메뉴 건너뛰기




Volumn 44, Issue , 2016, Pages 315-328

Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases

Author keywords

Iron sulfur cluster relay; Membrane bound hydrogenase; NiFe hydrogenase; Oxygen tolerance; Protein film electrochemistry

Indexed keywords

CYTOCHROME; HYDROGENASE; IRON SULFUR PROTEIN; MEMBRANE PROTEIN; NIFE PROTEIN; OXYGEN; UNCLASSIFIED DRUG; NICKEL-IRON HYDROGENASE;

EID: 84958162750     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20150201     Document Type: Article
Times cited : (33)

References (82)
  • 1
    • 0346095510 scopus 로고    scopus 로고
    • Climate change science: Adapt, mitigate, or ignore?
    • CrossRef PubMed
    • King, D.A. (2004) Climate change science: adapt, mitigate, or ignore? Science 303, 176-177 CrossRef PubMed
    • (2004) Science , vol.303 , pp. 176-177
    • King, D.A.1
  • 2
    • 15944396152 scopus 로고    scopus 로고
    • The properties of hydrogen as fuel tomorrow in sustainable energy system for a cleaner planet
    • CrossRef
    • Momirlan, M. and Veziroglu, T. (2005) The properties of hydrogen as fuel tomorrow in sustainable energy system for a cleaner planet. Int. J. Hydrogen Energy 30, 795-802 CrossRef
    • (2005) Int. J. Hydrogen Energy , vol.30 , pp. 795-802
    • Momirlan, M.1    Veziroglu, T.2
  • 4
    • 84942279728 scopus 로고    scopus 로고
    • Genomic and metagenomic surveys of hydrogenase distribution indicate h2 is a widely utilised energy source for microbial growth and survival
    • [Epub ahead of print]
    • Greening, C., Biswas, A., Carere, C.R., Jackson, C.J., Taylor, M.C., Stott, M.B., Cook, G.M. and Morales, S.E. (2015) Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival. ISME J., doi:10.1038/ismej.2015.153. [Epub ahead of print]
    • (2015) ISME J
    • Greening, C.1    Biswas, A.2    Carere, C.R.3    Jackson, C.J.4    Taylor, M.C.5    Stott, M.B.6    Cook, G.M.7    Morales, S.E.8
  • 6
    • 84884318697 scopus 로고    scopus 로고
    • Nife] hydrogenases: A common active site for hydrogen metabolism under diverse conditions
    • CrossRef
    • Shafaat, H.S., Rüdiger, O., Ogata, H. and Lubitz, W. (2013) [NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions. Biochim. Biophys. Acta 1827 986-1002 CrossRef
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 986-1002
    • Shafaat, H.S.1    Rüdiger, O.2    Ogata, H.3    Lubitz, W.4
  • 7
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • CrossRef PubMed
    • Vignais, P.M. and Billoud, B. (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107, 4206-4272 CrossRef PubMed
    • (2007) Chem. Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 8
    • 49049118534 scopus 로고    scopus 로고
    • Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis
    • CrossRef PubMed
    • Cracknell, J.A., Vincent, K.A. and Armstrong, F.A. (2008) Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. Chem. Rev. 108, 2439-2461 CrossRef PubMed
    • (2009) Chem. Rev , vol.108 , pp. 2439-2461
    • Cracknell, J.A.1    Vincent, K.A.2    Armstrong, F.A.3
  • 9
  • 10
    • 0023049446 scopus 로고
    • Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (1986) Eur. J. Biochem , vol.156 , pp. 277-284
    • Ballantine, S.P.1    Boxer, D.H.2
  • 11
    • 0023049475 scopus 로고
    • Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli k12
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (1986) Eur. J. Biochem , vol.156 , pp. 265-275
    • Sawers, R.G.1    Boxer, D.H.2
  • 12
    • 0019221674 scopus 로고
    • The role of the membrane-bound hydrogenase in the energy-conserving oxidation of molecular hydrogen by Escherichia coli
    • CrossRef PubMed
