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Volumn 290, Issue 1, 2009, Pages 114-120

Purification and biochemical characterization of a membrane-bound [NiFe]-hydrogenase from a hydrogen-oxidizing, lithotrophic bacterium, Hydrogenophaga sp. AH-24

Author keywords

Electron paramagnetic resonance; Hydrogen oxidizing bacterium; Hydrogenophaga sp. AH 24; Kinetic constants; Membrane bound NiFe hydrogenase; Purification

Indexed keywords

HYDROGEN; HYDROGENASE; MEMBRANE ENZYME; METHYLENE BLUE; PROTEIN SUBUNIT;

EID: 57449119095     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2008.01417.x     Document Type: Article
Times cited : (14)

References (27)
  • 1
    • 0018359364 scopus 로고
    • Properties of the solubilized membrane-bound hydrogenase from the photosynthetic bacterium Rhodospirillum rubrum
    • Adams MW Hall DO (1979) Properties of the solubilized membrane-bound hydrogenase from the photosynthetic bacterium Rhodospirillum rubrum. Arch Biochem Biophys 195 : 288 299.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 288-299
    • Adams, M.W.1    Hall, D.O.2
  • 2
    • 0021194792 scopus 로고
    • The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. a comparison with hydrogenase I
    • Adams MW Mortenson LE (1984) The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I. J Biol Chem 259 : 7045 7055.
    • (1984) J Biol Chem , vol.259 , pp. 7045-7055
    • Adams, M.W.1    Mortenson, L.E.2
  • 3
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht SP (1994) Nickel hydrogenases: in search of the active site. Biochim Biophys Acta 1188 : 167 204.
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.1
  • 4
    • 0030795942 scopus 로고    scopus 로고
    • Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16
    • Bernhard M, Benelli B, Hochkoeppler A, Zannoni D Friedrich B (1997) Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16. Eur J Biochem 248 : 179 186.
    • (1997) Eur J Biochem , vol.248 , pp. 179-186
    • Bernhard, M.1    Benelli, B.2    Hochkoeppler, A.3    Zannoni, D.4    Friedrich, B.5
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 : 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 21244441201 scopus 로고    scopus 로고
    • 2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site
    • 2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site. J Biol Chem 280 : 23791 23796.
    • (2005) J Biol Chem , vol.280 , pp. 23791-23796
    • Buhrke, T.1    Lenz, O.2    Krauss, N.3    Friedrich, B.4
  • 10
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps JC, Volbeda A, Cavazza C Nicolet Y (2007) Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 107 : 4273 4303.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 11
    • 33746889396 scopus 로고    scopus 로고
    • Hyperthermostable and oxygen resistant hydrogenases from a hyperthermophilic bacterium Aquifex aeolicus: Physicochemical properties
    • Guiral M, Tron P, Belle V, Aubert C, Léger C, Guigliarelli B Giudici-Orticoni MT (2006) Hyperthermostable and oxygen resistant hydrogenases from a hyperthermophilic bacterium Aquifex aeolicus: physicochemical properties. Int J Hydrogen Energ 31 : 1424 1431.
    • (2006) Int J Hydrogen Energ , vol.31 , pp. 1424-1431
    • Guiral, M.1    Tron, P.2    Belle, V.3    Aubert, C.4    Léger, C.5    Guigliarelli, B.6    Giudici-Orticoni, M.T.7
  • 12
    • 0024602984 scopus 로고
    • The membrane-bound hydrogenase from Paracoccus denitrificans: Purification and molecular characterization
    • Knüttel K, Schneider K, Schlegel HG Müller A (1989) The membrane-bound hydrogenase from Paracoccus denitrificans: purification and molecular characterization. Eur J Biochem 179 : 101 108.
    • (1989) Eur J Biochem , vol.179 , pp. 101-108
    • Knüttel, K.1    Schneider, K.2    Schlegel, H.G.3    Müller, A.4
  • 13
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques
    • Lubitz W, Reijerse E van Gastel M (2007) [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques. Chem Rev 107 : 4331 4365.
    • (2007) Chem Rev , vol.107 , pp. 4331-4365
    • Lubitz, W.1    Reijerse, E.2    Van Gastel, M.3
  • 14
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262 : 10035 10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 15
    • 3543131919 scopus 로고    scopus 로고
    • Biotechnological applications of hydrogenases
