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Volumn 187, Issue 9, 2005, Pages 3122-3132

The soluble NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH

Author keywords

[No Author keywords available]

Indexed keywords

HOX 1 PROTEIN; HOX PROTEIN; HYDROGENASE; IRON COMPLEX; NICKEL COMPLEX; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 20244376022     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.9.3122-3132.2005     Document Type: Article
Times cited : (95)

References (82)
  • 1
    • 0037422404 scopus 로고    scopus 로고
    • Quantitative amino-acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups
    • Albracht, S. P. J., E. van der Linden, and B. W. Faber. 2003. Quantitative amino-acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups. Biochim. Biophys. Acta 1557:41-49.
    • (2003) Biochim. Biophys. Acta , vol.1557 , pp. 41-49
    • Albracht, S.P.J.1    Van Der Linden, E.2    Faber, B.W.3
  • 2
    • 0034680865 scopus 로고    scopus 로고
    • Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I)
    • Albracht, S. P. J., and R. Hedderich. 2000. Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I). FEBS Lett. 485:1-6.
    • (2000) FEBS Lett. , vol.485 , pp. 1-6
    • Albracht, S.P.J.1    Hedderich, R.2
  • 3
    • 0027328631 scopus 로고
    • Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: Ubiquinone oxidoreductase
    • Albracht, S. P. J. 1993. Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: ubiquinone oxidoreductase. Biochim. Biophys. Acta 1144:221-224.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 221-224
    • Albracht, S.P.J.1
  • 4
    • 0030571582 scopus 로고    scopus 로고
    • Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I)
    • Appel, J., and R. Schulz. 1996. Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I). Biochim. Biophys. Acta 1298:141-147.
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 141-147
    • Appel, J.1    Schulz, R.2
  • 5
    • 0029066353 scopus 로고
    • Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum
    • Bagley, K. A., E. C. Duin, W. Roseboom, S. P. J. Albracht, and W. H. Woodruff. 1995. Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry 34:5527-5535.
    • (1995) Biochemistry , vol.34 , pp. 5527-5535
    • Bagley, K.A.1    Duin, E.C.2    Roseboom, W.3    Albracht, S.P.J.4    Woodruff, W.H.5
  • 6
    • 0028048410 scopus 로고
    • Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum
    • Bagley, K. A., C. J. Van Garderen, M. Chen, E. C. Duin, S. P. J. Albracht, and W. H. Woodruff. 1994. Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry 33:9229-9236.
    • (1994) Biochemistry , vol.33 , pp. 9229-9236
    • Bagley, K.A.1    Van Garderen, C.J.2    Chen, M.3    Duin, E.C.4    Albracht, S.P.J.5    Woodruff, W.H.6
  • 7
    • 0029764690 scopus 로고    scopus 로고
    • The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling
    • Bernhard, M., E. Schwartz, J. Rietdorf, and B. Friedrich. 1996. The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling. J. Bacteriol. 178:4522-4529.
    • (1996) J. Bacteriol. , vol.178 , pp. 4522-4529
    • Bernhard, M.1    Schwartz, E.2    Rietdorf, J.3    Friedrich, B.4
  • 8
    • 0036707995 scopus 로고    scopus 로고
    • A structurally conserved water molecule in Rossmann dinucleotide-binding domains
    • Bottoms, C. A., P. E. Smith, and J. J. Tanner. 2002. A structurally conserved water molecule in Rossmann dinucleotide-binding domains. Protein Sci. 11:2125-2137.
    • (2002) Protein Sci. , vol.11 , pp. 2125-2137
    • Bottoms, C.A.1    Smith, P.E.2    Tanner, J.J.3
  • 9
    • 0036318686 scopus 로고    scopus 로고
    • 2 assimilation in the chemoautotroph Ralstonia eutropha
    • 2 assimilation in the chemoautotroph Ralstonia eutropha. Arch. Microbiol. 178:85-93.