    • Jones, R.W. (1980) The role of the membrane-bound hydrogenase in the energy-conserving oxidation of molecular hydrogen by Escherichia coli. Biochem. J. 188, 345-350 CrossRef PubMed
    • (1980) Biochem. J , vol.188 , pp. 345-350
    • Jones, R.W.1
  • 13
    • 7044226199 scopus 로고    scopus 로고
    • Respiratory hydrogen use by salmonella enterica serovar typhimurium is essential for virulence
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (2004) Infect. Immun , vol.72 , pp. 6294-6299
    • Maier, R.J.1    Olczak, A.2    Maier, S.3    Soni, S.4    Gunn, J.5
  • 14
    • 77951202939 scopus 로고    scopus 로고
    • H2 conversion in the presence of o2 as performed by the membrane-bound [nife]-hydrogenase of ralstonia eutropha
    • CrossRef PubMed
    • Lenz, O., Ludwig, M., Schubert, T., Bürstel, I., Ganskow, S., Goris, T., Schwarze, A. and Friedrich, B. (2010) H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha. ChemPhysChem. 11, 1107-1119 CrossRef PubMed
    • (2010) ChemPhysChem , vol.11 , pp. 1107-1119
    • Lenz, O.1    Ludwig, M.2    Schubert, T.3    Bürstel, I.4    Ganskow, S.5    Goris, T.6    Schwarze, A.7    Friedrich, B.8
  • 16
    • 84862223771 scopus 로고    scopus 로고
    • Evolution and diversification of group 1 [nife] hydrogenases. Is there a phylogenetic marker for o2-tolerance?
    • CrossRef PubMed
    • Pandelia, M.-E., Lubitz, W. and Nitschke, W. (2012) Evolution and diversification of Group 1 [NiFe] hydrogenases. Is there a phylogenetic marker for O2-tolerance? Biochim. Biophys. Acta 1817, 1565-1575 CrossRef PubMed
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1565-1575
    • Pandelia, M.-E.1    Lubitz, W.2    Nitschke, W.3
  • 17
    • 84958199968 scopus 로고    scopus 로고
    • United States. Congress. House. Committee on Science. Subcommittee on Energy Available from
    • United States. Congress. House. Committee on Science. Subcommittee on Energy (2006) Fueling the future: on the road to the hydrogen economy. Available from: http://purl.access.gpo.gov/GPO/LPS67640
    • (2006) Fueling the Future: On the Road to the Hydrogen Economy
  • 19
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • CrossRef PubMed
    • Vincent, K.A., Parkin, A. and Armstrong, F.A. (2007) Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem. Rev. 107, 4366-4413 CrossRef PubMed
    • (2007) Chem. Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 20
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • CrossRef
    • Dubini, A., Pye, R.L., Jack, R.L., Palmer, T. and Sargent, F. (2002) How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. Int. J. Hydrogen Energy 27, 1413-1420 CrossRef
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1413-1420
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 21
    • 33746894166 scopus 로고    scopus 로고
    • Elucidating the mechanisms of coupled electron transfer and catalytic reactions by protein film voltammetry
    • CrossRef PubMed
    • Hirst, J. (2006) Elucidating the mechanisms of coupled electron transfer and catalytic reactions by protein film voltammetry. Biochim. Biophys. Acta 1757, 225-239 CrossRef PubMed
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 225-239
    • Hirst, J.1
  • 22
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • CrossRef PubMed
    • Léger, C. and Bertrand, P. (2008) Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chem. Rev. 108, 2379-2438 CrossRef PubMed
    • (2008) Chem. Rev , vol.108 , pp. 2379-2438
    • Léger, C.1    Bertrand, P.2
  • 23
    • 0016790173 scopus 로고
    • Structural and catalytic properties of hydrogenase from chromatium
    • CrossRef PubMed
    • Gitlitz, P.H. and Krasna, A.I. (1975) Structural and catalytic properties of hydrogenase from Chromatium. Biochemistry 14, 2561-2568 CrossRef PubMed
