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Volumn 114, Issue 5, 2012, Pages 479-484

O 2-stable membrane-bound [NiFe]hydrogenase from a newly isolated Citrobacter sp. S-77

Author keywords

Citrobacter sp. S 77; Cytochrome b 560; H 2 oxidation; Kinetic parameters; Membrane bound NiFe hydrogenase; O 2 stability

Indexed keywords

16S RRNA GENE SEQUENCE; [NIFE]-HYDROGENASE; AEROBIC CONDITION; BIOCHEMICAL CHARACTERIZATION; CITROBACTER SP. S-77; CYTOCHROME B; CYTOPLASMIC MEMBRANE; ELECTRON ACCEPTOR; HETERODIMERS; HYDROGENASES; IN-VITRO; ISOLATED STRAINS; MEMBRANE-BOUND; METABOLIC PATHWAYS; PHYLOGENETIC ANALYSIS; SPECIFIC ACTIVITY;

EID: 84866364900     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.05.018     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais P.M., Billoud B. Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 2007, 107:4206-4272.
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 2
    • 0034150044 scopus 로고    scopus 로고
    • Purification and characterization of membrane-bound hydrogenase from Hydrogenobacter thermophilus strain TK-6, an obligately autotrophic, thermophilic, hydrogen-oxidizing bacterium
    • Ishii M., Takishita S., Iwasaki T., Peerapornpisal Y., Yoshino J., Kodama T., Igarashi Y. Purification and characterization of membrane-bound hydrogenase from Hydrogenobacter thermophilus strain TK-6, an obligately autotrophic, thermophilic, hydrogen-oxidizing bacterium. Biosci. Biotechnol. Biochem. 2000, 64:492-502.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 492-502
    • Ishii, M.1    Takishita, S.2    Iwasaki, T.3    Peerapornpisal, Y.4    Yoshino, J.5    Kodama, T.6    Igarashi, Y.7
  • 3
    • 0037369931 scopus 로고    scopus 로고
    • Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Kanai T., Ito S., Imanaka T. Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 2003, 185:1705-1711.
    • (2003) J. Bacteriol. , vol.185 , pp. 1705-1711
    • Kanai, T.1    Ito, S.2    Imanaka, T.3
  • 5
    • 3543131919 scopus 로고    scopus 로고
    • Biotechnological applications of hydrogenases
    • Mertens R., Liese A. Biotechnological applications of hydrogenases. Curr. Opin. Biotechnol. 2004, 15:343-348.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 343-348
    • Mertens, R.1    Liese, A.2
  • 6
    • 49049118534 scopus 로고    scopus 로고
    • Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis
    • Cracknell J.A., Vincent K.A., Armstrong F.A. Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. Chem. Rev. 2008, 108:2439-2461.
    • (2008) Chem. Rev. , vol.108 , pp. 2439-2461
    • Cracknell, J.A.1    Vincent, K.A.2    Armstrong, F.A.3
  • 9
    • 0034088342 scopus 로고    scopus 로고
    • Fabrication of an electrode-viologen-hydrogenase heterogeneous system and the electrochemical hydrogen evolution
    • Qian D.J., Nakamura C., Noda K., Zorin N.A., Miyake J. Fabrication of an electrode-viologen-hydrogenase heterogeneous system and the electrochemical hydrogen evolution. Appl. Biochem. Biotechnol. 2000, 84-86:409-418.
    • (2000) Appl. Biochem. Biotechnol. , pp. 409-418
    • Qian, D.J.1    Nakamura, C.2    Noda, K.3    Zorin, N.A.4    Miyake, J.5
  • 10
    • 0021172038 scopus 로고
    • Reactivation of the hydrogenase from Desulfovibrio gigas by hydrogen. Influence of redox potential
    • Lissolo T., Pulvin S., Thomas D. Reactivation of the hydrogenase from Desulfovibrio gigas by hydrogen. Influence of redox potential. J. Biol. Chem. 1984, 259:11725-11729.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11725-11729
    • Lissolo, T.1    Pulvin, S.2    Thomas, D.3
  • 11
    • 0018832417 scopus 로고
    • 2-stability of hydrogenase in the anaerobic bacterium Desulfovibrio vulgaris (hildenborough)
    • 2-stability of hydrogenase in the anaerobic bacterium Desulfovibrio vulgaris (hildenborough). FEMS Microbiol. Lett. 1980, 7:35-39.
    • (1980) FEMS Microbiol. Lett. , vol.7 , pp. 35-39
    • Van der Westen, H.M.1    Mayhew, S.G.2    Veeger, C.3
  • 12
    • 79955893150 scopus 로고    scopus 로고
    • Purification and characterization of a highly thermostable, oxygen-resistant, respiratory [NiFe]-hydrogenase from a marine, aerobic hydrogen-oxidizing bacterium Hydrogenovibrio marinus
    • Yoon K.S., Fukuda K., Fujisawa K., Nishihara H. Purification and characterization of a highly thermostable, oxygen-resistant, respiratory [NiFe]-hydrogenase from a marine, aerobic hydrogen-oxidizing bacterium Hydrogenovibrio marinus. Int. J. Hydrogen Energy 2011, 36:7081-7088.
    • (2011) Int. J. Hydrogen Energy , vol.36 , pp. 7081-7088
    • Yoon, K.S.1    Fukuda, K.2    Fujisawa, K.3    Nishihara, H.4
  • 13
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe-3S] cluster in the Oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Shomura Y., Yoon K.S., Nishihara H., Higuchi Y. Structural basis for a [4Fe-3S] cluster in the Oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 2011, 479:253-256.