    • (2002) Arch. Microbiol. , vol.178 , pp. 85-93
    • Bowien, B.1    Kusian, B.2
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0142211218 scopus 로고    scopus 로고
    • Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: Changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III)
    • Brumaghim, J. L., Y. Li, E. Henle, and S. Linn. 2003. Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III). J. Biol. Chem. 278:42495-42504.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42495-42504
    • Brumaghim, J.L.1    Li, Y.2    Henle, E.3    Linn, S.4
  • 14
    • 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., S. Löscher, P. Liebisch, E. Van der Linden, M. Galander, F. Lendzian, W. Meyer-Klaucke, S. P. J. Albracht, B. Friedrich, H. Dau, and M. Haumann. 2005. 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. 127:576-592.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 576-592
    • Burgdorf, T.1    Löscher, S.2    Liebisch, P.3    Van Der Linden, E.4    Galander, M.5    Lendzian, F.6    Meyer-Klaucke, W.7    Albracht, S.P.J.8    Friedrich, B.9    Dau, H.10    Haumann, M.11
  • 17
    • 0000965857 scopus 로고
    • Redox behavior of nickel in hydrogenase from Methanobacterium thermoautotrophicum (strain Marburg) - Correlation between the nickel valence state and enzyme activity
    • Coremans, J. M. C. C., J. W. van der Zwaan, and S. P. J. Albracht. 1989. Redox behavior of nickel in hydrogenase from Methanobacterium thermoautotrophicum (strain Marburg) - correlation between the nickel valence state and enzyme activity. Biochim. Biophys. Acta 997:256-267.
    • (1989) Biochim. Biophys. Acta , vol.997 , pp. 256-267
    • Coremans, J.M.C.C.1    Van Der Zwaan, J.W.2    Albracht, S.P.J.3
  • 19
    • 0023036934 scopus 로고
    • Molecular cloning of structural and regulatory hydrogenase (hox) genes of Alcaligenes eutrophus H16
    • Eberz, G., C. Hogrefe, C. Kortlüke, A. Kamienski, and B. Friedrich. 1986. Molecular cloning of structural and regulatory hydrogenase (hox) genes of Alcaligenes eutrophus H16. J. Bacteriol. 168:636-641.
    • (1986) J. Bacteriol. , vol.168 , pp. 636-641
    • Eberz, G.1    Hogrefe, C.2    Kortlüke, C.3    Kamienski, A.4    Friedrich, B.5
  • 20
    • 0002151485 scopus 로고    scopus 로고
    • The NAD-linked soluble hydrogenase from Alcaligenes eutrophus H16: Detection and characterization of EPR signals derived from nickel and flavin
    • Erkens, A., K. Schneider, and A. Müller. 1996. The NAD-linked soluble hydrogenase from Alcaligenes eutrophus H16: detection and characterization of EPR signals derived from nickel and flavin. J. Biol. Inorg. Chem. 1:99-110.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 99-110
    • Erkens, A.1    Schneider, K.2    Müller, A.3
  • 22
    • 0037425515 scopus 로고    scopus 로고
    • Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F
    • Foerster, S., M. Stein, M. Brecht, H. Ogata, Y. Higuchi, and W. Lubitz. 2003. Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Am. Chem. Soc. 125:83-93.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 83-93
    • Foerster, S.1    Stein, M.2    Brecht, M.3    Ogata, H.4    Higuchi, Y.5    Lubitz, W.6
  • 23
    • 0033135158 scopus 로고    scopus 로고
    • The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
    • Garcin, E., X. Vernede, E. C. Hatchikian, A. Volbeda, M. Frey, and J. C. Fontecilla-Camps. 1999. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Struct. Fold. Des. 7:557-566.
    • (1999) Struct. Fold. Des. , 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
  • 24
    • 1842327489 scopus 로고    scopus 로고
    • Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11
    • Grzeszik, C., M. Lübbers, M. Reh, and H. G. Schlegel. 1997. Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11. Microbiology 143:1271-1286.