    • (1975) Biochemistry , vol.14 , pp. 2561-2568
    • Gitlitz, P.H.1    Krasna, A.I.2
  • 24
    • 77049246041 scopus 로고
    • The reduction of methylene blue by hydrogenase
    • PubMed
    • Whiteley, H.R. and Ordal, E.J. (1955) The reduction of methylene blue by hydrogenase. J. Bacteriol. 70, 608-613 PubMed
    • (1955) J. Bacteriol , vol.70 , pp. 608-613
    • Whiteley, H.R.1    Ordal, E.J.2
  • 27
    • 84896967315 scopus 로고    scopus 로고
    • Transforming an oxygen-tolerant [nife] uptake hydrogenase into a proficient, reversible hydrogen producer
    • CrossRef
    • Murphy, B.J., Sargent, F. and Armstrong, F.A. (2014) Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer. Energy Environ. Sci. 7, 1426 CrossRef
    • (2014) Energy Environ. Sci , vol.7 , pp. 1426
    • Murphy, B.J.1    Sargent, F.2    Armstrong, F.A.3
  • 28
    • 84055191475 scopus 로고    scopus 로고
    • Spectroscopic characterization of the key catalytic intermediate ni-c in the o2-tolerant [nife] hydrogenase i from aquifex aeolicus: Evidence of a weakly bound hydride
    • CrossRef
    • Pandelia, M.-E., Infossi, P., Stein, M., Giudici-Orticoni, M.-T. and Lubitz, W. (2011) Spectroscopic characterization of the key catalytic intermediate Ni-C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride. Chem. Commun. 48, 823-825 CrossRef
    • (2011) Chem. Commun , vol.48 , pp. 823-825
    • Pandelia, M.-E.1    Infossi, P.2    Stein, M.3    Giudici-Orticoni, M.-T.4    Lubitz, W.5
  • 29
    • 77952566611 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase i from the hyperthermophilic bacterium aquifex aeolicus: Enzyme activation, redox intermediates and oxygen tolerance
    • CrossRef PubMed
    • Pandelia, M.-E., Fourmond, V., Tron-Infossi, P., Lojou, E., Bertrand, P., L eger, C., Giudici-Orticoni, M.-T. and Lubitz, W. (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 CrossRef PubMed
    • (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    Ĺeger, C.6    Giudici-Orticoni, M.-T.7    Lubitz, W.8
  • 30
    • 67650273077 scopus 로고    scopus 로고
    • Spectroscopic insights into the oxygen-tolerant membrane-Associated [nife] hydrogenase of ralstonia eutropha h16
    • CrossRef PubMed
    • Saggu, M., Zebger, I., Ludwig, M., Lenz, O., Friedrich, B., Hildebrandt, P. and Lendzian, F. (2009) Spectroscopic insights into the oxygen-tolerant membrane-Associated [NiFe] hydrogenase of Ralstonia eutropha H16. J. Biol. Chem. 284, 16264-16276 CrossRef PubMed
    • (2009) J. Biol. Chem , vol.284 , pp. 16264-16276
    • Saggu, M.1    Zebger, I.2    Ludwig, M.3    Lenz, O.4    Friedrich, B.5    Hildebrandt, P.6    Lendzian, F.7
  • 31
    • 84930633448 scopus 로고    scopus 로고
    • Infrared spectroscopy during electrocatalytic turnover reveals the ni-l active site state during h2 oxidation by a nife hydrogenase
    • CrossRef
    • Hidalgo, R., Ash, P.A., Healy, A.J. and Vincent, K.A. (2015) Infrared spectroscopy during electrocatalytic turnover reveals the Ni-L active site state during H2 oxidation by a NiFe hydrogenase. Angew. Chem. Int. Ed. 54, 7110-7113 CrossRef
    • (2015) Angew. Chem. Int. Ed , vol.54 , pp. 7110-7113
    • Hidalgo, R.1    Ash, P.A.2    Healy, A.J.3    Vincent, K.A.4
  • 32
    • 58249114011 scopus 로고    scopus 로고
    • Monitoring catalysis of the membrane-bound hydrogenase from ralstonia eutropha h16 by surface-enhanced ir absorption spectroscopy
    • CrossRef
    • Wisitruangsakul, N., Lenz, O., Ludwig, M., Friedrich, B., Lendzian, F., Hildebrandt, P. and Zebger, I. (2009) Monitoring catalysis of the membrane-bound hydrogenase from Ralstonia eutropha H16 by surface-enhanced IR absorption spectroscopy. Angew. Chem. Int. Ed. 48, 611-613 CrossRef
