메뉴 건너뛰기




Volumn , Issue , 2015, Pages 61-96

Oxygen-tolerant hydrogenases and their biotechnological potential

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGICAL POTENTIALS; HYDROGENASES;

EID: 84937134260     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1515/9783110336733.61     Document Type: Chapter
Times cited : (33)

References (136)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais PM, Billoud B. Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 2007;107:4206-72.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 2
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]-and [FeFe]-hydrogenases
    • Fontecilla-Camps JC, Volbeda A, Cavazza C, Nicolet Y. Structure/function relationships of [NiFe]-and [FeFe]-hydrogenases. Chem Rev 2007;107:4273-303.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 3
    • 84929043896 scopus 로고    scopus 로고
    • Rosenberg E, DeLong E, Lory S, Stackebrandt E, Thompson F, eds, The Prokaryotes: Springer Berlin Heidelberg
    • Schwartz E, Fritsch J, Friedrich B. H2-Metabolizing Prokaryotes. In: Rosenberg E, DeLong E, Lory S, Stackebrandt E, Thompson F, eds. The Prokaryotes: Springer Berlin Heidelberg; 2013:119-99.
    • (2013) H2-Metabolizing Prokaryotes , pp. 119-199
    • Schwartz, E.1    Fritsch, J.2    Friedrich, B.3
  • 4
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • Vincent KA, Parkin A, Armstrong FA. Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem Rev 2007;107:4366-413.
    • (2007) Chem Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 5
    • 0037149937 scopus 로고    scopus 로고
    • Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
    • Jones AK, Sillery E, Albracht SP, Armstrong FA. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun (Camb) 2002;21:866-7.
    • (2002) Chem Commun (Camb) , vol.21 , pp. 866-867
    • Jones, A.K.1    Sillery, E.2    Albracht, S.P.3    Armstrong, F.A.4
  • 6
    • 84872475055 scopus 로고    scopus 로고
    • Structure, function and biosynthesis of O2-tolerant hydrogenases
    • Fritsch J, Lenz O, Friedrich B. Structure, function and biosynthesis of O2-tolerant hydrogenases. Nat Rev Microbiol 2013;11:106-14.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 106-114
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 7
    • 77951202939 scopus 로고    scopus 로고
    • H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha
    • Lenz O, Ludwig M, Schubert T, et al. H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha. Chemphyschem 2010;11:1107-19.
    • (2010) Chemphyschem , vol.11 , pp. 1107-1119
    • Lenz, O.1    Ludwig, M.2    Schubert, T.3
  • 8
    • 80052722488 scopus 로고    scopus 로고
    • Genome data mining and soil survey for the novel group 5 [NiFe]-hydrogenase to explore the diversity and ecological importance of presumptive high-affinity H2-oxidizing bacteria
    • Constant P, Chowdhury SP, Hesse L, Pratscher J, Conrad R. Genome data mining and soil survey for the novel group 5 [NiFe]-hydrogenase to explore the diversity and ecological importance of presumptive high-affinity H2-oxidizing bacteria. Appl Environ Microbiol 2011;77:6027-35.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 6027-6035
    • Constant, P.1    Chowdhury, S.P.2    Hesse, L.3    Pratscher, J.4    Conrad, R.5
  • 9
    • 50249104385 scopus 로고    scopus 로고
    • Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species
    • Goldet G, Wait AF, Cracknell JA, et al. Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species. J Am Chem Soc 2008;130:11106-13.
    • (2008) J am Chem Soc , vol.130 , pp. 11106-11113
    • Goldet, G.1    Wait, A.F.2    Cracknell, J.A.3
  • 10
    • 80855128805 scopus 로고    scopus 로고
    • The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre
    • Fritsch J, Scheerer P, Frielingsdorf S, et al. The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre. Nature 2011;479:249-52.
    • (2011) Nature , vol.479 , pp. 249-252
    • Fritsch, J.1    Scheerer, P.2    Frielingsdorf, S.3
  • 11
    • 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;248:179-86.
    • (1997) Eur J Biochem , vol.248 , pp. 179-186
    • Bernhard, M.1    Benelli, B.2    Hochkoeppler, A.3    Zannoni, D.4    Friedrich, B.5
  • 12
    • 0034967749 scopus 로고    scopus 로고
    • Isolation and characterization of CO2-fixing hydrogen-oxidizing marine bacteria
    • Bae S, Kwak K, Kim S, Chung S, Igarashi Y. Isolation and characterization of CO2-fixing hydrogen-oxidizing marine bacteria. J Biosci Bioeng 2001;91.
    • (2001) J Biosci Bioeng , pp. 91
    • Bae, S.1    Kwak, K.2    Kim, S.3    Chung, S.4    Igarashi, Y.5
  • 13
    • 51249192607 scopus 로고
    • Studies on-true dissimilatory nitrate reduction. IV. On adaptation in Micrococcus denitrificans
    • Kluyver AJ, Verhoeven W. Studies on-true dissimilatory nitrate reduction. IV. On adaptation in Micrococcus denitrificans. Antonie Van Leeuwenhoek 1954;20:337-58.
    • (1954) Antonie Van Leeuwenhoek , vol.20 , pp. 337-358
    • Kluyver, A.J.1    Verhoeven, W.2
  • 14
    • 84857768182 scopus 로고    scopus 로고
    • Analysis of hydrogenase 1 levels reveals an intimate link between carbon and hydrogen metabolism in Escherichia coli K-12
    • Pinske C, McDowall JS, Sargent F, Sawers RG. Analysis of hydrogenase 1 levels reveals an intimate link between carbon and hydrogen metabolism in Escherichia coli K-12. Microbiology 2012;158:856-68.
    • (2012) Microbiology , vol.158 , pp. 856-868
    • Pinske, C.1    McDowall, J.S.2    Sargent, F.3    Sawers, R.G.4
  • 15
    • 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 FA, Fontecilla-Camps JC. Crystal structure of the O2-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b. Structure 2013;21:184-90.
    • (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
    • 7044226199 scopus 로고    scopus 로고
    • Respiratory hydrogen use by Salmonella enterica serovar Typhimurium is essential for virulence
    • Maier RJ, Olczak A, Maier S, Soni S, Gunn J. Respiratory hydrogen use by Salmonella enterica serovar Typhimurium is essential for virulence. Infect Immun 2004;72:6294-9.
    • (2004) Infect Immun , vol.72 , pp. 6294-6299
    • Maier, R.J.1    Olczak, A.2    Maier, S.3    Soni, S.4    Gunn, J.5
  • 17
    • 27944451793 scopus 로고    scopus 로고
    • Hydrogenases in Desulfovibrio vulgaris Hildenborough: Structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase
    • Valente FM, Oliveira AS, Gnadt N, et al. Hydrogenases in Desulfovibrio vulgaris Hildenborough: Structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase. J Biol Inorg Chem 2005;10:667-82.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 667-682
    • Valente, F.M.1    Oliveira, A.S.2    Gnadt, N.3
  • 18
    • 0033135158 scopus 로고    scopus 로고
    • The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
    • Garcin E, Vernede X, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 1999;7:557-66.
    • (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
  • 19
    • 53549119985 scopus 로고    scopus 로고
    • The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum
    • Parkin A, Goldet G, Cavazza C, Fontecilla-Camps JC, Armstrong FA. The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. J Am Chem Soc 2008;130:13410-6.