    • (1997) Microbiology , vol.143 , pp. 1271-1286
    • Grzeszik, C.1    Lübbers, M.2    Reh, M.3    Schlegel, H.G.4
  • 27
    • 0035810698 scopus 로고    scopus 로고
    • Allosteric regulation of the cAMP receptor protein
    • Harman, J. G. 2001. Allosteric regulation of the cAMP receptor protein. Biochim. Biophys. Acta 1547:1-17.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 1-17
    • Harman, J.G.1
  • 28
    • 0015864046 scopus 로고
    • Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondria
    • Hatefi, Y., and W. G. Hanstein. 1973. Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondria. Biochemistry 12:3515-3522.
    • (1973) Biochemistry , vol.12 , pp. 3515-3522
    • Hatefi, Y.1    Hanstein, W.G.2
  • 29
    • 0035980822 scopus 로고    scopus 로고
    • Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Kaneko, T., Y. Nakamura, C. P. Wolk, et al. 2001. Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res. 8:205-213, 227-253.
    • (2001) DNA Res. , vol.8 , pp. 205-213
    • Kaneko, T.1    Nakamura, Y.2    Wolk, C.P.3
  • 30
    • 0023216980 scopus 로고
    • Purification and properties of a protein linked to the soluble hydrogenase of hydrogen-oxidizing bacteria
    • Karst, U., S. Suetin, and C. G. Friedrich. 1987. Purification and properties of a protein linked to the soluble hydrogenase of hydrogen-oxidizing bacteria. J. Bacteriol. 169:2079-2085.
    • (1987) J. Bacteriol. , vol.169 , pp. 2079-2085
    • Karst, U.1    Suetin, S.2    Friedrich, C.G.3
  • 32
    • 0017843653 scopus 로고
    • Metabolic regulation in Pseudomonas oxalaticus OX1. Enzyme and coenzyme concentration changes during substrate transition experiments
    • Knight, M., L. Dijkhuizen, and W. Harder. 1978. Metabolic regulation in Pseudomonas oxalaticus OX1. Enzyme and coenzyme concentration changes during substrate transition experiments. Arch. Microbiol. 116:85-90.
    • (1978) Arch. Microbiol. , vol.116 , pp. 85-90
    • Knight, M.1    Dijkhuizen, L.2    Harder, W.3
  • 33
    • 0036129945 scopus 로고    scopus 로고
    • Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site
    • Korndörfer, I. P., and A. Skerra. 2002. Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site. Protein Sci. 11:883-893.
    • (2002) Protein Sci. , vol.11 , pp. 883-893
    • Korndörfer, I.P.1    Skerra, A.2
  • 34
    • 0026700702 scopus 로고
    • A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16
    • Kortlüke, C., K. Horstmann, E. Schwartz, M. Rohde, R. Binsack, and B. Friedrich. 1992. A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 174:6277-6289.
    • (1992) J. Bacteriol. , vol.174 , pp. 6277-6289
    • Kortlüke, C.1    Horstmann, K.2    Schwartz, E.3    Rohde, M.4    Binsack, R.5    Friedrich, B.6
  • 35
    • 0006392352 scopus 로고
    • Genes of lithoautotrophic metabolism are clustered on the megaplasmid pHG1 in Alcaligenes eutrophus
    • Kortlüke, C., C. Hogrefe, G. Eberz, A. Pühler, and B. Friedrich. 1987. Genes of lithoautotrophic metabolism are clustered on the megaplasmid pHG1 in Alcaligenes eutrophus. Mol. Gen. Genet. 210:122-128.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 122-128
    • Kortlüke, C.1    Hogrefe, C.2    Eberz, G.3    Pühler, A.4    Friedrich, B.5
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the asssembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the asssembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0028228427 scopus 로고
    • The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation
    • Lenz, O., E. Schwartz, J. Dernedde, M. Eitinger, and B. Friedrich. 1994. The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation. J. Bacteriol. 176:4385-4393.