    • (2009) Angew. Chem. Int. Ed , vol.48 , pp. 611-613
    • Wisitruangsakul, N.1    Lenz, O.2    Ludwig, M.3    Friedrich, B.4    Lendzian, F.5    Hildebrandt, P.6    Zebger, I.7
  • 33
    • 84928538572 scopus 로고    scopus 로고
    • Hydrogens detected by subatomic resolution protein crystallography in a [nife] hydrogenase
    • CrossRef PubMed
    • Ogata, H., Nishikawa, K. and Lubitz, W. (2015) Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase. Nature 520, 571-574 CrossRef PubMed
    • (2015) Nature , vol.520 , pp. 571-574
    • Ogata, H.1    Nishikawa, K.2    Lubitz, W.3
  • 34
    • 84946041646 scopus 로고    scopus 로고
    • Ft-ir characterization of the light-induced ni-l2 and ni-l3 states of [nife] hydrogenase from desulfovibrio vulgaris miyazaki f
    • CrossRef PubMed
    • Tai, H., Nishikawa, K., Inoue, S., Higuchi, Y. and Hirota, S. (2015) FT-IR characterization of the light-induced Ni-L2 and Ni-L3 states of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Phys. Chem. B 119, 13668-13674 CrossRef PubMed
    • (2015) J. Phys. Chem. B , vol.119 , pp. 13668-13674
    • Tai, H.1    Nishikawa, K.2    Inoue, S.3    Higuchi, Y.4    Hirota, S.5
  • 35
    • 70349881886 scopus 로고    scopus 로고
    • Ftir study on the light sensitivity of the [nife] hydrogenase from desulfovibrio vulgaris miyazaki f: Ni-c to ni-l photoconversion, kinetics of proton rebinding and h/d isotope effect
    • CrossRef PubMed
    • Kellers, P., Pandelia, M.-E., Currell, L.J., Görner, H. and Lubitz, W. (2009) FTIR study on the light sensitivity of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Ni-C to Ni-L photoconversion, kinetics of proton rebinding and H/D isotope effect. Phys. Chem. Chem. Phys. 11, 8680-8683 CrossRef PubMed
    • (2009) Phys. Chem. Chem. Phys , vol.11 , pp. 8680-8683
    • Kellers, P.1    Pandelia, M.-E.2    Currell, L.J.3    Görner, H.4    Lubitz, W.5
  • 36
    • 0012005579 scopus 로고
    • Studies of light-induced nickel epr signals in desulfovibrio gigas hydrogenase
    • CrossRef
    • Medina, M., Williams, R., Cammack, R. and Hatchikian, E.C. (1994) Studies of light-induced nickel EPR signals in Desulfovibrio gigas hydrogenase. J. Chem. Soc. Faraday Trans. 90, 2921-2924 CrossRef
    • (1994) J. Chem. Soc. Faraday Trans , vol.90 , pp. 2921-2924
    • Medina, M.1    Williams, R.2    Cammack, R.3    Hatchikian, E.C.4
  • 37
    • 0038375489 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of allochromatium vinosum [nife]-hydrogenase
    • CrossRef PubMed
    • Jones, A.K., Lamle, S.E., Pershad, H.R., Vincent, K.A., Albracht, S.P.J. 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 CrossRef PubMed
    • (2003) J. Am. Chem. Soc , vol.125 , 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
  • 39
    • 84859638884 scopus 로고    scopus 로고
    • The hows and whys of aerobic h2 metabolism
    • CrossRef PubMed
    • Parkin, A. and Sargent, F. (2012) The hows and whys of aerobic H2 metabolism. Curr. Opin. Chem. Biol. 16, 26-34 CrossRef PubMed
    • (2012) Curr. Opin. Chem. Biol , vol.16 , pp. 26-34
    • Parkin, A.1    Sargent, F.2
  • 40
    • 73949146943 scopus 로고    scopus 로고
    • A kinetic and thermodynamic understanding of o2 tolerance in [nife]-hydrogenases
    • CrossRef PubMed
    • Cracknell, J.A., Wait, A.F., Lenz, O., Friedrich, B. and Armstrong, F.A. (2009) A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases. Proc. Natl. Acad. Sci. U.S.A. 106, 20681-20686 CrossRef PubMed
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 20681-20686
    • Cracknell, J.A.1    Wait, A.F.2    Lenz, O.3    Friedrich, B.4    Armstrong, F.A.5
  • 41
    • 0037116445 scopus 로고    scopus 로고