    • (2008) J am Chem Soc , vol.130 , pp. 13410-13416
    • Parkin, A.1    Goldet, G.2    Cavazza, C.3    Fontecilla-Camps, J.C.4    Armstrong, F.A.5
  • 20
    • 29844441433 scopus 로고    scopus 로고
    • Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases
    • Vincent KA, Parkin A, Lenz O, et al. Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases. J Am Chem Soc 2005;127:18179-89.
    • (2005) J am Chem Soc , vol.127 , pp. 18179-18189
    • Vincent, K.A.1    Parkin, A.2    Lenz, O.3
  • 21
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Shomura Y, Yoon KS, Nishihara H, Higuchi Y. Structural basis for a [4Fe3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 2011;479:253-6.
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 22
    • 84859464540 scopus 로고    scopus 로고
    • X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli
    • Volbeda A, Amara P, Darnault C, et al. X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli. Proc Natl Acad Sci USA 2012;109:5305-10.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5305-5310
    • Volbeda, A.1    Amara, P.2    Darnault, C.3
  • 23
    • 84896774103 scopus 로고    scopus 로고
    • How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase
    • Bowman L, Flanagan L, Fyfe PK, Parkin A, Hunter WN, Sargent F. How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase. Biochem J 2014;458:449-58.
    • (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
  • 24
    • 0022370609 scopus 로고
    • Properties and reactivation of two different deactivated forms of Desulfovibrio gigas hydrogenase
    • Fernandez VM, Hatchikian EC, Cammack R. Properties and reactivation of two different deactivated forms of Desulfovibrio gigas hydrogenase. Biochim Biophys Acta 1985;832:69-79.
    • (1985) Biochim Biophys Acta , vol.832 , pp. 69-79
    • Fernandez, V.M.1    Hatchikian, E.C.2    Cammack, R.3
  • 26
    • 77950503486 scopus 로고    scopus 로고
    • How Escherichia coli is equipped to oxidize hydrogen under different redox conditions
    • Lukey MJ, Parkin A, Roessler MM, et al. How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. J Biol Chem 2010;285:3928-38.
    • (2010) J Biol Chem , vol.285 , pp. 3928-3938
    • Lukey, M.J.1    Parkin, A.2    Roessler, M.M.3
  • 27
    • 77952566611 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: Enzyme activation, redox intermediates and oxygen tolerance
    • Pandelia ME, Fourmond V, Tron-Infossi P, et al. Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance. J Am Chem Soc 2010;132:6991-7004.
    • (2010) J am Chem Soc , vol.132 , pp. 6991-7004
    • Pandelia, M.E.1    Fourmond, V.2    Tron-Infossi, P.3
  • 28
    • 67650273077 scopus 로고    scopus 로고
    • Spectroscopic insights into the oxygen-tolerant membrane-associated [NiFe] hydrogenase of Ralstonia eutropha H16
    • Saggu M, Zebger I, Ludwig M, et al. Spectroscopic insights into the oxygen-tolerant membrane-associated [NiFe] hydrogenase of Ralstonia eutropha H16. J Biol Chem 2009;284:16264-76.
    • (2009) J Biol Chem , vol.284 , pp. 16264-16276
    • Saggu, M.1    Zebger, I.2    Ludwig, M.3
  • 29
    • 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
    • Pandelia ME, Infossi P, Stein M, Giudici-Orticoni MT, Lubitz W. 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 (Camb) 2012;48:823-5.
    • (2012) Chem Commun (Camb) , vol.48 , pp. 823-825
    • Pandelia, M.E.1    Infossi, P.2    Stein, M.3    Giudici-Orticoni, M.T.4    Lubitz, W.5
  • 30
    • 84866518261 scopus 로고    scopus 로고
    • EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from E. Coli, and characterization of the unique [4Fe3S] cluster by HYSCORE
    • Roessler MM, Evans RM, Davies RA, Harmer JR, Armstrong FA. EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from E. coli, and characterization of the unique [4Fe3S] cluster by HYSCORE. J Am Chem Soc 2012;134:15581-94.
    • (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
    • 58649121731 scopus 로고    scopus 로고
    • Oxygen-tolerant H2 oxidation by membrane-bound [NiFe] hydrogenases of Ralstonia species. Coping with low level H2 in air
    • Ludwig M, Cracknell JA, Vincent KA, Armstrong FA, Lenz O. Oxygen-tolerant H2 oxidation by membrane-bound [NiFe] hydrogenases of Ralstonia species. Coping with low level H2 in air. J Biol Chem 2009;284:465-77.
    • (2009) J Biol Chem , vol.284 , pp. 465-477
    • Ludwig, M.1    Cracknell, J.A.2    Vincent, K.A.3    Armstrong, F.A.4    Lenz, O.5
  • 32
    • 84899478527 scopus 로고    scopus 로고
    • Reversible [4Fe3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase
    • Frielingsdorf S, Fritsch J, Schmidt A, et al. Reversible [4Fe3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase. Nat Chem Biol 2014.
    • (2014) Nat Chem Biol
    • Frielingsdorf, S.1    Fritsch, J.2    Schmidt, A.3
  • 33
    • 25544480306 scopus 로고
    • Redox properties of the metal centres in the membrane-bound hydrogenase from Alcaligenes eutrophus CH34
    • Knüttel K, Schneider K, Erkens A, et al. Redox properties of the metal centres in the membrane-bound hydrogenase from Alcaligenes eutrophus CH34. Bull Polish Acad Sci 1994;42:495-511.
    • (1994) Bull Polish Acad Sci , vol.42 , pp. 495-511
    • Knüttel, K.1    Schneider, K.2    Erkens, A.3
  • 34
    • 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
    • Pandelia ME, Nitschke W, Infossi P, Giudici-Orticoni MT, Bill E, Lubitz W. 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 2011;108:6097-102.
    • (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
  • 35
    • 84872194321 scopus 로고    scopus 로고
    • Electronic structure of the unique [4Fe3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mössbauer and EPR spectroscopy
    • Pandelia ME, Bykov D, Izsak R, et al. Electronic structure of the unique [4Fe3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mössbauer and EPR spectroscopy. Proc Natl Acad Sci USA 2013;110:483-8.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 483-488
    • Pandelia, M.E.1    Bykov, D.2    Izsak, R.3
  • 36
    • 0029088950 scopus 로고
    • Reversible super-reduction of the cubane [4Fe4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions: EPR spectroscopic and electrochemical studies
    • Heering HA, Bulsink YBM, Hagen WR, Meyer TE. Reversible super-reduction of the cubane [4Fe4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions: EPR spectroscopic and electrochemical studies. Eur J Biochem 1995;232:811-7.
    • (1995) Eur J Biochem , vol.232 , pp. 811-817
    • Heering, H.A.1    Bulsink, Y.2    Hagen, W.R.3    Meyer, T.E.4
  • 37
    • 0015835755 scopus 로고
    • Super-reduction of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide
    • Cammack R. “Super-reduction” of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide. Biochem Biophys Res Commun 1973;54:548-54.
