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Volumn 458, Issue 3, 2014, Pages 449-458

How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase

Author keywords

Hydrogen metabolism; Iron sulphur cluster NiFe hydrogenase; Oxygen tolerance; Protein film electrochemistry (PFE); Salmonella enterica

Indexed keywords

ALANINE; GLUTAMIC ACID; HISTIDINE; HYDROGEN; NICKEL IRON HYDROGENASE;

EID: 84896774103     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20131520     Document Type: Article
Times cited : (35)

References (45)
  • 3
    • 7044226199 scopus 로고    scopus 로고
    • Respiratory hydrogen use by Salmonella enterica serovar Typhimurium is essential for virulence
    • DOI 10.1128/IAI.72.11.6294-6299.2004
    • Maier, R. J., Olczak, A., Maier, S., Soni, S. and Gunn, J. (2004) Respiratory hydrogen use by Salmonella enterica serovar Typhimurium is essential for virulence. Infect. Immun. 72, 6294-6299 (Pubitemid 39425407)
    • (2004) Infection and Immunity , vol.72 , Issue.11 , pp. 6294-6299
    • Maier, R.J.1    Olczak, A.2    Maier, S.3    Soni, S.4    Gunn, J.5
  • 4
    • 14644405627 scopus 로고    scopus 로고
    • Use of molecular hydrogen as an energy substrate by human pathogenic bacteria
    • Maier, R. J. (2005) Use of molecular hydrogen as an energy substrate by human pathogenic bacteria. Biochem. Soc. Trans. 33, 83-85
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 83-85
    • Maier, R.J.1
  • 6
    • 35449005828 scopus 로고    scopus 로고
    • Differential expression of NiFe uptake-type hydrogenase genes in Salmonella enterica serovar Typhimurium
    • DOI 10.1099/mic.0.2007/009027-0
    • Zbell, A. L., Benoit, S. L. and Maier, R. J. (2007) Differential expression of NiFe uptake-type hydrogenase genes in Salmonella enterica serovar Typhimurium. Microbiology 153, 3508-3516 (Pubitemid 47629554)
    • (2007) Microbiology , vol.153 , Issue.10 , pp. 3508-3516
    • Zbell, A.L.1    Benoit, S.L.2    Maier, R.J.3
  • 8
    • 0022489526 scopus 로고
    • Characterization and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium
    • Sawers, R. G., Jamieson, D. J., Higgins, C. F. and Boxer, D. H. (1986) Characterization and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium. J. Bacteriol. 168, 398-404 (Pubitemid 16001628)
    • (1986) Journal of Bacteriology , vol.168 , Issue.1 , pp. 398-404
    • Sawers, R.G.1    Jamieson, D.J.2    Higgins, C.F.3    Boxer, D.H.4
  • 11
    • 0023049446 scopus 로고
    • Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli
    • Ballantine, S. P. and Boxer, D. H. (1986) Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. Eur. J. Biochem. 156, 277-284
    • (1986) Eur. J. Biochem. , vol.156 , pp. 277-284
    • Ballantine, S.P.1    Boxer, D.H.2
  • 12
    • 0023049475 scopus 로고
    • Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12
    • Sawers, R. G. and Boxer, D. H. (1986) Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12. Eur. J. Biochem. 156, 265-275
    • (1986) Eur. J. Biochem. , vol.156 , pp. 265-275
    • Sawers, R.G.1    Boxer, D.H.2
  • 13
    • 84872126781 scopus 로고    scopus 로고
    • Crystal structure of the O2 -tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b
    • Volbeda, A., Darnault, C., Parkin, A., Sargent, F., Armstrong, F. A. and Fontecilla-Camps, J. C. (2013) Crystal structure of the O2 -tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b. Structure 21, 184-190
    • (2013) Structure , vol.21 , pp. 184-190
    • Volbeda, A.1    Darnault, C.2    Parkin, A.3    Sargent, F.4    Armstrong, F.A.5    Fontecilla-Camps, J.C.6
  • 16
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • DOI 10.1046/j.1365-2958.2003.03642.x
    • Hatzixanthis, K., Palmer, T. and Sargent, F. (2003) A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol. Microbiol. 49, 1377-1390 (Pubitemid 37153504)
    • (2003) Molecular Microbiology , vol.49 , Issue.5 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 17
    • 53649098448 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium NiFe uptake-type hydrogenases are differentially expressed in vivo
    • Zbell, A. L., Maier, S. E. and Maier, R. J. (2008) Salmonella enterica serovar Typhimurium NiFe uptake-type hydrogenases are differentially expressed in vivo. Infect. Immun. 76, 4445-4454
    • (2008) Infect. Immun. , vol.76 , pp. 4445-4454
    • Zbell, A.L.1    Maier, S.E.2    Maier, R.J.3
  • 18
    • 79952140732 scopus 로고    scopus 로고
    • The Hyb hydrogenase permits hydrogen-dependent respiratory growth of Salmonella enterica serovar Typhimurium
    • Lamichhane-Khadka, R., Kwiatkowski, A. and Maier, R. J. (2010) The Hyb hydrogenase permits hydrogen-dependent respiratory growth of Salmonella enterica serovar Typhimurium. MBio 1, e00284-10
    • (2010) MBio , vol.1
    • Lamichhane-Khadka, R.1    Kwiatkowski, A.2    Maier, R.J.3
  • 19
    • 61649125193 scopus 로고    scopus 로고
    • Role of the Hya hydrogenase in recycling of anaerobically produced H2 in Salmonella enterica serovar Typhimurium
    • Zbell, A. L. and Maier, R. J. (2009) Role of the Hya hydrogenase in recycling of anaerobically produced H2 in Salmonella enterica serovar Typhimurium. App. Env. Microbiol. 75, 1456-1459
    • (2009) App. Env. Microbiol. , vol.75 , pp. 1456-1459