    • 17o endor detection of a solvent-derived ni? Ohx)?fe bridge that is lost upon activation of the hydrogenase from desulfovibrio gigas
    • CrossRef PubMed
    • Carepo, M., Tierney, D.L., Brondino, C.D., Yang, T.C., Pamplona, A., Telser, J., Moura, I., Moura, J.J.G. and Hoffman, B.M. (2002) 17O ENDOR detection of a solvent-derived Ni?(OHx)?Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas. J. Am. Chem. Soc. 124, 281-286 CrossRef PubMed
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 281-286
    • Carepo, M.1    Tierney, D.L.2    Brondino, C.D.3    Yang, T.C.4    Pamplona, A.5    Telser, J.6    Moura, I.7    Moura, J.J.G.8    Hoffman, B.M.9
  • 42
    • 0025134895 scopus 로고
    • Effect of 17o2 and 13co on epr spectra of nickel in hydrogenase from chromatium vinosum
    • CrossRef PubMed
    • van der Zwaan, J.W., Coremans, J.M., Bouwens, E.C. and Albracht, S.P. (1990) Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosum. Biochim. Biophys. Acta 1041, 101-110 CrossRef PubMed
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 101-110
    • Van Der Zwaan, J.W.1    Coremans, J.M.2    Bouwens, E.C.3    Albracht, S.P.4
  • 44
    • 84899819167 scopus 로고    scopus 로고
    • How oxygen reacts with oxygen-tolerant respiratory [nife]-hydrogenases
    • CrossRef
    • Wulff, P., Day, C.C., Sargent, F. and Armstrong, F.A. (2014) How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases. Proc. Natl. Acad. Sci. 111, 6606-6611 CrossRef
    • (2014) Proc. Natl. Acad. Sci , vol.111 , pp. 6606-6611
    • Wulff, P.1    Day, C.C.2    Sargent, F.3    Armstrong, F.A.4
  • 45
    • 77950795503 scopus 로고    scopus 로고
    • Two-step" chronoamperometric method for studying the anaerobic inactivation of an oxygen tolerant nife hydrogenase
    • CrossRef PubMed
    • Fourmond, V., Infossi, P., Giudici-Orticoni, M.-T., Bertrand, P. and Léger, C. (2010) "Two-step" chronoamperometric method for studying the anaerobic inactivation of an oxygen tolerant NiFe hydrogenase. J. Am. Chem. Soc. 132, 4848-4857 CrossRef PubMed
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 4848-4857
    • Fourmond, V.1    Infossi, P.2    Giudici-Orticoni, M.-T.3    Bertrand, P.4    Léger, C.5
  • 47
    • 0024264943 scopus 로고
    • A pulsed epr study of redox-dependent hyperfine interactions for the nickel centre of desulfovibrio gigas hydrogenase
    • CrossRef PubMed
    • Chapman, A., Cammack, R., Hatchikian, C.E., McCracken, J. and Peisach, J. (1988) A pulsed EPR study of redox-dependent hyperfine interactions for the nickel centre of Desulfovibrio gigas hydrogenase. FEBS Lett. 242, 134-138 CrossRef PubMed
    • (1988) FEBS Lett , vol.242 , pp. 134-138
    • Chapman, A.1    Cammack, R.2    Hatchikian, C.E.3    McCracken, J.4    Peisach, J.5
  • 49
    • 8844220418 scopus 로고    scopus 로고
    • Electrochemical potential-step investigations of the aerobic interconversions of [nife]-hydrogenase from allochromatium vinosum: Insights into the puzzling difference between unready and ready oxidized inactive states
    • CrossRef PubMed
    • Lamle, S.E., Albracht, S.P.J. and Armstrong, F.A. (2004) Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states. J. Am. Chem. Soc. 126, 14899-14909 CrossRef PubMed
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 14899-14909
    • Lamle, S.E.1    Albracht, S.P.J.2    Armstrong, F.A.3
  • 51
    • 0028889166 scopus 로고
    • Crystal structure of the nickel-iron hydrogenase from desulfovibrio gigas
    • CrossRef PubMed
    • Volbeda, A., Charon, M.H., Piras, C., Hatchikian, E.C., Frey, M. and Fontecilla-Camps, J.C. (1995) Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 373, 580-587 CrossRef PubMed
    • (1995) Nature , vol.373 , pp. 580-587