    • (1973) Biochem Biophys Res Commun , vol.54 , pp. 548-554
    • Cammack, R.1
  • 39
    • 79955072473 scopus 로고    scopus 로고
    • A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase
    • Goris T, Wait AF, Saggu M, et al. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nat Chem Biol 2011;7:310-8.
    • (2011) Nat Chem Biol , vol.7 , pp. 310-318
    • Goris, T.1    Wait, A.F.2    Saggu, M.3
  • 40
    • 83455221549 scopus 로고    scopus 로고
    • A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16
    • Frielingsdorf S, Schubert T, Pohlmann A, Lenz O, Friedrich B. A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16. Biochemistry 2011;50:10836-43.
    • (2011) Biochemistry , vol.50 , pp. 10836-10843
    • Frielingsdorf, S.1    Schubert, T.2    Pohlmann, A.3    Lenz, O.4    Friedrich, B.5
  • 41
    • 80052235153 scopus 로고    scopus 로고
    • Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha immobilized on electrodes
    • Sezer M, Frielingsdorf S, Millo D, et al. Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha immobilized on electrodes. J Phys Chem B 2011;115:10368-74.
    • (2011) J Phys Chem B , vol.115 , pp. 10368-10374
    • Sezer, M.1    Frielingsdorf, S.2    Millo, D.3
  • 42
    • 77957276541 scopus 로고    scopus 로고
    • Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: Role of lipids and physiological partners in enzyme stability and activity
    • Infossi P, Lojou E, Chauvin JP, Herbette G, Brugna M, Giudici-Orticoni MT. Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: Role of lipids and physiological partners in enzyme stability and activity. Int J Hydrogen Energ 2010;35:10778-89.
    • (2010) Int J Hydrogen Energ , vol.35 , pp. 10778-10789
    • Infossi, P.1    Lojou, E.2    Chauvin, J.P.3    Herbette, G.4    Brugna, M.5    Giudici-Orticoni, M.T.6
  • 43
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [NiFe]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster
    • Lukey MJ, Roessler MM, Parkin A, et al. Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. J Am Chem Soc 2011;133:16881-92.
    • (2011) J am Chem Soc , vol.133 , pp. 16881-16892
    • Lukey, M.J.1    Roessler, M.M.2    Parkin, A.3
  • 44
    • 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
    • Evans RM, Parkin A, Roessler MM, et al. 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 2013;135:2694-707.
    • (2013) J am Chem Soc , vol.135 , pp. 2694-2707
    • Evans, R.M.1    Parkin, A.2    Roessler, M.M.3
  • 45
    • 84889261366 scopus 로고    scopus 로고
    • Catalytic production of hydrogen peroxide and water by oxygentolerant [NiFe]-hydrogenase during H2 cycling in the presence of O2
    • Lauterbach L, Lenz O. Catalytic production of hydrogen peroxide and water by oxygentolerant [NiFe]-hydrogenase during H2 cycling in the presence of O2. J Am Chem Soc 2013;135:17897-905.
    • (2013) J am Chem Soc , vol.135 , pp. 17897-17905
    • Lauterbach, L.1    Lenz, O.2
  • 46
    • 77955336661 scopus 로고    scopus 로고
    • Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst
    • Wait AF, Parkin A, Morley GM, dos Santos L, Armstrong FA. Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst. J Phys Chem C 2010;114:12003-9.
    • (2010) J Phys Chem C , vol.114 , pp. 12003-12009
    • Wait, A.F.1    Parkin, A.2    Morley, G.M.3    Dos Santos, L.4    Armstrong, F.A.5
  • 47
    • 84863899218 scopus 로고    scopus 로고
    • Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
    • Hexter SV, Grey F, Happe T, Climent V, Armstrong FA. Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proc Natl Acad Sci USA 2012;109:11516-21.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11516-11521
    • Hexter, S.V.1    Grey, F.2    Happe, T.3    Climent, V.4    Armstrong, F.A.5
  • 48
    • 84896967315 scopus 로고    scopus 로고
    • Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer
    • Murphy BJ, Sargent F, Armstrong FA. Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer. Energ Environ Sci 2014;7:1426.
    • (2014) Energ Environ Sci , vol.7 , pp. 1426
    • Murphy, B.J.1    Sargent, F.2    Armstrong, F.A.3
  • 49
    • 55249110895 scopus 로고    scopus 로고
    • Genomic view of energy metabolism in Ralstonia eutropha H16
    • Cramm R. Genomic view of energy metabolism in Ralstonia eutropha H16. J Mol Microbiol Biotechnol 2009;16:38-52.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 38-52
    • Cramm, R.1
  • 50
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington SJ, Skehel JM, Gennis RB, Walker JE. Relationship between mitochondrial NADH ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 1991;30:2166-75.
    • (1991) Biochemistry , vol.30 , pp. 2166-2175
    • Pilkington, S.J.1    Skehel, J.M.2    Gennis, R.B.3    Walker, J.E.4
  • 51
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis
    • Appel J, Phunpruch S, Steinmüller K, Schulz R. The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis. Arch Microbiol 2000;173:333-8.
    • (2000) Arch Microbiol , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 52
    • 33845355867 scopus 로고    scopus 로고
    • Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module
    • Long M, Liu J, Chen Z, Bleijlevens B, Roseboom W, Albracht SP. Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. J Biol Inorg Chem 2007;12:62-78.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 62-78
    • Long, M.1    Liu, J.2    Chen, Z.3    Bleijlevens, B.4    Roseboom, W.5    Albracht, S.P.6
  • 54
    • 84893141463 scopus 로고    scopus 로고
    • The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions
    • Gutekunst K, Chen X, Schreiber K, Kaspar U, Makam S, Appel J. The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions. J Biol Chem 2014;289:1930-7.
    • (2014) J Biol Chem , vol.289 , pp. 1930-1937
    • Gutekunst, K.1    Chen, X.2    Schreiber, K.3    Kaspar, U.4    Makam, S.5    Appel, J.6
  • 55
    • 77955565900 scopus 로고    scopus 로고
    • A second soluble Hox-type NiFe enzyme completes the hydrogenase set in Thiocapsa roseopersicina BBS
    • Maroti J, Farkas A, Nagy IK, et al. A second soluble Hox-type NiFe enzyme completes the hydrogenase set in Thiocapsa roseopersicina BBS. Appl Environ Microbiol 2010;76:5113-23.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5113-5123
    • Maroti, J.1    Farkas, A.2    Nagy, I.K.3
  • 56
    • 0021753750 scopus 로고
    • Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b
    • Schneider K, Cammack R, Schlegel HG. Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b. Eur J Biochem 1984;142:75-84.
    • (1984) Eur J Biochem , vol.142 , pp. 75-84
    • Schneider, K.1    Cammack, R.2    Schlegel, H.G.3
  • 57
    • 0017110320 scopus 로고
    • Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H16
    • Schneider K, Schlegel HG. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H16. Biochim Biophys Acta 1976;452:66-80.
    • (1976) Biochim Biophys Acta , vol.452 , pp. 66-80
    • Schneider, K.1    Schlegel, H.G.2
  • 58
    • 33744503148 scopus 로고    scopus 로고
    • [NiFe]-hydrogenases of Ralstonia eutropha H16: Modular enzymes for oxygen-tolerant biological hydrogen oxidation
    • Burgdorf T, Lenz O, Buhrke T, et al. [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation. J Mol Microbiol Biotechnol 2005;10:181-96.
