메뉴 건너뛰기




Volumn 10, Issue 2-4, 2006, Pages 181-196

[NiFe]-hydrogenases of Ralstonia eutropha H16: Modular enzymes for oxygen-tolerant biological hydrogen oxidation

Author keywords

NiFe hydrogenases; H2 sensing; Hydrogenase maturation; Metal center assembly; NADH dehydrogenase; Ni Fe active site; Protein complexes; Two component system

Indexed keywords

BACTERIAL ENZYME; CYTOPLASM PROTEIN; HYDROGEN; HYDROGENASE; IRON; MEMBRANE ENZYME; NICKEL; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXYGEN; REGULATOR PROTEIN;

EID: 33744503148     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000091564     Document Type: Short Survey
Times cited : (191)

References (100)
  • 1
    • 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 SP, Hedderich R: Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I). FEBS Lett 2000;485:1-6.
    • (2000) FEBS Lett , vol.485 , pp. 1-6
    • Albracht, S.P.1    Hedderich, R.2
  • 2
    • 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;173:333-338.
    • (2000) Arch Microbiol , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 3
    • 1842583991 scopus 로고    scopus 로고
    • Hydrogenases: Active site puzzles and progress
    • Armstrong FA: Hydrogenases: active site puzzles and progress. Curr Opin Chem Biol 2004;8:133-140.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 133-140
    • Armstrong, F.A.1
  • 4
    • 20744457727 scopus 로고    scopus 로고
    • [NiFe]-hydrogenases: Spectroscopic and electrochemical definition of reactions and intermediates
    • Armstrong FA, Albracht SP: [NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates. Philos Transact A Math Phys Eng Sci 2005;363:937-954.
    • (2005) Philos Transact A Math Phys Eng Sci , vol.363 , pp. 937-954
    • Armstrong, F.A.1    Albracht, S.P.2
  • 5
    • 0028048410 scopus 로고
    • Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum
    • Bagley KA, Van Garderen CJ, Chen M, Duin EC, Albracht SPJ, Woodruff WH: Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry 1994;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
  • 6
    • 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;248:179-186.
    • (1997) Eur J Biochem , vol.248 , pp. 179-186
    • Bernhard, M.1    Benelli, B.2    Hochkoeppler, A.3    Zannoni, D.4    Friedrich, B.5
  • 8
    • 0033971919 scopus 로고    scopus 로고
    • Ralstonia eutropha TF93 is blocked in tat-mediated protein export
    • Bernhard M, Friedrich B, Siddiqui RA: Ralstonia eutropha TF93 is blocked in tat-mediated protein export. J Bacteriol 2000;182:581-588.
    • (2000) J Bacteriol , vol.182 , pp. 581-588
    • Bernhard, M.1    Friedrich, B.2    Siddiqui, R.A.3
  • 9
    • 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;178:4522-4529.
    • (1996) J Bacteriol , vol.178 , pp. 4522-4529
    • Bernhard, M.1    Schwartz, E.2    Rietdorf, J.3    Friedrich, B.4
  • 10
    • 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;176:7102-7106.
    • (1994) J Bacteriol , vol.176 , pp. 7102-7106
    • Black, L.K.1    Fu, C.2    Maier, R.J.3
  • 11
    • 8744311816 scopus 로고    scopus 로고
    • The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel
    • Bleijlevens B, Buhrke T, van der Linden E, Friedrich B, Albracht SP: The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel. J Biol Chem 2004;279:46686-46691.
    • (2004) J Biol Chem , vol.279 , pp. 46686-46691
    • Bleijlevens, B.1    Buhrke, T.2    Van Der Linden, E.3    Friedrich, B.4    Albracht, S.P.5
  • 12
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases
    • Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Böck A: The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J Mol Biol 2004a;344:155-167.
    • (2004) J Mol Biol , vol.344 , pp. 155-167
    • Blokesch, M.1    Albracht, S.P.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Böck, A.6
  • 13
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli: The HypC cycle
    • Blokesch M, Böck A: Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle. J Mol Biol 2002;324:287-296.
    • (2002) J Mol Biol , vol.324 , pp. 287-296
    • Blokesch, M.1    Böck, A.2
  • 14
    • 4344582395 scopus 로고    scopus 로고
    • Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE
    • Blokesch M, Paschos A, Bauer A, Reissmann S, Drapal N, Böck A: Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur J Biochem 2004b;271:3428-3436.
    • (2004) Eur J Biochem , vol.271 , pp. 3428-3436
    • Blokesch, M.1    Paschos, A.2    Bauer, A.3    Reissmann, S.4    Drapal, N.5    Böck, A.6
  • 17
    • 21244441201 scopus 로고    scopus 로고
    • 2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site