    • Volbeda, A.1    Charon, M.H.2    Piras, C.3    Hatchikian, E.C.4    Frey, M.5    Fontecilla-Camps, J.C.6
  • 52
    • 27644552110 scopus 로고    scopus 로고
    • Activation process of [nife] hydrogenase elucidated by high-resolution x-ray analyses: Conversion of the ready to the unready state
    • CrossRef PubMed
    • Ogata, H., Hirota, S., Nakahara, A., Komori, H., Shibata, N., Kato, T., Kano, K. and Higuchi, Y. (2005) Activation process of [NiFe] hydrogenase elucidated by high-resolution X-ray analyses: conversion of the ready to the unready state. Structure 13, 1635-1642 CrossRef PubMed
    • (2005) Structure , vol.13 , pp. 1635-1642
    • Ogata, H.1    Hirota, S.2    Nakahara, A.3    Komori, H.4    Shibata, N.5    Kato, T.6    Kano, K.7    Higuchi, Y.8
  • 54
    • 84927647151 scopus 로고    scopus 로고
    • Nife]-hydrogenases revisited: Nickel-carboxamido bond formation in a variant with accrued o2-tolerance and a tentative re-interpretation of ni-si states
    • CrossRef PubMed
    • Volbeda, A., Martin, L., Liebgott, P.-P., Lacey, A.L.D. and Fontecilla-Camps, J.C. (2015) [NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states. Metallomics 7, 710-718 CrossRef PubMed
    • (2015) Metallomics , vol.7 , pp. 710-718
    • Volbeda, A.1    Martin, L.2    Liebgott, P.-P.3    Lacey, A.L.D.4    Fontecilla-Camps, J.C.5
  • 55
    • 84935911614 scopus 로고    scopus 로고
    • Structural differences between the active sites of the ni-A and ni-b states of the [nife] hydrogenase: An approach by quantum chemistry and single crystal endor spectroscopy
    • CrossRef PubMed
    • Barilone, J.L., Ogata, H., Lubitz, W. and Gastel, M. van (2015) Structural differences between the active sites of the Ni-A and Ni-B states of the [NiFe] hydrogenase: an approach by quantum chemistry and single crystal ENDOR spectroscopy. Phys. Chem. Chem. Phys. 17, 16204-16212 CrossRef PubMed
    • (2015) Phys. Chem. Chem. Phys , vol.17 , pp. 16204-16212
    • Barilone, J.L.1    Ogata, H.2    Lubitz, W.3    Van Gastel, M.4
  • 57
    • 82355182096 scopus 로고    scopus 로고
    • Efficient electron transfer from hydrogen to benzyl viologen by the [nife]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit
    • CrossRef PubMed
    • Pinske, C., Krüger, S., Soboh, B., Ihling, C., Kuhns, M., Braussemann, M., Jaroschinsky, M., Sauer, C., Sargent, F., Sinz, A. et al. (2011) Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit. Arch. Microbiol. 193, 893-903 CrossRef PubMed
    • (2011) Arch. Microbiol , vol.193 , pp. 893-903
    • Pinske, C.1    Krüger, S.2    Soboh, B.3    Ihling, C.4    Kuhns, M.5    Braussemann, M.6    Jaroschinsky, M.7    Sauer, C.8    Sargent, F.9    Sinz, A.10
  • 58
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4fe-3s] cluster in the oxygen-tolerant membrane-bound [nife]-hydrogenase
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.-S.2    Nishihara, H.3    Higuchi, Y.4
  • 59
    • 80855128805 scopus 로고    scopus 로고
    • The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre
    • CrossRef PubMed
    • Fritsch, J., Scheerer, P., Frielingsdorf, S., Kroschinsky, S., Friedrich, B., Lenz, O. and Spahn, C.M.T. (2011) The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre. Nature 479, 249-252 CrossRef PubMed
    • (2011) Nature , vol.479 , pp. 249-252
    • Fritsch, J.1    Scheerer, P.2    Frielingsdorf, S.3    Kroschinsky, S.4    Friedrich, B.5    Lenz, O.6    Spahn, C.M.T.7
  • 62
    • 0037009993 scopus 로고    scopus 로고
    • Structural studies of the carbon monoxide complex of [nife]hydrogenase from desulfovibrio vulgaris miyazaki f: Suggestion for the initial activation site for dihydrogen
    • CrossRef PubMed
