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Volumn 21, Issue 1, 2013, Pages 184-190

Crystal structure of the O2-Tolerant membrane-bound hydrogenase 1 from escherichia coli in complex with its cognate cytochrome b

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; HYDROGENASE; OXYGEN;

EID: 84872126781     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.11.010     Document Type: Article
Times cited : (84)

References (37)
  • 1
    • 73649146540 scopus 로고    scopus 로고
    • Cytochrome d but not cytochrome o rescues the toluidine blue growth sensitivity of arc mutants of Escherichia coli
    • A.F. Alvarez, R. Malpica, M. Contreras, E. Escamilla, and D. Georgellis Cytochrome d but not cytochrome o rescues the toluidine blue growth sensitivity of arc mutants of Escherichia coli J. Bacteriol. 192 2010 391 399
    • (2010) J. Bacteriol. , vol.192 , pp. 391-399
    • Alvarez, A.F.1    Malpica, R.2    Contreras, M.3    Escamilla, E.4    Georgellis, D.5
  • 2
    • 0030609822 scopus 로고    scopus 로고
    • Effects of σ(s) and the transcriptional activator AppY on induction of the Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation
    • T. Atlung, K. Knudsen, L. Heerfordt, and L. Brøndsted Effects of sigmaS and the transcriptional activator AppY on induction of the Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation J. Bacteriol. 179 1997 2141 2146 (Pubitemid 27146866)
    • (1997) Journal of Bacteriology , vol.179 , Issue.7 , pp. 2141-2146
    • Atlung, T.1    Knudsen, K.2    Heerfordt, L.3    BrOndsted, L.4
  • 3
    • 0027980255 scopus 로고
    • Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli
    • L. Brøndsted, and T. Atlung Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli J. Bacteriol. 176 1994 5423 5428 (Pubitemid 24273532)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5423-5428
    • Brondsted, L.1    Atlung, T.2
  • 5
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • DOI 10.1021/cr050195z
    • J.C. Fontecilla-Camps, A. Volbeda, C. Cavazza, and Y. Nicolet Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases Chem. Rev. 107 2007 4273 4303 (Pubitemid 350041745)
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 6
    • 83455221549 scopus 로고    scopus 로고
    • A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16
    • S. Frielingsdorf, T. Schubert, A. Pohlmann, O. Lenz, and B. Friedrich A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16 Biochemistry 50 2011 10836 10843
    • (2011) Biochemistry , vol.50 , pp. 10836-10843
    • Frielingsdorf, S.1    Schubert, T.2    Pohlmann, A.3    Lenz, O.4    Friedrich, B.5
  • 7
    • 79956101455 scopus 로고    scopus 로고
    • The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe] hydrogenase in Ralstonia eutropha H16
    • J. Fritsch, O. Lenz, and B. Friedrich The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe] hydrogenase in Ralstonia eutropha H16 J. Bacteriol. 193 2011 2487 2497
    • (2011) J. Bacteriol. , vol.193 , pp. 2487-2497
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 10
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • DOI 10.1126/science.1068186
    • M. Jormakka, S. Törnroth, B. Byrne, and S. Iwata Molecular basis of proton motive force generation: structure of formate dehydrogenase-N Science 295 2002 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
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 14
  • 15
    • 0035822537 scopus 로고    scopus 로고
    • 2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors
    • DOI 10.1016/S0378-1097(01)00308-1, PII S0378109701003081
    • 2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors FEMS Microbiol. Lett. 202 2001 121 124 (Pubitemid 32744802)
    • (2001) FEMS Microbiology Letters , vol.202 , Issue.1 , pp. 121-124
    • Laurinavichene, T.V.1    Tsygankov, A.A.2
  • 19
    • 0025914936 scopus 로고
    • Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1
    • N.K. Menon, J. Robbins, J.C. Wendt, K.T. Shanmugam, and A.E. Przybyla Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1 J. Bacteriol. 173 1991 4851 4861
    • (1991) J. Bacteriol. , vol.173 , pp. 4851-4861
    • Menon, N.K.1    Robbins, J.2    Wendt, J.C.3    Shanmugam, K.T.4    Przybyla, A.E.5
  • 21
    • 61349134073 scopus 로고    scopus 로고
    • Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation
    • A.D. Nesbit, J.L. Giel, J.C. Rose, and P.J. Kiley Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation J. Mol. Biol. 387 2009 28 41
    • (2009) J. Mol. Biol. , vol.387 , pp. 28-41
    • Nesbit, A.D.1    Giel, J.L.2    Rose, J.C.3    Kiley, P.J.4
  • 22
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • DOI 10.1016/j.cbpa.2003.08.005