    • (2005) J Mol Microbiol Biotechnol , vol.10 , pp. 181-196
    • Burgdorf, T.1    Lenz, O.2    Buhrke, T.3
  • 59
    • 0019396561 scopus 로고
    • Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16
    • Schneider K, Schlegel HG. Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16. Biochem J 1981;193:99-107.
    • (1981) Biochem J , vol.193 , pp. 99-107
    • Schneider, K.1    Schlegel, H.G.2
  • 60
    • 0027120930 scopus 로고
    • Hydrogenase mutants of Alcaligenes eutrophus H16 show alterations in the electron transport system
    • Kömen R, Schmidt K, Friedrich B. Hydrogenase mutants of Alcaligenes eutrophus H16 show alterations in the electron transport system. FEMS Microbiol Lett 1992;75:173-8.
    • (1992) FEMS Microbiol Lett , vol.75 , pp. 173-178
    • Kömen, R.1    Schmidt, K.2    Friedrich, B.3
  • 61
    • 0021173250 scopus 로고
    • Hydrogen evolution by strictly aerobic hydrogen bacteria under anaerobic conditions
    • Kuhn M, Steinbüchel A, Schlegel HG. Hydrogen evolution by strictly aerobic hydrogen bacteria under anaerobic conditions. J Bacteriol 1984;159:633-9.
    • (1984) J Bacteriol , vol.159 , pp. 633-639
    • Kuhn, M.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 62
    • 20244376022 scopus 로고    scopus 로고
    • The soluble NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH
    • Burgdorf T, van der Linden E, Bernhard M, et al. The soluble NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH. J Bacteriol 2005;187:3122-32.
    • (2005) J Bacteriol , vol.187 , pp. 3122-3132
    • Burgdorf, T.1    Van Der Linden, E.2    Bernhard, M.3
  • 63
    • 73649123872 scopus 로고    scopus 로고
    • Overexpression, isolation and spectroscopic characterization of the bidirectional [NiFe]-hydrogenase from Synechocystis sp. PCC 6803
    • Germer F, Zebger I, Saggu M, Lendzian F, Schulz R, Appel J. Overexpression, isolation and spectroscopic characterization of the bidirectional [NiFe]-hydrogenase from Synechocystis sp. PCC 6803. J Biol Chem 2009; 284:36462-36472.
    • (2009) J Biol Chem , vol.284 , pp. 36462-36472
    • Germer, F.1    Zebger, I.2    Saggu, M.3    Lendzian, F.4    Schulz, R.5    Appel, J.6
  • 64
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov LA, Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 2006;311:1430-6.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 65
    • 84857915091 scopus 로고    scopus 로고
    • NAD(H)-coupled hydrogen cycling-structure-function relationships of bidirectional [NiFe] hydrogenases
    • Horch M, Lauterbach L, Lenz O, Hildebrandt P, Zebger I. NAD(H)-coupled hydrogen cycling-structure-function relationships of bidirectional [NiFe] hydrogenases. FEBS Lett 2012;586:545-56.
    • (2012) FEBS Lett , vol.586 , pp. 545-556
    • Horch, M.1    Lauterbach, L.2    Lenz, O.3    Hildebrandt, P.4    Zebger, I.5
  • 66
    • 80053898681 scopus 로고    scopus 로고
    • Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha
    • Lauterbach L, Idris Z, Vincent KA, Lenz O. Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha. PLoS One 2011;6:e25939.
    • (2011) Plos One , vol.6
    • Lauterbach, L.1    Idris, Z.2    Vincent, K.A.3    Lenz, O.4
  • 67
    • 79951900196 scopus 로고    scopus 로고
    • The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha-insights into catalysis and redox interconversions
    • Lauterbach L, Liu JA, Horch M, et al. The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha-insights into catalysis and redox interconversions. Eur J Inorg Chem 2011:1067-79.
    • (2011) Eur J Inorg Chem , pp. 1067-1079
    • Lauterbach, L.1    Liu, J.A.2    Horch, M.3
  • 68
    • 1342343929 scopus 로고    scopus 로고
    • Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha
    • van der Linden E, Faber BW, Bleijlevens B, et al. Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha. Eur JBiochem 2004;271:801-8.
    • (2004) Eur Jbiochem , vol.271 , pp. 801-808
    • Van Der Linden, E.1    Faber, B.W.2    Bleijlevens, B.3
  • 69
    • 0028951871 scopus 로고
    • EPR and Mossbauer spectroscopic studies on the tetrameric, NAD-linked hydrogenase of Nocardia opaca-1b and its 2 dimers.1. The beta-delta-dimer-a prototype of a simple hydrogenase
    • Zaborosch C, Köster M, Bill E, Schneider K, Schlegel HG, Trautwein AX. EPR and Mossbauer spectroscopic studies on the tetrameric, NAD-linked hydrogenase of Nocardia opaca-1b and its 2 dimers.1. The beta-delta-dimer-a prototype of a simple hydrogenase. Biometals 1995;8:149-62.
    • (1995) Biometals , vol.8 , pp. 149-162
    • Zaborosch, C.1    Köster, M.2    Bill, E.3    Schneider, K.4    Schlegel, H.G.5    Trautwein, A.X.6
  • 70
    • 78349301233 scopus 로고    scopus 로고
    • Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy
    • Horch M, Lauterbach L, Saggu M, et al. Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy. Angew Chem Int Ed Engl 2010;49:8026-9.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 8026-8029
    • Horch, M.1    Lauterbach, L.2    Saggu, M.3
  • 71
    • 0018795813 scopus 로고
    • The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus
    • Schneider K, Cammack R, Schlegel HG, Hall DO. The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus. Biochim Biophys Acta 1979;578:445-61.
    • (1979) Biochim Biophys Acta , vol.578 , pp. 445-461
    • Schneider, K.1    Cammack, R.2    Schlegel, H.G.3    Hall, D.O.4
  • 72
    • 32444440595 scopus 로고    scopus 로고
    • An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: New insights into its (in)stability and spectroscopic properties
    • van der Linden E, Burgdorf T, de Lacey AL, et al. An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties. J Biol Inorg Chem 2006;11:247-60.
    • (2006) J Biol Inorg Chem , vol.11 , pp. 247-260
    • Van Der Linden, E.1    Burgdorf, T.2    De Lacey, A.L.3
  • 73
    • 0002151485 scopus 로고    scopus 로고
    • The NAD linked soluble hydrogenase from Alcaligenes eutrophus H16: Detection and characterization of EPR signals deriving from nickel and flavin
    • Erkens A, Schneider K, Müller A. The NAD linked soluble hydrogenase from Alcaligenes eutrophus H16: Detection and characterization of EPR signals deriving from nickel and flavin. J Biol Inorg Chem 1996;1:99-110.
    • (1996) J Biol Inorg Chem , vol.1 , pp. 99-110
    • Erkens, A.1    Schneider, K.2    Müller, A.3
  • 74
    • 33747502852 scopus 로고    scopus 로고
    • Spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F
    • Fichtner C, Laurich C, Bothe E, Lubitz W. Spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F. Biochemistry 2006;45:9706-16.
