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Volumn 180, Issue 5, 1998, Pages 1023-1029

Subforms and in vitro reconstitution of the NAD-reducing hydrogenase of Alcaligenes eutrophus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ISOENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0031886480     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.5.1023-1029.1998     Document Type: Article
Times cited : (46)

References (50)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron hydrogenases
    • Adams, M. W. W. 1990. The structure and mechanism of iron hydrogenases. Biochim. Biophys. Acta 1020:115-145.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 2
    • 0016301935 scopus 로고
    • Studies on a gram-positive hydrogen bacterium, Nocardia opaca strain 1b. III. Purification, stability and some properties of the soluble hydrogen dehydrogenase
    • Aggag, M., and H. G. Schlegel. 1974. Studies on a gram-positive hydrogen bacterium, Nocardia opaca strain 1b. III. Purification, stability and some properties of the soluble hydrogen dehydrogenase. Arch. Mikrobiol. 100:25-39.
    • (1974) Arch. Mikrobiol. , vol.100 , pp. 25-39
    • Aggag, M.1    Schlegel, H.G.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
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht, S. P. J. 1994. Nickel hydrogenases: in search of the active site. Biochim. Biophys. Acta 1188:167-204.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.J.1
  • 5
    • 0030571582 scopus 로고    scopus 로고
    • Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC6803 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. PCC6803 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
  • 6
    • 0030795942 scopus 로고    scopus 로고
    • The membrane-bound hydrogenase (MBH) of Alcaligenes eutrophus H16: Functional and structural role of the cytochrome b subunit
    • Bernhard, M., B. Benelli, A. Hochkoeppler, D. Zanoni, and B. Friedrich. 1997. The membrane-bound hydrogenase (MBH) of Alcaligenes eutrophus H16: functional and structural role of the cytochrome b subunit. Eur. J. Biochem. 248:179-186.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 179-186
    • Bernhard, M.1    Benelli, B.2    Hochkoeppler, A.3    Zanoni, D.4    Friedrich, B.5
  • 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
    • 0030607245 scopus 로고    scopus 로고
    • Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans
    • Boison. G., O. Schmitz, L. Mikheeva, S. Shestakov, and H. Bothe. 1996. Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans. FEBS Lett. 394:153-158.
    • (1996) FEBS Lett. , vol.394 , pp. 153-158
    • Boison, G.1    Schmitz, O.2    Mikheeva, L.3    Shestakov, S.4    Bothe, H.5
  • 10
    • 0029671234 scopus 로고    scopus 로고
    • hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-maturation system
    • Dernedde, J., T. Eitinger, N. Patenge, and B. Friedrich. 1996. hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-maturation system. Eur. J. Biochem. 235:351-358.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 351-358
    • Dernedde, J.1    Eitinger, T.2    Patenge, N.3    Friedrich, B.4
  • 11
    • 0028785074 scopus 로고
    • Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm
    • Eismann, K., K. Mlejnek, D. Zipprich, M. Hoppert, H. Gerberding, and F. Mayer. 1995. Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm. J. Bacteriol. 177:6309-6312.
    • (1995) J. Bacteriol. , vol.177 , pp. 6309-6312
    • Eismann, K.1    Mlejnek, K.2    Zipprich, D.3    Hoppert, M.4    Gerberding, H.5    Mayer, F.6
  • 12
    • 0002151485 scopus 로고    scopus 로고
    • The NAD-linked soluble hydrogenase from Alcaligenes eutrophus H16: Detection and characterisation of EPR signals deriving from nickel and flavin
    • Erkens, A., K. Schneider, and A. Müller. 1996. The NAD-linked soluble hydrogenase from Alcaligenes eutrophus H16: detection and characterisation of EPR signals deriving 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
  • 13
  • 14
    • 0019419819 scopus 로고
    • Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus
    • Friedrich, B., E. Heine, A. Finck, and C. G. Friedrich. 1981. Nickel requirement for active hydrogenase formation in Alcaligenes eutrophus. J. Bacteriol. 145:1144-1149.