    • (1994) J. Bacteriol. , vol.176 , pp. 4385-4393
    • Lenz, O.1    Schwartz, E.2    Dernedde, J.3    Eitinger, M.4    Friedrich, B.5
  • 40
    • 0033607244 scopus 로고    scopus 로고
    • 2-activating site of the NAD-reducing hydrogenase from Alcaligenes eutrophus
    • 2-activating site of the NAD-reducing hydrogenase from Alcaligenes eutrophus. Biochemistry 38:14330-14337.
    • (1999) Biochemistry , vol.38 , pp. 14330-14337
    • Massanz, C.1    Friedrich, B.2
  • 41
    • 0031886480 scopus 로고    scopus 로고
    • Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Massanz, C., S. Schmidt, and B. Friedrich. 1998. Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus. J. Bacteriol. 180:1023-1029.
    • (1998) J. Bacteriol. , vol.180 , pp. 1023-1029
    • Massanz, C.1    Schmidt, S.2    Friedrich, B.3
  • 43
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 44
    • 4243810906 scopus 로고    scopus 로고
    • NADH-induzierte Einflüsse auf die Koordination des Nickels im aktiven Zentrum der löslichen Hydrogenase aus Alcaligenes eutrophus: XAFS-Untersuchungen an drei ESR-spektroskopisch unterscheidbaren Zuständen
    • Müller, A., A. Erkens, K. Schneider, H.-F. Nolting, V. A. Solé, and G. Henkel. 1997. NADH-induzierte Einflüsse auf die Koordination des Nickels im aktiven Zentrum der löslichen Hydrogenase aus Alcaligenes eutrophus: XAFS-Untersuchungen an drei ESR-spektroskopisch unterscheidbaren Zuständen. Angew. Chem. 109:1812-1815.
    • (1997) Angew. Chem. , vol.109 , pp. 1812-1815
    • Müller, A.1    Erkens, A.2    Schneider, K.3    Nolting, H.-F.4    Solé, V.A.5    Henkel, G.6
  • 45
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Nicolet, Y., A. L. de Lacey, X. Vernede, V. M. Fernandez, E. C. Hatchikian, and J. C. Fontecilla-Camps. 2001. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem. Soc. 123:1596-1601.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2    Vernede, X.3    Fernandez, V.M.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 46
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet, Y., C. Piras, P. Legrand, C. E. Hatchikian, and J. C. Fontecilla-Camps. 1999. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Struct. Fold. Des. 7:13-23.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 47
    • 0025689089 scopus 로고
    • Differential stability of mRNA species of Alcaligenes eutrophus soluble and particulate hydrogenases
    • Oelmüller, U., H. G. Schlegel, and C. G. Friedrich. 1990. Differential stability of mRNA species of Alcaligenes eutrophus soluble and particulate hydrogenases. J. Bacteriol. 172:7057-7064.
    • (1990) J. Bacteriol. , vol.172 , pp. 7057-7064
    • Oelmüller, U.1    Schlegel, H.G.2    Friedrich, C.G.3
  • 48
    • 0037056042 scopus 로고    scopus 로고
    • The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade
    • Papa, S. 2002. The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade. Biochim. Biophys. Acta 1555:147-153.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 147-153
    • Papa, S.1
  • 49
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters, J. W., W. N. Lanzilotta, B. J. Lemon, and L. C. Seefeldt. 1998. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282:1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 51
    • 0032403791 scopus 로고    scopus 로고
    • A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases
    • Pierik, A. J., M. Hulstein, W. R. Hagen, and S. P. J. Albracht. 1998. A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. Eur. J. Biochem. 258:572-578.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 572-578
    • Pierik, A.J.1    Hulstein, M.2    Hagen, W.R.3    Albracht, S.P.J.4
  • 52
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington, S. J., J. M. Skehel, R. B. Gennis, and J. E. Walker. 1991. Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 30:2166-2175.