    • (2006) Biochemistry , vol.45 , pp. 9706-9716
    • Fichtner, C.1    Laurich, C.2    Bothe, E.3    Lubitz, W.4
  • 75
    • 0033956391 scopus 로고    scopus 로고
    • Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha
    • Happe RP, Roseboom W, Egert G, et al. Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha. FEBS Lett 2000;466:259-63.
    • (2000) FEBS Lett , vol.466 , pp. 259-263
    • Happe, R.P.1    Roseboom, W.2    Egert, G.3
  • 76
    • 3943058946 scopus 로고    scopus 로고
    • The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
    • Van der Linden E, Burgdorf T, Bernhard M, Bleijlevens B, Friedrich B, Albracht SP. The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen. J Biol Inorg Chem 2004;9:616-26.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 616-626
    • Van Der Linden, E.1    Burgdorf, T.2    Bernhard, M.3    Bleijlevens, B.4    Friedrich, B.5    Albracht, S.P.6
  • 77
    • 19944431547 scopus 로고    scopus 로고
    • Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy
    • Burgdorf T, Löscher S, Liebisch P, et al. Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy. J Am Chem Soc 2005;127:576-92.
    • (2005) J am Chem Soc , vol.127 , pp. 576-592
    • Burgdorf, T.1    Löscher, S.2    Liebisch, P.3
  • 78
    • 10544248165 scopus 로고    scopus 로고
    • Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and the effects of redox poise
    • Gu ZJ, Dong J, Allan CB, et al. Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and the effects of redox poise. J Am Chem Soc 1996;118:11155-65.
    • (1996) J am Chem Soc , vol.118 , pp. 11155-11165
    • Gu, Z.J.1    Dong, J.2    Allan, C.B.3
  • 79
    • 79960588023 scopus 로고    scopus 로고
    • The [NiFe]-hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 works bidirectionally with a bias to H2 production
    • McIntosh CL, Germer F, Schulz R, Appel J, Jones AK. The [NiFe]-hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 works bidirectionally with a bias to H2 production. J Am Chem Soc 2011;133:11308-19.
    • (2011) J am Chem Soc , vol.133 , pp. 11308-11319
    • McIntosh, C.L.1    Germer, F.2    Schulz, R.3    Appel, J.4    Jones, A.K.5
  • 80
    • 0019365984 scopus 로고
    • Formation of enzymes of autotrophic metabolism during heterotrophic growth of Alcaligenes eutrophus
    • Friedrich CG, Friedrich B, Bowien B. Formation of enzymes of autotrophic metabolism during heterotrophic growth of Alcaligenes eutrophus. J Gen Microbiol 1981;122:69-78.
    • (1981) J Gen Microbiol , vol.122 , pp. 69-78
    • Friedrich, C.G.1    Friedrich, B.2    Bowien, B.3
  • 81
    • 0043009827 scopus 로고    scopus 로고
    • Complete nucleotide sequence of pHG1: A Ralstonia eutropha H16 megaplasmid encoding key enzymes of H2-based ithoautotrophy and anaerobiosis
    • Schwartz E, Henne A, Cramm R, Eitinger T, Friedrich B, Gottschalk G. Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H2-based ithoautotrophy and anaerobiosis. J Mol Biol 2003;332:369-83.
    • (2003) J Mol Biol , vol.332 , pp. 369-383
    • Schwartz, E.1    Henne, A.2    Cramm, R.3    Eitinger, T.4    Friedrich, B.5    Gottschalk, G.6
  • 82
    • 0029764690 scopus 로고    scopus 로고
    • The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling
    • Bernhard M, Schwartz E, Rietdorf J, Friedrich B. The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling. J Bacteriol 1996;178:4522-9.
    • (1996) J Bacteriol , vol.178 , pp. 4522-4529
    • Bernhard, M.1    Schwartz, E.2    Rietdorf, J.3    Friedrich, B.4
  • 83
    • 59049107349 scopus 로고    scopus 로고
    • Concerted action of two novel auxiliary proteins in assembly of the active site in a membrane-bound [NiFe] hydrogenase
    • Ludwig M, Schubert T, Zebger I, et al. Concerted action of two novel auxiliary proteins in assembly of the active site in a membrane-bound [NiFe] hydrogenase. J Biol Chem 2009;284:2159-68.
    • (2009) J Biol Chem , vol.284 , pp. 2159-2168
    • Ludwig, M.1    Schubert, T.2    Zebger, I.3
  • 84
    • 34748882510 scopus 로고    scopus 로고
    • Chaperones specific for the membranebound [NiFe]-hydrogenase interact with the Tat signal peptide of the small subunit precursor in Ralstonia eutropha H16
    • Schubert T, Lenz O, Krause E, Volkmer R, Friedrich B. Chaperones specific for the membranebound [NiFe]-hydrogenase interact with the Tat signal peptide of the small subunit precursor in Ralstonia eutropha H16. Mol Microbiol 2007;66:453-67.
    • (2007) Mol Microbiol , vol.66 , pp. 453-467
    • Schubert, T.1    Lenz, O.2    Krause, E.3    Volkmer, R.4    Friedrich, B.5
  • 85
    • 79956101455 scopus 로고    scopus 로고
    • The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe] hydrogenase in Ralstonia eutropha H16
    • Fritsch J, Lenz O, Friedrich B. The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe] hydrogenase in Ralstonia eutropha H16. J Bacteriol 2011;193:2487-97.
    • (2011) J Bacteriol , vol.193 , pp. 2487-2497
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 86
    • 84896306720 scopus 로고    scopus 로고
    • Rubredoxin-related maturation factor guarantees metal cofactor integrity during aerobic biosynthesis of membrane-bound [NiFe] hydrogenase
    • Fritsch J, Siebert E, Priebe J, et al. Rubredoxin-related maturation factor guarantees metal cofactor integrity during aerobic biosynthesis of membrane-bound [NiFe] hydrogenase. J Biol Chem 2014;289:7982-93.
    • (2014) J Biol Chem , vol.289 , pp. 7982-7993
    • Fritsch, J.1    Siebert, E.2    Priebe, J.3
  • 88
    • 84869029258 scopus 로고    scopus 로고
    • A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase
    • Bürstel I, Siebert E, Winter G, et al. A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase. J Biol Chem 2012;287:38845-53.
    • (2012) J Biol Chem , vol.287 , pp. 38845-38853
    • Bürstel, I.1    Siebert, E.2    Winter, G.3
  • 89
    • 0029841365 scopus 로고    scopus 로고
    • The hydrogenase gene cluster of Rhizobium leguminosarum bv. Viciae contains an additional gene (hypX), which encodes a protein with sequence similarity to the N10-formyltetrahydrofolate-dependent enzyme family and is required for nickel-dependent hydrogenase processing and activity
    • Rey L, Fernandez D, Brito B, et al. The hydrogenase gene cluster of Rhizobium leguminosarum bv. viciae contains an additional gene (hypX), which encodes a protein with sequence similarity to the N10-formyltetrahydrofolate-dependent enzyme family and is required for nickel-dependent hydrogenase processing and activity. Molecular and General Genetics 1996;252:237-48.
    • (1996) Molecular and General Genetics , vol.252 , pp. 237-248
    • Rey, L.1    Fernandez, D.2    Brito, B.3
  • 90
    • 84455192785 scopus 로고    scopus 로고
    • Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase
    • Bürstel I, Hummel P, Siebert E, et al. Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase. J Biol Chem 2011;286:44937-44.