    • Ogata, H., Mizoguchi, Y., Mizuno, N., Miki, K., Adachi, S., Yasuoka, N., Yagi, T., Yamauchi, O., Hirota, S. and Higuchi, Y. (2002) Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen. J. Am. Chem. Soc. 124, 11628-11635 CrossRef PubMed
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 11628-11635
    • Ogata, H.1    Mizoguchi, Y.2    Mizuno, N.3    Miki, K.4    Adachi, S.5    Yasuoka, N.6    Yagi, T.7    Yamauchi, O.8    Hirota, S.9    Higuchi, Y.10
  • 63
    • 0033134667 scopus 로고    scopus 로고
    • Removal of the bridging ligand atom at the ni-fe active site of [nife] hydrogenase upon reduction with h2, as revealed by x-ray structure analysis at 1.4 a resolution
    • CrossRef PubMed
    • Higuchi, Y., Ogata, H., Miki, K., Yasuoka, N. and Yagi, T. (1999) Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution. Structure 7, 549-556 CrossRef PubMed
    • (1999) Structure , vol.7 , pp. 549-556
    • Higuchi, Y.1    Ogata, H.2    Miki, K.3    Yasuoka, N.4    Yagi, T.5
  • 64
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in ni-fe active center and an additional mg site in hydrogenase revealed by high resolution x-ray structure analysis
    • CrossRef PubMed
    • Higuchi, Y., Yagi, T. and Yasuoka, N. (1997) Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure 5, 1671-1680 CrossRef PubMed
    • (1997) Structure , vol.5 , pp. 1671-1680
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 65
    • 84882258226 scopus 로고    scopus 로고
    • Structural foundations for the o2 resistance of desulfomicrobium baculatum [nifese]-hydrogenase
    • CrossRef
    • Volbeda, A., Amara, P., Iannello, M., Lacey, A.L.D., Cavazza, C. and Fontecilla-Camps, J.C. (2013) Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase. Chem. Commun. 49, 7061-7063 CrossRef
    • (2013) Chem. Commun , vol.49 , pp. 7061-7063
    • Volbeda, A.1    Amara, P.2    Iannello, M.3    Lacey, A.L.D.4    Cavazza, C.5    Fontecilla-Camps, J.C.6
  • 66
    • 0033135158 scopus 로고    scopus 로고
    • The crystal structure of a reduced [nifese] hydrogenase provides an image of the activated catalytic center
    • CrossRef PubMed
    • Garcin, E., Vernede, X., Hatchikian, E.C., Volbeda, A., Frey, M. and Fontecilla-Camps, J.C. (1999) The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 7, 557-566 CrossRef PubMed
    • (1999) Structure , vol.7 , pp. 557-566
    • Garcin, E.1    Vernede, X.2    Hatchikian, E.C.3    Volbeda, A.4    Frey, M.5    Fontecilla-Camps, J.C.6
  • 67
    • 77956759468 scopus 로고    scopus 로고
    • The crystal structure of the [nife] hydrogenase from the photosynthetic bacterium allochromatium vinosum: Characterization of the oxidized enzyme (ni-A state
    • CrossRef PubMed
    • Ogata, H., Kellers, P. and Lubitz, W. (2010) The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A State). J. Mol. Biol. 402, 428-444 CrossRef PubMed
    • (2010) J. Mol. Biol , vol.402 , pp. 428-444
    • Ogata, H.1    Kellers, P.2    Lubitz, W.3
  • 68
    • 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
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (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
  • 70
    • 84896774103 scopus 로고    scopus 로고
    • How the structure of the large subunit controls function in an oxygen-tolerant [nife]-hydrogenase
    • CrossRef PubMed
    • Bowman, L., Flanagan, L., Fyfe, P.K., Parkin, A., Hunter, W.N. and Sargent, F. (2014) How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase. Biochem. J. 458, 449-458 CrossRef PubMed
    • (2014) Biochem. J , vol.458 , pp. 449-458
    • Bowman, L.1    Flanagan, L.2    Fyfe, P.K.3    Parkin, A.4    Hunter, W.N.5    Sargent, F.6
  • 72
    • 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
    • CrossRef PubMed