    • Mertens R Liese A (2004) Biotechnological applications of hydrogenases. Curr Opin Biotech 15 : 343 348.
    • (2004) Curr Opin Biotech , vol.15 , pp. 343-348
    • Mertens, R.1    Liese, A.2
  • 16
    • 0026326459 scopus 로고
    • Growth characteristics and high cell-density cultivation of a marine obligately chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenovibrio marinus strain MH-110 under a continuous gas-flow system
    • Nishihara H, Igarashi Y Kodama T (1991) Growth characteristics and high cell-density cultivation of a marine obligately chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenovibrio marinus strain MH-110 under a continuous gas-flow system. J Ferment Bioeng 72 : 358 361.
    • (1991) J Ferment Bioeng , vol.72 , pp. 358-361
    • Nishihara, H.1    Igarashi, Y.2    Kodama, T.3
  • 17
    • 0031587791 scopus 로고    scopus 로고
    • Characterization of an extremely thermophilic and oxygen-stable membrane-bound hydrogenase from a marine hydrogen-oxidizing bacterium Hydrogenovibrio marinus
    • Nishihara H, Miyashita Y, Aoyama K, Kodama T, Igarashi Y Takamura Y (1997) Characterization of an extremely thermophilic and oxygen-stable membrane-bound hydrogenase from a marine hydrogen-oxidizing bacterium Hydrogenovibrio marinus. Biochem Bioph Res Co 232 : 766 770.
    • (1997) Biochem Bioph Res Co , vol.232 , pp. 766-770
    • Nishihara, H.1    Miyashita, Y.2    Aoyama, K.3    Kodama, T.4    Igarashi, Y.5    Takamura, Y.6
  • 18
    • 85007878384 scopus 로고
    • Purification and characterization of membrane-bound hydrogenase from a thermophilic hydrogen-oxidizing bacterium, Pseudomonas hydrogenothermophila strain TH-1
    • Ono T, Ishii M, Yoon K-S, Igarashi Y Kodama T (1995) Purification and characterization of membrane-bound hydrogenase from a thermophilic hydrogen-oxidizing bacterium, Pseudomonas hydrogenothermophila strain TH-1. Biosci Biotech Bioch 59 : 917 919.
    • (1995) Biosci Biotech Bioch , vol.59 , pp. 917-919
    • Ono, T.1    Ishii, M.2    Yoon, K.-S.3    Igarashi, Y.4    Kodama, T.5
  • 19
    • 0010431917 scopus 로고
    • ESR properties of membrane-bound hydrogenases from aerobic hydrogen bacteria
    • Schneider K, Patil DS Cammack R (1983) ESR properties of membrane-bound hydrogenases from aerobic hydrogen bacteria. Biochim Biophys Acta 748 : 353 361.
    • (1983) Biochim Biophys Acta , vol.748 , pp. 353-361
    • Schneider, K.1    Patil, D.S.2    Cammack, R.3
  • 21
    • 0021826804 scopus 로고
    • Electron paramagnetic resonance studies of the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from Desulfovibrio gigas
    • Teixeira M, Moura I, Xavier AV, Huynh BH, DerVartanian DV, Peck HD Jr., LeGall J Moura JJ (1985) Electron paramagnetic resonance studies of the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from Desulfovibrio gigas. J Biol Chem 260 : 8942 8950.
    • (1985) J Biol Chem , vol.260 , pp. 8942-8950
    • Teixeira, M.1    Moura, I.2    Xavier, A.V.3    Huynh, B.H.4    Dervartanian, D.V.5    Peck Jr., H.D.6    Legall, J.7    Moura, J.J.8
  • 24
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais PM Billoud B (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 107 : 4206 4272.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 26
    • 0035941189 scopus 로고    scopus 로고
    • Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum
    • Yoon K-S, Bobst C, Hemann CF, Hille R Tabita FR (2001) Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum. J Biol Chem 276 : 44027 44036.
    • (2001) J Biol Chem , vol.276 , pp. 44027-44036
    • Yoon, K.-S.1    Bobst, C.2    Hemann, C.F.3    Hille, R.4    Tabita, F.R.5
  • 27
    • 36749103763 scopus 로고    scopus 로고
    • Isolation and characterization of a new facultatively autotrophic hydrogen-oxidizing Betaproteobacterium, Hydrogenophaga sp. AH-24
    • Yoon K-S, Tsukada N, Sakai Y, Ishii M, Igarashi Y Nishihara H (2008) Isolation and characterization of a new facultatively autotrophic hydrogen-oxidizing Betaproteobacterium, Hydrogenophaga sp. AH-24. FEMS Microbiol Lett 278 : 94 100.
    • (2008) FEMS Microbiol Lett , vol.278 , pp. 94-100
    • Yoon, K.-S.1    Tsukada, N.2    Sakai, Y.3    Ishii, M.4    Igarashi, Y.5    Nishihara, H.6


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