    • C.C. Page, C.C. Moser, and P.L. Dutton Mechanism for electron transfer within and between proteins Curr. Opin. Chem. Biol. 7 2003 551 556 (Pubitemid 37315789)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.5 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 23
    • 79955027963 scopus 로고    scopus 로고
    • Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus
    • M.E. Pandelia, W. Nitschke, P. Infossi, M.T. Giudici-Orticoni, E. Bill, and W. Lubitz Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus Proc. Natl. Acad. Sci. USA 108 2011 6097 6102
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6097-6102
    • Pandelia, M.E.1    Nitschke, W.2    Infossi, P.3    Giudici-Orticoni, M.T.4    Bill, E.5    Lubitz, W.6
  • 25
    • 84857768182 scopus 로고    scopus 로고
    • Analysis of hydrogenase 1 levels reveals an intimate link between carbon and hydrogen metabolism in Escherichia coli K-12
    • C. Pinske, J.S. McDowall, F. Sargent, and R.G. Sawers Analysis of hydrogenase 1 levels reveals an intimate link between carbon and hydrogen metabolism in Escherichia coli K-12 Microbiology 158 2012 856 868
    • (2012) Microbiology , vol.158 , pp. 856-868
    • Pinske, C.1    McDowall, J.S.2    Sargent, F.3    Sawers, R.G.4
  • 26
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - Roles of the terminal oxidases
    • DOI 10.1023/A:1027336712748
    • R.K. Poole, and S. Hill Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases Biosci. Rep. 17 1997 303 317 (Pubitemid 27466754)
    • (1997) Bioscience Reports , vol.17 , Issue.3 , pp. 303-317
    • Poole, R.K.1    Hill, S.2
  • 27
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • R.J. Read Improved Fourier coefficients for maps using phases from partial structures with errors Acta Crystallogr. A 42 1986 140 149
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 28
    • 36749100610 scopus 로고    scopus 로고
    • Dissecting the roles of Escherichia coli hydrogenases in biohydrogen production
    • DOI 10.1111/j.1574-6968.2007.00966.x
    • M.D. Redwood, I.P. Mikheenko, F. Sargent, and L.E. Macaskie Dissecting the roles of Escherichia coli hydrogenases in biohydrogen production FEMS Microbiol. Lett. 278 2008 48 55 (Pubitemid 350215879)
    • (2008) FEMS Microbiology Letters , vol.278 , Issue.1 , pp. 48-55
    • Redwood, M.D.1    Mikheenko, I.P.2    Sargent, F.3    Macaskie, L.E.4
  • 29
    • 0032873183 scopus 로고    scopus 로고
    • Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli
    • D.J. Richard, G. Sawers, F. Sargent, L. McWalter, and D.H. Boxer Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli Microbiology 145 1999 2903 2912 (Pubitemid 29485905)
    • (1999) Microbiology , vol.145 , Issue.10 , pp. 2903-2912
    • Richard, D.J.1    Sawers, G.2    Sargent, F.3    McWalter, L.4    Boxer, D.H.5
  • 30
    • 84866518261 scopus 로고    scopus 로고
    • EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE
    • M.M. Roessler, R.M. Evans, R.A. Davies, J.R. Harmer, and F.A. Armstrong EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE J. Am. Chem. Soc. 134 2012 15581 15594
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15581-15594
    • Roessler, M.M.1    Evans, R.M.2    Davies, R.A.3    Harmer, J.R.4    Armstrong, F.A.5
  • 31
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • G. Sawers The hydrogenases and formate dehydrogenases of Escherichia coli Antonie van Leeuwenhoek 66 1994 57 88
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 32
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Y. Shomura, K.S. Yoon, H. Nishihara, and Y. Higuchi Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase Nature 479 2011 253 256
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 33
    • 0001741688 scopus 로고    scopus 로고
    • A method to stabilize reduced and/or gas-treated protein crystals by flash-cooling under a controlled atmosphere
    • X. Vernede, and J.C. Fontecilla-Camps A method to stabilize reduced and or gas-treated protein crystals by flash-cooling under a controlled atmosphere J. Appl. Crystallogr. 32 1999 505 509 (Pubitemid 129699384)
    • (1999) Journal of Applied Crystallography , vol.32 , Issue.3 , pp. 505-509
    • Vernede, X.1    Fontecilla-Camps, J.C.2
  • 37
    • 53649098448 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium NiFe uptake-type hydrogenases are differentially expressed in vivo
    • A.L. Zbell, S.E. Maier, and R.J. Maier Salmonella enterica serovar Typhimurium NiFe uptake-type hydrogenases are differentially expressed in vivo Infect. Immun. 76 2008 4445 4454
    • (2008) Infect. Immun. , vol.76 , pp. 4445-4454
    • Zbell, A.L.1    Maier, S.E.2    Maier, R.J.3


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