    • Pandelia, M.-E., Nitschke, W., Infossi, P., Giudici-Orticoni, M.-T., Bill, E. and Lubitz, W. (2011) Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proc. Natl. Acad. Sci. U.S.A. 108, 6097-6102 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A , 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
  • 74
    • 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
    • CrossRef PubMed
    • Roessler, M.M., Evans, R.M., Davies, R.A., Harmer, J. and Armstrong, F.A. (2012) 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, 15581-15594 CrossRef PubMed
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 15581-15594
    • Roessler, M.M.1    Evans, R.M.2    Davies, R.A.3    Harmer, J.4    Armstrong, F.A.5
  • 75
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [nife]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal fe-s cluster
    • CrossRef PubMed
    • 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 CrossRef PubMed
    • (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
  • 76
    • 84922282570 scopus 로고    scopus 로고
    • What is the trigger mechanism for the reversal of electron flow in oxygen-tolerant [nife] hydrogenases?
    • CrossRef
    • Dance, I. (2015) What is the trigger mechanism for the reversal of electron flow in oxygen-tolerant [NiFe] hydrogenases? Chem. Sci. 6, 1433-1443 CrossRef
    • (2015) Chem Sci , vol.6 , pp. 1433-1443
    • Dance, I.1
  • 77
    • 84863899218 scopus 로고    scopus 로고
    • Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
    • CrossRef PubMed
    • Hexter, S.V., Grey, F., Happe, T., Climent, V. and Armstrong, F.A. (2012) Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proc. Natl. Acad. Sci. U.S.A. 109, 11516-11521 CrossRef PubMed
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 11516-11521
    • Hexter, S.V.1    Grey, F.2    Happe, T.3    Climent, V.4    Armstrong, F.A.5
  • 78
    • 84874101282 scopus 로고    scopus 로고
    • Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen-the crucial influence of high potential fe-s clusters in the electron relay of [nife]-hydrogenases
    • CrossRef PubMed
    • Evans, R.M., Parkin, A., Roessler, M.M., Murphy, B.J., Adamson, H., Lukey, M.J., Sargent, F., Volbeda, A., Fontecilla-Camps, J.C. and Armstrong, F.A. (2013) Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen-the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases. J. Am. Chem. Soc. 135, 2694-2707 CrossRef PubMed
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 2694-2707
    • Evans, R.M.1    Parkin, A.2    Roessler, M.M.3    Murphy, B.J.4    Adamson, H.5    Lukey, M.J.6    Sargent, F.7    Volbeda, A.8    Fontecilla-Camps, J.C.9    Armstrong, F.A.10
  • 81
    • 83455221549 scopus 로고    scopus 로고
    • A trimeric supercomplex of the oxygen-tolerant membrane-bound [nife]-hydrogenase from ralstonia eutropha h16
    • CrossRef PubMed
    • Frielingsdorf, S., Schubert, T., Pohlmann, A., Lenz, O. and Friedrich, B. (2011) A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16. Biochemistry 50, 10836-10843 CrossRef PubMed
    • (2011) Biochemistry , vol.50 , pp. 10836-10843
    • Frielingsdorf, S.1    Schubert, T.2    Pohlmann, A.3    Lenz, O.4    Friedrich, B.5
  • 82
    • 84902665564 scopus 로고    scopus 로고
    • Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [nife]-hydrogenase of ralstonia eutropha
    • CrossRef PubMed
    • Radu, V., Frielingsdorf, S., Evans, S.D., Lenz, O. and Jeuken, L.J.C. (2014) Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha. J. Am. Chem. Soc. 136, 8512-8515 CrossRef PubMed
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 8512-8515
    • Radu, V.1    Frielingsdorf, S.2    Evans, S.D.3    Lenz, O.4    Jeuken, L.J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.