    • Zbell, A.L.1    Maier, R.J.2
  • 20
    • 79957993544 scopus 로고    scopus 로고
    • Oxygen-tolerant hydrogenases in hydrogen-based technologies
    • Friedrich, B., Fritsch, J. and Lenz, O. (2011) Oxygen-tolerant hydrogenases in hydrogen-based technologies. Curr. Opin. Biotechnol. 22, 358-364
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 358-364
    • Friedrich, B.1    Fritsch, J.2    Lenz, O.3
  • 21
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [NiFe]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster
    • Lukey, M. J., Roessler, M. M., Parkin, A., Evans, R. M., Davies, R. A., Lenz, O., Friedrich, B., Sargent, F. and Armstrong, F. A. (2011) Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. J. Am. Chem. Soc. 133, 16881-16892
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16881-16892
    • Lukey, M.J.1    Roessler, M.M.2    Parkin, A.3    Evans, R.M.4    Davies, R.A.5    Lenz, O.6    Friedrich, B.7    Sargent, F.8    Armstrong, F.A.9
  • 23
    • 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. and Higuchi, Y. (2011) Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 479, 253-256
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 24
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C. M., Aldea, M., Washburn, B. K., Babitzke, P. and Kushner, S. R. (1989) New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171, 4617-4622 (Pubitemid 19209055)
    • (1989) Journal of Bacteriology , vol.171 , Issue.9 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 25
    • 77954739358 scopus 로고    scopus 로고
    • Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli
    • Palmer, T., Berks, B. C. and Sargent, F. (2010) Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. Methods Mol. Biol. 619, 191-216
    • (2010) Methods Mol. Biol. , vol.619 , pp. 191-216
    • Palmer, T.1    Berks, B.C.2    Sargent, F.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0022553775 scopus 로고
    • Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies
    • Dunn, S. D. (1986) Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies. Anal. Biochem. 157, 144-153
    • (1986) Anal. Biochem. , vol.157 , pp. 144-153
    • Dunn, S.D.1
  • 34
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J. and Merritt, E. A. (2006) TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39, 109-111
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 36
    • 0038375489 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase
    • DOI 10.1021/ja035296y
    • Jones, A. K., Lamle, S. E., Pershad, H. R., Vincent, K. A., Albracht, S. P. and Armstrong, F. A. (2003) Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. J. Am. Chem. Soc. 125, 8505-8514 (Pubitemid 36858418)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.28 , pp. 8505-8514
    • Jones, A.K.1    Lamle, S.E.2    Pershad, H.R.3    Vincent, K.A.4    Albracht, S.P.J.5    Armstrong, F.A.6
  • 38
    • 84859638884 scopus 로고    scopus 로고
    • The hows and whys of aerobic H2 metabolism
    • Parkin, A. and Sargent, F. (2012) The hows and whys of aerobic H2 metabolism. Curr. Opin. Chem. Biol. 16, 26-34
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 26-34
    • Parkin, A.1    Sargent, F.2
  • 39
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • DOI 10.1126/science.1068186
    • Jormakka, M., Tornroth, S., Byrne, B. and Iwata, S. (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295, 1863-1868 (Pubitemid 34214117)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 41
    • 84864659415 scopus 로고    scopus 로고
    • The coupling mechanism of respiratory complex I: A structural and evolutionary perspective
    • Efremov, R. G. and Sazanov, L. A. (2012) The coupling mechanism of respiratory complex I: a structural and evolutionary perspective. Biochim. Biophys. Acta 1817, 1785-1795
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1785-1795
    • Efremov, R.G.1    Sazanov, L.A.2
  • 42
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov, L. A. and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436 (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 43
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • Kashani-Poor, N., Zwicker, K., Kerscher, S. and Brandt, U. (2001) A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I. J. Biol. Chem. 276, 24082-24087
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 44
    • 33747370385 scopus 로고    scopus 로고
    • The Redox-Bohr group associated with iron-sulfur cluster N2 of complex I
    • Zwicker, K., Galkin, A., Drose, S., Grgic, L., Kerscher, S. and Brandt, U. (2006) The Redox-Bohr group associated with iron-sulfur cluster N2 of complex I. J. Biol. Chem. 281, 23013-23017
    • (2006) J. Biol. Chem. , vol.281 , pp. 23013-23017
    • Zwicker, K.1    Galkin, A.2    Drose, S.3    Grgic, L.4    Kerscher, S.5    Brandt, U.6
  • 45
    • 56749154097 scopus 로고    scopus 로고
    • Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration
    • Ekici, O. D., Paetzel, M. and Dalbey, R. E. (2008) Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci. 17, 2023-2037
    • (2008) Protein Sci. , vol.17 , pp. 2023-2037
    • Ekici, O.D.1    Paetzel, M.2    Dalbey, R.E.3


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