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 15
    • 77957916530 scopus 로고    scopus 로고
    • The oxygen-tolerant hydrogenase I from Aquifex aeolicus weakly interacts with carbon monoxide: an electrochemical and time-resolved FTIR study
    • Pandelia M.E., Infossi P., Giudici-Orticoni M.T., Lubitz W. The oxygen-tolerant hydrogenase I from Aquifex aeolicus weakly interacts with carbon monoxide: an electrochemical and time-resolved FTIR study. Biochemistry 2010, 49:8873-8881.
    • (2010) Biochemistry , vol.49 , pp. 8873-8881
    • Pandelia, M.E.1    Infossi, P.2    Giudici-Orticoni, M.T.3    Lubitz, W.4
  • 16
    • 0019335261 scopus 로고
    • Competitive inhibition of the membrane-bound hydrogenase of Alcaligenes eutrophus by molecular oxygen
    • Schink B., Probst I. Competitive inhibition of the membrane-bound hydrogenase of Alcaligenes eutrophus by molecular oxygen. Biochem. Biophys. Res. Commun. 1980, 95:1563-1569.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1563-1569
    • Schink, B.1    Probst, I.2
  • 20
    • 0023389140 scopus 로고
    • Basic studies of hydrogen evolution by Escherichia coli containing a cloned Citrobacter freundii hydrogenase gene
    • Kanayama H., Sode K., Karube I. Basic studies of hydrogen evolution by Escherichia coli containing a cloned Citrobacter freundii hydrogenase gene. Appl. Biochem. Biotechnol. 1987, 15:97-106.
    • (1987) Appl. Biochem. Biotechnol. , vol.15 , pp. 97-106
    • Kanayama, H.1    Sode, K.2    Karube, I.3
  • 21
    • 0041828377 scopus 로고    scopus 로고
    • Fermentative biohydrogen production by a new chemoheterotrophic bacterium Citrobacter sp. Y19
    • Oh Y.K., Seol E.H., Kim J.R., Park S. Fermentative biohydrogen production by a new chemoheterotrophic bacterium Citrobacter sp. Y19. Int. J. Hydrogen Energy 2003, 28:1353-1359.
    • (2003) Int. J. Hydrogen Energy , vol.28 , pp. 1353-1359
    • Oh, Y.K.1    Seol, E.H.2    Kim, J.R.3    Park, S.4
  • 22
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 23
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 24
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: a maximum likelihood approach
    • Felsenstein J. Evolutionary trees from DNA sequences: a maximum likelihood approach. J. Mol. Evol. 1981, 17:368-376.
    • (1981) J. Mol. Evol. , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 25
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 2004, 5:150-163.
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 26
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: an approach using the bootstrap
    • Felsenstein J. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 1985, 39:783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 27
    • 57449119095 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a membrane-bound [NiFe]-hydrogenase from a hydrogen-oxidizing, lithotrophic bacterium, Hydrogenophaga sp. AH-24
    • Yoon K.S., Sakai Y., Tsukada N., Fujisawa K., Nishihara H. Purification and biochemical characterization of a membrane-bound [NiFe]-hydrogenase from a hydrogen-oxidizing, lithotrophic bacterium, Hydrogenophaga sp. AH-24. FEMS Microbiol. Lett. 2009, 290:114-120.
    • (2009) FEMS Microbiol. Lett. , vol.290 , pp. 114-120
    • Yoon, K.S.1    Sakai, Y.2    Tsukada, N.3    Fujisawa, K.4    Nishihara, H.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 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 Y. Isolation and characterization of a new facultatively autotrophic hydrogen-oxidizing Betaproteobacterium, Hydrogenophaga sp. AH-24. FEMS Microbiol. Lett. 2008, 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, Y.6
  • 30
    • 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. Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16. Eur. J. Biochem. 1997, 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
  • 33
    • 0018788563 scopus 로고
    • The membrane-bound Hydrogenase of Alcaligenes eutrophus
    • Schink B., Schlegel H.G. The membrane-bound Hydrogenase of Alcaligenes eutrophus. Biochim. Biophys. Acta 1979, 567:315-324.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 315-324
    • Schink, B.1    Schlegel, H.G.2
  • 34
    • 69049091873 scopus 로고    scopus 로고
    • Purification and characterization of the oxygen-thermostable hydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum camini
    • Nishimura H., Sako Y. Purification and characterization of the oxygen-thermostable hydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum camini. J. Biosci. Bioeng. 2009, 108:299-303.
    • (2009) J. Biosci. Bioeng. , vol.108 , pp. 299-303
    • Nishimura, H.1    Sako, Y.2


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