mechanism of respiratory Complex I. J Biol Chem 284: 29773-29783.
    • (2009) J Biol Chem , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 42
    • 0242573082 scopus 로고    scopus 로고
    • Proton translocation by transhydrogenase
    • Jackson JB, (2003) Proton translocation by transhydrogenase. FEBS Lett 555: 176-177.
    • (2003) FEBS Lett , vol.555 , pp. 176-177
    • Jackson, J.B.1
  • 43
    • 73849114263 scopus 로고    scopus 로고
    • Towards the molecular mechanism of respiratory Complex I
    • Hirst J, (2010) Towards the molecular mechanism of respiratory Complex I. Biochem J 425: 327-339.
    • (2010) Biochem J , vol.425 , pp. 327-339
    • Hirst, J.1
  • 45
    • 0345059204 scopus 로고    scopus 로고
    • The mitochondrial and prokaryotic proton-trans locating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites
    • Grivennikova VG, Roth R, Zakharova NV, Hagerhall C, Vinogradov AD, (2003) The mitochondrial and prokaryotic proton-trans locating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites. Biochim Biophys Acta 1607: 79-90.
    • (2003) Biochim Biophys Acta , vol.1607 , pp. 79-90
    • Grivennikova, V.G.1    Roth, R.2    Zakharova, N.V.3    Hagerhall, C.4    Vinogradov, A.D.5
  • 46
    • 33947370457 scopus 로고    scopus 로고
    • The flavoprotein subcomplex of Complex I (NADH:ubiquinone oxidoreductase) from bovine heart mitochondria: insights into the mechanisms of NADH oxidation and NAD+ reduction from protein film voltammetry
    • Barker CD, Reda T, Hirst J, (2007) The flavoprotein subcomplex of Complex I (NADH:ubiquinone oxidoreductase) from bovine heart mitochondria: insights into the mechanisms of NADH oxidation and NAD+ reduction from protein film voltammetry. Biochemistry 46: 3454-3464.
    • (2007) Biochemistry , vol.46 , pp. 3454-3464
    • Barker, C.D.1    Reda, T.2    Hirst, J.3
  • 47
    • 0027233474 scopus 로고
    • Reductive inactivation of the mitochondrial 3 subunit NADH dehydrogenase
    • Sled VD, Vinogradov AD, (1993) Reductive inactivation of the mitochondrial 3 subunit NADH dehydrogenase. Biochim Biophys Acta 1143: 199-203.
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 199-203
    • Sled, V.D.1    Vinogradov, A.D.2
  • 48
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (Complex I) from bovine heart mitochondria
    • Kussmaul L, Hirst J, (2006) The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (Complex I) from bovine heart mitochondria. Proc Natl Acad Sci USA 103: 7607-7612.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 49
    • 52949114593 scopus 로고    scopus 로고
    • Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of Complex I from Escherichia coli and Thermus thermophilus
    • Berrisford JM, Thompson CJ, Sazanov LA, (2008) Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of Complex I from Escherichia coli and Thermus thermophilus. Biochemistry 47: 10262-10270.
    • (2008) Biochemistry , vol.47 , pp. 10262-10270
    • Berrisford, J.M.1    Thompson, C.J.2    Sazanov, L.A.3
  • 50
    • 0029086244 scopus 로고
    • A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli
    • Imlay JA, (1995) A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli. J Biol Chem 270: 19767-19777.
    • (1995) J Biol Chem , vol.270 , pp. 19767-19777
    • Imlay, J.A.1
  • 51
    • 78349301233 scopus 로고    scopus 로고
    • Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy
    • Horch M, Lauterbach L, Saggu M, Hildebrandt P, Lendzian F, et al. (2010) Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy. Angew Chem Int Ed 49: 8026-8029.
    • (2010) Angew Chem Int Ed , vol.49 , pp. 8026-8029
    • Horch, M.1    Lauterbach, L.2    Saggu, M.3    Hildebrandt, P.4    Lendzian, F.5
  • 52
    • 8744311816 scopus 로고    scopus 로고
    • The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel
    • Bleijlevens B, Buhrke T, van der Linden E, Friedrich B, Albracht SPJ, (2004) The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel. J Biol Chem 279: 46686-46691.
    • (2004) J Biol Chem , vol.279 , pp. 46686-46691
    • Bleijlevens, B.1    Buhrke, T.2    van der Linden, E.3    Friedrich, B.4    Albracht, S.P.J.5
  • 53
    • 0033956391 scopus 로고    scopus 로고
    • Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha
    • Happe RP, Roseboom W, Egert G, Friedrich CG, Massanz C, et al. (2000) Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha. FEBS Lett 466: 259-263.
    • (2000) FEBS Lett , vol.466 , pp. 259-263
    • Happe, R.P.1    Roseboom, W.2    Egert, G.3    Friedrich, C.G.4    Massanz, C.5
  • 54
    • 3943058946 scopus 로고    scopus 로고
    • The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
    • van der Linden E, Burgdorf T, Bernhard M, Bleijlevens B, Friedrich B, et al. (2004) The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen. J Biol Inorg Chem 9: 616-626.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 616-626
    • van der Linden, E.1    Burgdorf, T.2    Bernhard, M.3    Bleijlevens, B.4    Friedrich, B.5
  • 55
    • 0031747821 scopus 로고    scopus 로고
    • Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes
    • Schwartz E, Gerischer U, Friedrich B, (1998) Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes. J Bacteriol 180: 3197-3204.
    • (1998) J Bacteriol , vol.180 , pp. 3197-3204
    • Schwartz, E.1    Gerischer, U.2    Friedrich, B.3
  • 56
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford MM, (1976) Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 57
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of Bacteriophage-T4
    • Laemmli UK, (1970) Cleavage of structural proteins during assembly of head of Bacteriophage-T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 58
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets- procedure and some applications
    • Towbin H, Staehelin T, Gordon J, (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets- procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 59
    • 70350462622 scopus 로고    scopus 로고
    • Two essential arginine residues in the T components of energy-coupling factor transporters
    • Neubauer O, Alfandega A, Schoknecht J, Sternberg U, Pohlmann A, et al. (2009) Two essential arginine residues in the T components of energy-coupling factor transporters. J Bacteriol 191: 6482-6488.
    • (2009) J Bacteriol , vol.191 , pp. 6482-6488
    • Neubauer, O.1    Alfandega, A.2    Schoknecht, J.3    Sternberg, U.4    Pohlmann, A.5
  • 60
    • 0019419819 scopus 로고
    • Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus
    • Friedrich B, Heine E, Finck A, Friedrich CG, (1981) Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus. J Bacteriol 145: 1144-1149.
    • (1981) J Bacteriol , vol.145 , pp. 1144-1149
    • Friedrich, B.1    Heine, E.2    Finck, A.3    Friedrich, C.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.