    • (2011) J Biol Chem , vol.286 , pp. 44937-44944
    • Bürstel, I.1    Hummel, P.2    Siebert, E.3
  • 91
    • 14644419534 scopus 로고    scopus 로고
    • Transcriptional regulation of the uptake [NiFe] hydrogenase genes in Rhodobacter capsulatus
    • Vignais PM, Elsen S, Colbeau A. Transcriptional regulation of the uptake [NiFe] hydrogenase genes in Rhodobacter capsulatus. Biochem Soc Trans 2005;33:28-32.
    • (2005) Biochem Soc Trans , vol.33 , pp. 28-32
    • Vignais, P.M.1    Elsen, S.2    Colbeau, A.3
  • 92
    • 0032514688 scopus 로고    scopus 로고
    • A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus
    • Lenz O, Friedrich B. A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus. Proc Natl Acad Sci USA 1998;95:12474-9.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12474-12479
    • Lenz, O.1    Friedrich, B.2
  • 94
    • 1642442726 scopus 로고    scopus 로고
    • The H2-sensing complex of Ralstonia eutropha: Interaction between a regulatory [NiFe] hydrogenase and a histidine protein kinase
    • Buhrke T, Lenz O, Porthun A, Friedrich B. The H2-sensing complex of Ralstonia eutropha: interaction between a regulatory [NiFe] hydrogenase and a histidine protein kinase. Mol Microbiol 2004;51:1677-89.
    • (2004) Mol Microbiol , vol.51 , pp. 1677-1689
    • Buhrke, T.1    Lenz, O.2    Porthun, A.3    Friedrich, B.4
  • 95
    • 0028007441 scopus 로고
    • Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression
    • Black LK, Fu C, Maier RJ. Sequences and characterization of hupU and hupV genes of Bradyrhizobium japonicum encoding a possible nickel-sensing complex involved in hydrogenase expression. J Bacteriol 1994;176:7102-6.
    • (1994) J Bacteriol , vol.176 , pp. 7102-7106
    • Black, L.K.1    Fu, C.2    Maier, R.J.3
  • 96
    • 0029812909 scopus 로고    scopus 로고
    • The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus
    • Elsen S, Colbeau A, Chabert J, Vignais PM. The hupTUV operon is involved in negative control of hydrogenase synthesis in Rhodobacter capsulatus. J Bacteriol 1996;178:5174-81.
    • (1996) J Bacteriol , vol.178 , pp. 5174-5181
    • Elsen, S.1    Colbeau, A.2    Chabert, J.3    Vignais, P.M.4
  • 97
    • 0035844249 scopus 로고    scopus 로고
    • The H2 sensor of Ralstonia eutropha. Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase
    • Bernhard M, Buhrke T, Bleijlevens B, et al. The H2 sensor of Ralstonia eutropha. Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase. J Biol Chem 2001;276:15592-7.
    • (2001) J Biol Chem , vol.276 , pp. 15592-15597
    • Bernhard, M.1    Buhrke, T.2    Bleijlevens, B.3
  • 98
    • 0032518335 scopus 로고    scopus 로고
    • Rhodobacter capsulatus HypF is involved in regulation of hydrogenase synthesis through the HupUV proteins
    • Colbeau A, Elsen S, Tomiyama M, Zorin NA, Dimon B, Vignais PM. Rhodobacter capsulatus HypF is involved in regulation of hydrogenase synthesis through the HupUV proteins. Eur J Biochem 1998;251:65-71.
    • (1998) Eur J Biochem , vol.251 , pp. 65-71
    • Colbeau, A.1    Elsen, S.2    Tomiyama, M.3    Zorin, N.A.4    Dimon, B.5    Vignais, P.M.6
  • 99
    • 0035205325 scopus 로고    scopus 로고
    • Involvement of hyp gene products in maturation of the H2-sensing [NiFe] hydrogenase of Ralstonia eutropha
    • Buhrke T, Bleijlevens B, Albracht SP, Friedrich B. Involvement of hyp gene products in maturation of the H2-sensing [NiFe] hydrogenase of Ralstonia eutropha. J Bacteriol 2001;183:7087-93.
    • (2001) J Bacteriol , vol.183 , pp. 7087-7093
    • Buhrke, T.1    Bleijlevens, B.2    Albracht, S.P.3    Friedrich, B.4
  • 100
    • 0031737764 scopus 로고    scopus 로고
    • Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus
    • Pierik AJ, Schmelz M, Lenz O, Friedrich B, Albracht SP. Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus. FEBS Lett 1998;438:231-5.
    • (1998) FEBS Lett , vol.438 , pp. 231-235
    • Pierik, A.J.1    Schmelz, M.2    Lenz, O.3    Friedrich, B.4    Albracht, S.P.5
  • 101
    • 0142152415 scopus 로고    scopus 로고
    • Direct detection of a hydrogen ligand in the [NiFe] center of the regulatory H2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy
    • Brecht M, van Gastel M, Buhrke T, Friedrich B, Lubitz W. Direct detection of a hydrogen ligand in the [NiFe] center of the regulatory H2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy. J Am Chem Soc 2003;125:13075-83.
    • (2003) J am Chem Soc , vol.125 , pp. 13075-13083
    • Brecht, M.1    Van Gastel, M.2    Buhrke, T.3    Friedrich, B.4    Lubitz, W.5
  • 102
    • 33845659958 scopus 로고    scopus 로고
    • Impact of alterations near the [NiFe] active site on the function of the H2 sensor from Ralstonia eutropha
    • Gebler A, Burgdorf T, De Lacey AL, et al. Impact of alterations near the [NiFe] active site on the function of the H2 sensor from Ralstonia eutropha. FEBS J 2007;274:74-85.
    • (2007) FEBS J , vol.274 , pp. 74-85
    • Gebler, A.1    Burgdorf, T.2    De Lacey, A.L.3
  • 103
    • 21244482538 scopus 로고    scopus 로고
    • Reduction of unusual iron-sulfur clusters in the H2-sensing regulatory Ni-Fe hydrogenase from Ralstonia eutropha H16
    • Buhrke T, Löscher S, Lenz O, et al. Reduction of unusual iron-sulfur clusters in the H2-sensing regulatory Ni-Fe hydrogenase from Ralstonia eutropha H16. J Biol Chem 2005;280:19488-95.
    • (2005) J Biol Chem , vol.280 , pp. 19488-19495
    • Buhrke, T.1    Löscher, S.2    Lenz, O.3
  • 104
    • 84884318697 scopus 로고    scopus 로고
    • [NiFe] hydrogenases: A common active site for hydrogen metabolism under diverse conditions
    • Shafaat HS, Rüdiger O, Ogata H, Lubitz W. [NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions. Biochim Biophys Acta 2013;1827:986-1002.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 986-1002
    • Shafaat, H.S.1    Rüdiger, O.2    Ogata, H.3    Lubitz, W.4
  • 106
    • 0031180380 scopus 로고    scopus 로고
    • Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
    • Montet Y, Amara P, Volbeda A, et al. Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nat Struct Biol 1997;4:523-6.