    • 2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site. J Biol Chem 2005a;280:23791-23796.
    • (2005) J Biol Chem , vol.280 , pp. 23791-23796
    • Buhrke, T.1    Lenz, O.2    Krauss, N.3    Friedrich, B.4
  • 18
    • 1642442726 scopus 로고    scopus 로고
    • 2-sensing complex of Ralstonia eutropha: Interaction between a regulatory [NiFe] hydrogenase and a histidine protein kinase
    • 2-sensing complex of Ralstonia eutropha: interaction between a regulatory [NiFe] hydrogenase and a histidine protein kinase. Mol Microbiol 2004;51:1677-1689.
    • (2004) Mol Microbiol , vol.51 , pp. 1677-1689
    • Buhrke, T.1    Lenz, O.2    Porthun, A.3    Friedrich, B.4
  • 21
    • 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, Van der Linden E, Galander M, Lendzian F, Meyer-Klaucke W, Albracht SP, Friedrich B, Dau H, Haumann M: 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 2005a;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.8    Friedrich, B.9    Dau, H.10    Haumann, M.11
  • 25
    • 0029845048 scopus 로고    scopus 로고
    • 2O, and NO)
    • 2O, and NO). Microbiol Rev 1996;60:609-640.
    • (1996) Microbiol Rev , vol.60 , pp. 609-640
    • Conrad, R.1
  • 26
    • 17644385506 scopus 로고    scopus 로고
    • The hydrogenases of Geobacter sulfurreducens: A comparative genomic perspective
    • Coppi M: The hydrogenases of Geobacter sulfurreducens: a comparative genomic perspective. Microbiology 2005;151:1239-1254.
    • (2005) Microbiology , vol.151 , pp. 1239-1254
    • Coppi, M.1
  • 28
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • Dubini A, Pye RL, Jack RL, Palmer T, Sargent F: How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. Int J Hydrogen Energy 2002;27:1413-1420.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1413-1420
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 29
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: Identification of precursor-binding accessory proteins
    • Dubini A, Sargent F: Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett 2003;549:141-146.
    • (2003) FEBS Lett , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 30
    • 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;178:5174-5181.
    • (1996) J Bacteriol , vol.178 , pp. 5174-5181
    • Elsen, S.1    Colbeau, A.2    Chabert, J.3    Vignais, P.M.4
  • 31
    • 0344666703 scopus 로고    scopus 로고
    • 2 sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus
    • 2 sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus. J Bacteriol 2003;185:7111-7119.
    • (2003) J Bacteriol , vol.185 , pp. 7111-7119
    • Elsen, S.1    Duche, O.2    Colbeau, A.3
  • 32
    • 0032885925 scopus 로고    scopus 로고
    • The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from Wolinella succinogenes
    • Gross R, Simon J, Kröger A: The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from Wolinella succinogenes. Arch Microbiol 1999;172:227-232.
    • (1999) Arch Microbiol , vol.172 , pp. 227-232
    • Gross, R.1    Simon, J.2    Kröger, A.3
  • 33
    • 1842327489 scopus 로고    scopus 로고
    • Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11
    • Grzeszik C, Lübbers M, Reh M, Schlegel HG: Genes encoding the NAD-reducing hydrogenase of Rhodococcus opacus MR11. Microbiology 1997;143:1271-1286.
    • (1997) Microbiology , vol.143 , pp. 1271-1286
    • Grzeszik, C.1    Lübbers, M.2    Reh, M.3    Schlegel, H.G.4
  • 34
    • 0036166885 scopus 로고    scopus 로고
    • Detection and localization of two hydrogenases in Methylococcus capsulatus (Bath) and their potential role in methane metabolism
    • Hanczar T, Csaki R, Bodrossy L, Murrell JC, Kovacs KL: Detection and localization of two hydrogenases in Methylococcus capsulatus (Bath) and their potential role in methane metabolism. Arch Microbiol 2002;177:167-172.
    • (2002) Arch Microbiol , vol.177 , pp. 167-172
    • Hanczar, T.1    Csaki, R.2    Bodrossy, L.3    Murrell, J.C.4    Kovacs, K.L.5
  • 38
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
    • Higuchi Y, Yagi T, Yasuoka N: Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure 1997;5:1671-1680.
    • (1997) Structure , vol.5 , pp. 1671-1680
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 39
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli: Role of accessory proteins HypA and HybF
    • Hube M, Blokesch M, Böck A: Network of hydrogenase maturation in Escherichia coli: role of accessory proteins HypA and HybF. J Bacteriol 2002;184:3879-3885.
    • (2002) J Bacteriol , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Böck, A.3
  • 40
    • 6344223356 scopus 로고    scopus 로고