    • (1981) J. Bacteriol. , vol.145 , pp. 1144-1149
    • Friedrich, B.1    Heine, E.2    Finck, A.3    Friedrich, C.G.4
  • 15
    • 0027382485 scopus 로고
    • Molecular biology of hydrogen utilization in aerobic chemolithotrophs
    • Friedrich, B., and E. Schwartz. 1993. Molecular biology of hydrogen utilization in aerobic chemolithotrophs. Annu. Rev. Microbiol. 47:351-383.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 351-383
    • Friedrich, B.1    Schwartz, E.2
  • 16
    • 0020463996 scopus 로고
    • Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus
    • Friedrich, C. G., K. Schneider, and B. Friedrich. 1982. Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus. J. Bacteriol. 152:42-48.
    • (1982) J. Bacteriol. , vol.152 , pp. 42-48
    • Friedrich, C.G.1    Schneider, K.2    Friedrich, B.3
  • 17
    • 1842327489 scopus 로고    scopus 로고
    • Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11
    • Grzesnik, C., M. Lübbers, M. Reh, and H. G. Schlegel. 1997. Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11. Microbiology 24:1271-1286.
    • (1997) Microbiology , vol.24 , pp. 1271-1286
    • Grzesnik, C.1    Lübbers, M.2    Reh, M.3    Schlegel, H.G.4
  • 18
    • 0030899612 scopus 로고    scopus 로고
    • Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22
    • Grzesnik, C., K. Roß, K. Schneider, M. Reh, and H. G. Schlegel. 1997. Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22. Arch. Microbiol. 167:172-176.
    • (1997) Arch. Microbiol. , vol.167 , pp. 172-176
    • Grzesnik, C.1    Roß, K.2    Schneider, K.3    Reh, M.4    Schlegel, H.G.5
  • 20
    • 0022628358 scopus 로고
    • Characterisation of a native subunit of the NAD-linked hydrogenase isolated from a mutant of Alcaligenes eutrophus H16
    • Hornhardt, S., K. Schneider, and H. G. Schlegel. 1986. Characterisation of a native subunit of the NAD-linked hydrogenase isolated from a mutant of Alcaligenes eutrophus H16. Biochimie 68:15-24.
    • (1986) Biochimie , vol.68 , pp. 15-24
    • Hornhardt, S.1    Schneider, K.2    Schlegel, H.G.3
  • 21
    • 0026011904 scopus 로고
    • Structural aspects of the soluble NAD-dependent hydrogenase isolated from Alcaligenes eutrophus H16 and from Nocardia opaca 1b
    • Johannssen, W., H. Gerberding, M. Rohde, C. Zaborosch, and F. Mayer. 1991. Structural aspects of the soluble NAD-dependent hydrogenase isolated from Alcaligenes eutrophus H16 and from Nocardia opaca 1b. Arch. Microbiol. 155:303-308.
    • (1991) Arch. Microbiol. , vol.155 , pp. 303-308
    • Johannssen, W.1    Gerberding, H.2    Rohde, M.3    Zaborosch, C.4    Mayer, F.5
  • 22
    • 0019904249 scopus 로고
    • Wide host range cloning vectors: A cosmid clone bank of an Agrobacterium Ti plasmid
    • Knauf, V. C., and E. W. Nester. 1982. Wide host range cloning vectors: a cosmid clone bank of an Agrobacterium Ti plasmid. Plasmid 8:45-54.
    • (1982) Plasmid , vol.8 , pp. 45-54
    • Knauf, V.C.1    Nester, E.W.2
  • 23
    • 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
  • 24
    • 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
  • 26
    • 0001789455 scopus 로고    scopus 로고
    • Nickel incorporation into hydrogenases
    • R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli (ed.), VCH Publishers Inc., New York, N.Y.
    • Maier, T., and A. Böck. 1996. Nickel incorporation into hydrogenases, p. 173-192. In R. P. Hausinger, G. L. Eichhorn, and L. G. Marzilli (ed.), Advances in inorganic biochemistry, vol. 11. Mechanisms of metallocenter assembly. VCH Publishers Inc., New York, N.Y.