    • (1997) Nat Struct Biol , vol.4 , pp. 523-526
    • Montet, Y.1    Amara, P.2    Volbeda, A.3
  • 107
    • 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
    • Ogata H, Mizoguchi Y, Mizuno N, et al. 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 2002;124:11628-35.
    • (2002) J am Chem Soc , vol.124 , pp. 11628-11635
    • Ogata, H.1    Mizoguchi, Y.2    Mizuno, N.3
  • 108
    • 21244441201 scopus 로고    scopus 로고
    • Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site
    • Buhrke T, Lenz O, Krauss N, Friedrich B. Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site. J Biol Chem 2005;280:23791-6.
    • (2005) J Biol Chem , vol.280 , pp. 23791-23796
    • Buhrke, T.1    Lenz, O.2    Krauss, N.3    Friedrich, B.4
  • 109
    • 23644448705 scopus 로고    scopus 로고
    • Enlarging the gas access channel to the active site renders the regulatory hydrogenase HupUV of Rhodobacter capsulatus O2 sensitive without affecting its transductory activity
    • Duche O, Elsen S, Cournac L, Colbeau A. Enlarging the gas access channel to the active site renders the regulatory hydrogenase HupUV of Rhodobacter capsulatus O2 sensitive without affecting its transductory activity. FEBS J 2005;272:3899-908.
    • (2005) FEBS J , vol.272 , pp. 3899-3908
    • Duche, O.1    Elsen, S.2    Cournac, L.3    Colbeau, A.4
  • 110
    • 49649094062 scopus 로고    scopus 로고
    • Experimental approaches to kinetics of gas diffusion in hydrogenase
    • Leroux F, Dementin S, Burlat B, et al. Experimental approaches to kinetics of gas diffusion in hydrogenase. Proc Natl Acad Sci USA 2008;105:11188-93.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11188-11193
    • Leroux, F.1    Dementin, S.2    Burlat, B.3
  • 111
    • 74049124292 scopus 로고    scopus 로고
    • Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase
    • Liebgott PP, Leroux F, Burlat B, et al. Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase. Nat Chem Biol 2010;6:63-70.
    • (2010) Nat Chem Biol , vol.6 , pp. 63-70
    • Liebgott, P.P.1    Leroux, F.2    Burlat, B.3
  • 112
    • 79851504099 scopus 로고    scopus 로고
    • Original design of an oxygen-tolerant [NiFe] hydrogenase: Major effect of a valine-to-cysteine mutation near the active site
    • Liebgott PP, de Lacey AL, Burlat B, et al. Original design of an oxygen-tolerant [NiFe] hydrogenase: major effect of a valine-to-cysteine mutation near the active site. J Am Chem Soc 2011;133:986-97.
    • (2011) J am Chem Soc , vol.133 , pp. 986-997
    • Liebgott, P.P.1    De Lacey, A.L.2    Burlat, B.3
  • 113
    • 84870589774 scopus 로고    scopus 로고
    • Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants
    • Abou Hamdan A, Liebgott PP, Fourmond V, et al. Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants. Proc Natl Acad Sci USA 2012;109:19916-21.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19916-19921
    • Abou Hamdan, A.1    Liebgott, P.P.2    Fourmond, V.3
  • 114
    • 0029845048 scopus 로고    scopus 로고
    • Soil microorganisms as controllers of atmospheric trace gases (H2, CO, CH4, OCS, N2O, and NO)
    • Conrad R. Soil microorganisms as controllers of atmospheric trace gases (H2, CO, CH4, OCS, N2O, and NO). Microbiol Rev 1996;60:609-40.
    • (1996) Microbiol Rev , vol.60 , pp. 609-640
    • Conrad, R.1
  • 115
    • 0003188761 scopus 로고
    • Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas
    • Wilde E. Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas. Archiv für Mikrobiologie 1962;43:109-37.
    • (1962) Archiv für Mikrobiologie , vol.43 , pp. 109-137
    • Wilde, E.1
  • 116
    • 33745519799 scopus 로고    scopus 로고
    • The overwhelming role of soils in the global atmospheric hydrogen cycle
    • Rhee TS, Brenninkmeijer CAM, Röckmann T. The overwhelming role of soils in the global atmospheric hydrogen cycle. Atmos Chem Phys 2006;6:1611-25.
    • (2006) Atmos Chem Phys , vol.6 , pp. 1611-1625
    • Rhee, T.S.1    Brenninkmeijer, C.2    Röckmann, T.3
  • 117
    • 0028045283 scopus 로고
    • Demonstration of two different H2-oxidizing activities in soil using an H2 consumption and a tritium exchange assay
    • Häring V, Conrad R. Demonstration of two different H2-oxidizing activities in soil using an H2 consumption and a tritium exchange assay. Biol Fertil Soils 1994;17:125-8.
    • (1994) Biol Fertil Soils , vol.17 , pp. 125-128
    • Häring, V.1    Conrad, R.2
  • 118
    • 53849096342 scopus 로고    scopus 로고
    • Isolation of Streptomyces sp. PCB7, the first microorganism demonstrating high-affinity uptake of tropospheric H2
    • Constant P, Poissant L, Villemur R. Isolation of Streptomyces sp. PCB7, the first microorganism demonstrating high-affinity uptake of tropospheric H2. ISME J 2008;2:1066-76.
    • (2008) ISME J , vol.2 , pp. 1066-1076
    • Constant, P.1    Poissant, L.2    Villemur, R.3
  • 119
    • 77953950338 scopus 로고    scopus 로고
    • Streptomycetes contributing to atmospheric molecular hydrogen soil uptake are widespread and encode a putative high-affinity [NiFe]-hydrogenase
    • Constant P, Chowdhury SP, Pratscher J, Conrad R. Streptomycetes contributing to atmospheric molecular hydrogen soil uptake are widespread and encode a putative high-affinity [NiFe]-hydrogenase. Environ Microbiol 2010;12:821-9.
    • (2010) Environ Microbiol , vol.12 , pp. 821-829
    • Constant, P.1    Chowdhury, S.P.2    Pratscher, J.3    Conrad, R.4
  • 120
    • 84891634880 scopus 로고    scopus 로고
    • Three different [NiFe] hydrogenases confer metabolic flexibility in the obligate aerobe Mycobacterium smegmatis
    • Berney M, Greening C, Hards K, Collins D, Cook GM. Three different [NiFe] hydrogenases confer metabolic flexibility in the obligate aerobe Mycobacterium smegmatis. Environ Microbiol 2014;16:318-30.
    • (2014) Environ Microbiol , vol.16 , pp. 318-330
    • Berney, M.1    Greening, C.2    Hards, K.3    Collins, D.4    Cook, G.M.5
  • 121
    • 77649141318 scopus 로고    scopus 로고
    • Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia
    • Berney M, Cook GM. Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia. PLoS One 2010;5:e8614.