    • (1991) Biochemistry , vol.30 , pp. 2166-2175
    • Pilkington, S.J.1    Skehel, J.M.2    Gennis, R.B.3    Walker, J.E.4
  • 54
    • 0018788563 scopus 로고
    • The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties
    • Schink, B., and H. G. Schlegel. 1979. The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties. Biochim. Biophys. Acta 567:315-324.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 315-324
    • Schink, B.1    Schlegel, H.G.2
  • 55
    • 0037156874 scopus 로고    scopus 로고
    • HoxE - A subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
    • Schmitz, O., G. Boison, H. Salzmann, H. Bothe, K. Schutz, S. H. Wang, and T. Happe. 2002. HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria. Biochim. Biophys. Acta 1554:66-74.
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 66-74
    • Schmitz, O.1    Boison, G.2    Salzmann, H.3    Bothe, H.4    Schutz, K.5    Wang, S.H.6    Happe, T.7
  • 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., R. Cammack, and H. G. Schlegel. 1984. Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b. Eur. J. Biochem. 142:75-84.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 75-84
    • Schneider, K.1    Cammack, R.2    Schlegel, H.G.3
  • 57
    • 0020807235 scopus 로고
    • Purification of hydrogenases by affinity chromatography on Procion Red-agarose
    • Schneider, K., M. Pinkwart, and K. Jochim. 1983. Purification of hydrogenases by affinity chromatography on Procion Red-agarose. Biochem. J. 213:391-398.
    • (1983) Biochem. J. , vol.213 , pp. 391-398
    • Schneider, K.1    Pinkwart, M.2    Jochim, K.3
  • 58
    • 0017110320 scopus 로고
    • Purification and properties of the soluble hydrogenase from Alcaligenes eutrophus H16
    • Schneider, K., and H. G. Schlegel. 1976. Purification and properties of the soluble hydrogenase from Alcaligenes eutrophus H16. Biochim. Biophys. Acta 452:66-80.
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 66-80
    • Schneider, K.1    Schlegel, H.G.2
  • 59
    • 0033600871 scopus 로고    scopus 로고
    • A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex
    • Schulte, U., V. Haupt, A. Abelmann, W. Fecke, B. Brors, T. Rasmussen, T. Friedrich, and H. Weiss. 1999. A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex. J. Mol. Biol. 292:569-580.
    • (1999) J. Mol. Biol. , vol.292 , pp. 569-580
    • Schulte, U.1    Haupt, V.2    Abelmann, A.3    Fecke, W.4    Brors, B.5    Rasmussen, T.6    Friedrich, T.7    Weiss, H.8
  • 60
    • 0031747821 scopus 로고    scopus 로고
    • Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes
    • Schwartz, E., U. Gerischer, and B. Friedrich. 1998. Transcriptional regulation of Alcaligenes eutrophus hydrogenase genes. J. Bacteriol. 180:3197-3204.
    • (1998) J. Bacteriol. , vol.180 , pp. 3197-3204
    • Schwartz, E.1    Gerischer, U.2    Friedrich, B.3
  • 61
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 63
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 64
    • 2342552466 scopus 로고    scopus 로고
    • Relativistic DFT calculation of the reaction cycle intermediates of [NiFe] hydrogenase: A contribution to understanding the enzymatic mechanism
    • Stein, M., and W. Lubitz. 2004. Relativistic DFT calculation of the reaction cycle intermediates of [NiFe] hydrogenase: a contribution to understanding the enzymatic mechanism. J. Inorg. Biochem. 98:862-877.
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 862-877
    • Stein, M.1    Lubitz, W.2
  • 66
    • 0025330489 scopus 로고
    • cAMP-dependent protein kinase: Framework for a diverse family of regulatory enzymes
    • Taylor, S. S., J. A. Buechler, and W. Yonemoto. 1990. cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59:971-1005.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 971-1005
    • Taylor, S.S.1    Buechler, J.A.2    Yonemoto, W.3
  • 67
    • 0030012735 scopus 로고    scopus 로고
    • Carboxy-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product
    • Thiemermann, S., J. Dernedde, M. Bernhard, W. Schroeder, C. Massanz, and B. Friedrich. 1996. Carboxy-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product. J. Bacteriol. 178:2368-2374.