    • (1996) Advances in Inorganic Biochemistry, Vol. 11. Mechanisms of Metallocenter Assembly , vol.11 , pp. 173-192
    • Maier, T.1    Böck, A.2
  • 27
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki, S., I. Saimmaime, G. De Luca, M. Rousset, Z. Dermoun, and J.-P. Belaich. 1995. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 177:2628-2636.
    • (1995) J. Bacteriol. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.-P.6
  • 28
    • 0030968506 scopus 로고    scopus 로고
    • 2-activating subunit, HoxH, directs maturation of the NAD-reducing hydrogenase in Alcaligenes eutrophus
    • 2-activating subunit, HoxH, directs maturation of the NAD-reducing hydrogenase in Alcaligenes eutrophus. Eur. J. Biochem. 245:441-448.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 441-448
    • Massanz, C.1    Fernandez, V.M.2    Friedrich, B.3
  • 29
  • 30
    • 2642628958 scopus 로고    scopus 로고
    • Characterisation of the fds operon encoding the soluble formate dehydrogenase in Ralstonia eutropha
    • Oh, J.-I., and B. Bowien. 1997. Characterisation of the fds operon encoding the soluble formate dehydrogenase in Ralstonia eutropha. Biospectrum 1997: 127.
    • (1997) Biospectrum , vol.1997 , pp. 127
    • Oh, J.-I.1    Bowien, B.2
  • 32
    • 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
  • 33
    • 0026814596 scopus 로고
    • Structure/ function relationships among the nickel-containing hydrogenases
    • Przybyla, A. E., J. Robbins, N. Menon, and H. D. J. Peck, Jr. 1992. Structure/ function relationships among the nickel-containing hydrogenases. FEMS Microbiol. Rev. 88:109-136.
    • (1992) FEMS Microbiol. Rev. , vol.88 , pp. 109-136
    • Przybyla, A.E.1    Robbins, J.2    Menon, N.3    Peck Jr., H.D.J.4
  • 37
    • 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. Biochem. Biophys. Acta 567:315-324.
    • (1979) Biochem. Biophys. Acta , vol.567 , pp. 315-324
    • Schink, B.1    Schlegel, H.G.2
  • 38
    • 0020468613 scopus 로고
    • Effect of molecular hydrogen on histidine utilisation by Alcaligenes eutrophus
    • Schlesier, M., and B. Friedrich. 1982. Effect of molecular hydrogen on histidine utilisation by Alcaligenes eutrophus. Arch. Mikrobiol. 132:260-265.
    • (1982) Arch. Mikrobiol. , vol.132 , pp. 260-265
    • Schlesier, M.1    Friedrich, B.2
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0021381108 scopus 로고
    • Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1b
    • Schneider, K., H. G. Schlegel, and K. Jochim. 1984. Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1b. Eur. J. Biochem. 138:533-541.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 533-541
    • Schneider, K.1    Schlegel, H.G.2    Jochim, K.3
  • 43
    • 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 1:717-743.
    • (1983) Bio/Technology , vol.1 , pp. 717-743
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 44
    • 0030012735 scopus 로고    scopus 로고
    • Carboxyl-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. Carboxyl-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
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehlin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4357.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4357
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 46
    • 0025291627 scopus 로고
    • Cloning and nucleotide sequence 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 sequence 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
  • 49
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli
    • Weidner, U., S. Geier, A. Ptock, T. Friedrich, H. Leif, and H. Weiss. 1993. The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. J. Mol. Biol. 233:109-122.
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 50
    • 0028951871 scopus 로고
    • EPR and Mössbauer spectroscopic studies on the tetrameric, NAD-linked hydrogenase of Nocardia opaca 1b and its two dimers. 1. The βδ dimer - A prototype of a simple hydrogenase
    • Zaborosch, C., M. Köster, E. Bill, K. Schneider, H. G. Schlegel, and A. X. Trautwein. 1995. EPR and Mössbauer spectroscopic studies on the tetrameric, NAD-linked hydrogenase of Nocardia opaca 1b and its two dimers. 1. The βδ dimer - a prototype of a simple hydrogenase. BioMetals 8:149-162.
    • (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


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