    • (2010) Plos One , vol.5
    • Berney, M.1    Cook, G.M.2
  • 122
    • 84896541745 scopus 로고    scopus 로고
    • A soil actinobacterium scavenges atmospheric H2 using two membrane-associated, oxygen-dependent [NiFe] hydrogenases
    • Greening C, Berney M, Hards K, Cook GM, Conrad R. A soil actinobacterium scavenges atmospheric H2 using two membrane-associated, oxygen-dependent [NiFe] hydrogenases. Proc Natl Acad Sci USA 2014;111:4257-61.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4257-4261
    • Greening, C.1    Berney, M.2    Hards, K.3    Cook, G.M.4    Conrad, R.5
  • 123
    • 84884237449 scopus 로고    scopus 로고
    • Novel, oxygen-insensitive group 5 [NiFe]-hydrogenase in Ralstonia eutropha
    • Schäfer C, Friedrich B, Lenz O. Novel, oxygen-insensitive group 5 [NiFe]-hydrogenase in Ralstonia eutropha. Appl Environ Microbiol 2013;79:5137-45.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 5137-5145
    • Schäfer, C.1    Friedrich, B.2    Lenz, O.3
  • 124
    • 40149096419 scopus 로고    scopus 로고
    • Enzymatic oxidation of H2 in atmospheric O2: The electrochemistry of energy generation from trace H2 by aerobic microorganisms
    • Cracknell JA, Vincent KA, Ludwig M, Lenz O, Friedrich B, Armstrong FA. Enzymatic oxidation of H2 in atmospheric O2: the electrochemistry of energy generation from trace H2 by aerobic microorganisms. J Am Chem Soc 2008;130:424-5.
    • (2008) J am Chem Soc , vol.130 , pp. 424-425
    • Cracknell, J.A.1    Vincent, K.A.2    Ludwig, M.3    Lenz, O.4    Friedrich, B.5    Armstrong, F.A.6
  • 125
    • 33845270211 scopus 로고    scopus 로고
    • Electricity from low-level H2 in still air-an ultimate test for an oxygen tolerant hydrogenase
    • Vincent KA, Cracknell JA, Clark JR, et al. Electricity from low-level H2 in still air-an ultimate test for an oxygen tolerant hydrogenase. Chem Commun (Camb) 2006:5033-5.
    • (2006) Chem Commun (Camb) , pp. 5033-5035
    • Vincent, K.A.1    Cracknell, J.A.2    Clark, J.R.3
  • 126
    • 84883038778 scopus 로고    scopus 로고
    • Optimizing the power of enzyme-based membrane-less hydrogen fuel cells for hydrogen-rich H2-air mixtures
    • Xu L, Armstrong FA. Optimizing the power of enzyme-based membrane-less hydrogen fuel cells for hydrogen-rich H2-air mixtures Energ Environ Sci 2013;6:2166-71.
    • (2013) Energ Environ Sci , vol.6 , pp. 2166-2171
    • Xu, L.1    Armstrong, F.A.2
  • 128
    • 84879248221 scopus 로고    scopus 로고
    • H2-driven cofactor regeneration with NAD(P)+-reducing hydrogenases
    • Lauterbach L, Lenz O, Vincent KA. H2-driven cofactor regeneration with NAD(P)+-reducing hydrogenases. FEBS J 2013;280:3058-68.
    • (2013) FEBS J , vol.280 , pp. 3058-3068
    • Lauterbach, L.1    Lenz, O.2    Vincent, K.A.3
  • 129
    • 82355169256 scopus 로고    scopus 로고
    • Systematic evaluation of the dihydrogen-oxidising and NAD+-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 as a cofactor regeneration catalyst
    • Ratzka J, Lauterbach L, Lenz O, Ansorge-Schumacher MB. Systematic evaluation of the dihydrogen-oxidising and NAD+-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 as a cofactor regeneration catalyst. Biocatal Biotransformation 2011;29:246-52.
    • (2011) Biocatal Biotransformation , vol.29 , pp. 246-252
    • Ratzka, J.1    Lauterbach, L.2    Lenz, O.3    Ansorge-Schumacher, M.B.4
  • 130
    • 84883621746 scopus 로고    scopus 로고
    • Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification
    • Herr N, Ratzka J, Lauterbach L, Lenz O, Ansorge-Schumacher MB. Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification. J Mol Catal B 2013;97 169-74.
    • (2013) J Mol Catal B , vol.97 , pp. 169-174
    • Herr, N.1    Ratzka, J.2    Lauterbach, L.3    Lenz, O.4    Ansorge-Schumacher, M.B.5
  • 131
    • 84855668583 scopus 로고    scopus 로고
    • A modular system for regeneration of NAD cofactors using graphite particles modified with hydrogenase and diaphorase moieties
    • Reeve HA, Lauterbach L, Ash PA, Lenz O, Vincent KA. A modular system for regeneration of NAD cofactors using graphite particles modified with hydrogenase and diaphorase moieties. Chem Commun (Camb) 2012;48:1589-91.
    • (2012) Chem Commun (Camb) , vol.48 , pp. 1589-1591
    • Reeve, H.A.1    Lauterbach, L.2    Ash, P.A.3    Lenz, O.4    Vincent, K.A.5
  • 132
    • 84855224161 scopus 로고    scopus 로고
    • Coupling of permeabilized cells of Gluconobacter oxydans and Ralstonia eutropha for asymmetric ketone reduction using H2 as reductant
    • Rundbäck F, Fidanoska M, Adlercreutz P. Coupling of permeabilized cells of Gluconobacter oxydans and Ralstonia eutropha for asymmetric ketone reduction using H2 as reductant. J Biotechnol 2012;157:154-8.
    • (2012) J Biotechnol , vol.157 , pp. 154-158
    • Rundbäck, F.1    Fidanoska, M.2    Adlercreutz, P.3
  • 133
    • 84872118145 scopus 로고    scopus 로고
    • Hydrogen-driven asymmetric reduction of hydroxyacetone to (R)-1,2-propanediol by Ralstonia eutropha transformant expressing alcohol dehydrogenase from Kluyveromyces lactis
    • Oda T, Oda K, Yamamoto H, et al. Hydrogen-driven asymmetric reduction of hydroxyacetone to (R)-1,2-propanediol by Ralstonia eutropha transformant expressing alcohol dehydrogenase from Kluyveromyces lactis. Microb Cell Fact 2013 12:2.
    • (2013) Microb Cell Fact , vol.12 , pp. 2
    • Oda, T.1    Oda, K.2    Yamamoto, H.3
  • 135
    • 33745844815 scopus 로고    scopus 로고
    • Light-driven hydrogen production by a hybrid complex of a [NiFe]-hydrogenase and the cyanobacterial photosystem I
    • Ihara M, Nishihara H, Yoon KS, et al. Light-driven hydrogen production by a hybrid complex of a [NiFe]-hydrogenase and the cyanobacterial photosystem I. Photochem Photobiol 2006;82:676-82.
    • (2006) Photochem Photobiol , vol.82 , pp. 676-682
    • Ihara, M.1    Nishihara, H.2    Yoon, K.S.3
  • 136
    • 73849083474 scopus 로고    scopus 로고
    • Photosynthetic hydrogen production by a hybrid complex of photosystem I and [NiFe]-hydrogenase
    • Krassen H, Schwarze A, Friedrich B, Ataka K, Lenz O, Heberle J. Photosynthetic hydrogen production by a hybrid complex of photosystem I and [NiFe]-hydrogenase. ACS Nano 2009;3:4055-61.
    • (2009) ACS Nano , vol.3 , pp. 4055-4061
    • Krassen, H.1    Schwarze, A.2    Friedrich, B.3    Ataka, K.4    Lenz, O.5    Heberle, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.