    • (1996) J. Bacteriol. , vol.178 , pp. 2368-2374
    • Thiemermann, S.1    Dernedde, J.2    Bernhard, M.3    Schroeder, W.4    Massanz, C.5    Friedrich, B.6
  • 68
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 69
    • 0025291627 scopus 로고
    • Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
    • Tran-Betcke, A., U. Warnecke, C. Böcker, C. Zaborosch, and B. Friedrich. 1990. Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 172:2920-2929.
    • (1990) J. Bacteriol. , vol.172 , pp. 2920-2929
    • Tran-Betcke, A.1    Warnecke, U.2    Böcker, C.3    Zaborosch, C.4    Friedrich, B.5
  • 70
    • 0025311855 scopus 로고
    • New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles
    • van Belzen, R., M. C. van Gaalen, P. A. Cuypers, and S. P. J. Albracht. 1990. New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles. Biochim. Biophys. Acta 101:152-159.
    • (1990) Biochim. Biophys. Acta , vol.101 , pp. 152-159
    • Van Belzen, R.1    Van Gaalen, M.C.2    Cuypers, P.A.3    Albracht, S.P.J.4
  • 71
    • 0024981157 scopus 로고
    • The pathway of electron transfer in NADH:Q oxidoreductase
    • van Belzen, R., and S. P. J. Albracht. 1989. The pathway of electron transfer in NADH:Q oxidoreductase. Biochim. Biophys. Acta 974:311-320.
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 311-320
    • Van Belzen, R.1    Albracht, S.P.J.2
  • 73
    • 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., T. Burgdorf, M. Bernhard, B. Bleijlevens, B. Friedrich, and S. P. J. Albracht. 2004. 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. 9:616-626.
    • (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.J.6
  • 74
    • 0029891513 scopus 로고    scopus 로고
    • Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy
    • van der Spek, T. M., A. F. Arendsen, R. P. Happe, S. Yun, K. A. Bagley, D. J. Stufkens, W. R. Hagen, and S. P. J. Albracht. 1996. Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy. Eur. J. Biochem. 237:629-634.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 629-634
    • Van Der Spek, T.M.1    Arendsen, A.F.2    Happe, R.P.3    Yun, S.4    Bagley, K.A.5    Stufkens, D.J.6    Hagen, W.R.7    Albracht, S.P.J.8
  • 75
    • 0033902955 scopus 로고    scopus 로고
    • Effects of the Calvin cycle on nicotinamide adenine dinucleotide concentrations and redox balances of Xanthobacter flavus
    • van Keulen, G., L. Dijkhuizen, and W. G. Meijer. 2000. Effects of the Calvin cycle on nicotinamide adenine dinucleotide concentrations and redox balances of Xanthobacter flavus. J. Bacteriol. 182:4637-4639.
    • (2000) J. Bacteriol. , vol.182 , pp. 4637-4639
    • Van Keulen, G.1    Dijkhuizen, L.2    Meijer, W.G.3
  • 76
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais, P. M., and A. Colbeau. 2004. Molecular biology of microbial hydrogenases. Curr. Issues Mol. Biol. 6:159-188.
    • (2004) Curr. Issues Mol. Biol. , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 77
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25:455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 80
    • 0033979304 scopus 로고    scopus 로고
    • The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Yamaguchi, M., G. I. Belogrudov, A. Matsuno-Yagi, and Y. Hatefi. 2000. The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 267:329-336.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 329-336
    • Yamaguchi, M.1    Belogrudov, G.I.2    Matsuno-Yagi, A.3    Hatefi, Y.4
  • 81
    • 0032478597 scopus 로고    scopus 로고
    • Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin
    • Yamaguchi, M., G. I. Belogrudov, and J. Hatefi. 1998. Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin. J. Biol. Chem. 273:8094-8098.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8094-8098
    • Yamaguchi, M.1    Belogrudov, G.I.2    Hatefi, J.3
  • 82
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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