    • NiFe hydrogenase-active site biosynthesis: Identification of Hyp protein complexes in Ralstonia eutropha
    • Jones AK, Lenz O, Strack A, Buhrke T, Friedrich B: NiFe hydrogenase-active site biosynthesis: identification of Hyp protein complexes in Ralstonia eutropha. Biochemistry 2004;43:13467-13477.
    • (2004) Biochemistry , vol.43 , pp. 13467-13477
    • Jones, A.K.1    Lenz, O.2    Strack, A.3    Buhrke, T.4    Friedrich, B.5
  • 41
    • 0023216980 scopus 로고
    • Purification and properties of a protein linked to the soluble hydrogenase of hydrogen-oxidizing bacteria
    • Kärst U, Suetin S, Friedrich CG: Purification and properties of a protein linked to the soluble hydrogenase of hydrogen-oxidizing bacteria. J Bacteriol 1987;169:2079-2085.
    • (1987) J Bacteriol , vol.169 , pp. 2079-2085
    • Kärst, U.1    Suetin, S.2    Friedrich, C.G.3
  • 42
    • 0037369931 scopus 로고    scopus 로고
    • Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Kanai T, Ito S, Imanaka T: Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Bacteriol 2003;185:1705-1711.
    • (2003) J Bacteriol , vol.185 , pp. 1705-1711
    • Kanai, T.1    Ito, S.2    Imanaka, T.3
  • 43
    • 0034056389 scopus 로고    scopus 로고
    • 2 sensor of Ralstonia eutropha is a member of the subclass of regulatory [NiFe] hydrogenases
    • 2 sensor of Ralstonia eutropha is a member of the subclass of regulatory [NiFe] hydrogenases. J Bacteriol 2000;182:2716-2724.
    • (2000) J Bacteriol , vol.182 , pp. 2716-2724
    • Kleihues, L.1    Lenz, O.2    Bernhard, M.3    Buhrke, T.4    Friedrich, B.5
  • 47
    • 0032514688 scopus 로고    scopus 로고
    • 2 sensing in Alcaligenes eutrophus
    • USA
    • 2 sensing in Alcaligenes eutrophus. Proc Natl Acad Sci USA 1998;95:12474-12479.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 12474-12479
    • Lenz, O.1    Friedrich, B.2
  • 48
    • 24944510413 scopus 로고    scopus 로고
    • Requirements for heterologous production of a complex metalloenzyme: The membrane-bound [NiFe] hydrogenase
    • Lenz O, Gleiche A, Strack A, Friedrich B: Requirements for heterologous production of a complex metalloenzyme: the membrane-bound [NiFe] hydrogenase. J Bacteriol 2005;187:6590-6595.
    • (2005) J Bacteriol , vol.187 , pp. 6590-6595
    • Lenz, O.1    Gleiche, A.2    Strack, A.3    Friedrich, B.4
  • 49
    • 23044432936 scopus 로고    scopus 로고
    • Hydrogen sensing by enzyme-catalyzed electrochemical detection
    • Lutz BJ, Fan ZH, Burgdorf T, Friedrich B: Hydrogen sensing by enzyme-catalyzed electrochemical detection. Anal Chem 2005;77:4969-4975.
    • (2005) Anal Chem , vol.77 , pp. 4969-4975
    • Lutz, B.J.1    Zh, F.2    Burgdorf, T.3    Friedrich, B.4
  • 51
    • 0034065733 scopus 로고    scopus 로고
    • Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
    • Ma K, Weiss R, Adams MW: Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J Bacteriol 2000;182:1864-1871.
    • (2000) J Bacteriol , vol.182 , pp. 1864-1871
    • Ma, K.1    Weiss, R.2    Adams, M.W.3
  • 53
    • 17644429864 scopus 로고    scopus 로고
    • Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation
    • Magalon A, Böck A: Dissection of the maturation reactions of the [NiFe] hydrogenase 3 from Escherichia coli taking place after nickel incorporation. FEBS Lett 2000;473:254-258.
    • (2000) FEBS Lett , vol.473 , pp. 254-258
    • Magalon, A.1    Böck, A.2
  • 54
    • 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 1999;38:14330-14337.
    • (1999) Biochemistry , vol.38 , pp. 14330-14337
    • Massanz, C.1    Friedrich, B.2
  • 55
    • 0034846760 scopus 로고    scopus 로고
    • [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: Gene sequencing, three-dimensional structure determination and refinement at 1.8 Å and modelling studies of its interaction with the tetrahaem cytochrome c3
    • Matias PM, Soares CM, Saraiva LM, Coelho R, Morais J, Le Gall J, Carrondo MA: [NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 Å and modelling studies of its interaction with the tetrahaem cytochrome c3. J Biol Inorg Chem 2001;6:63-81.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 63-81
    • Matias, P.M.1    Soares, C.M.2    Saraiva, L.M.3    Coelho, R.4    Morais, J.5    Le Gall, J.6    Carrondo, M.A.7
  • 58
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson JW, Mehta NS, Maier RJ: Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol Microbiol 2001;39:176-182.
    • (2001) Mol Microbiol , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 59
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik IJ, Ladner CL, Turner RJ: Identification of a twin-arginine leader-binding protein. Mol Microbiol 2001;40:323-331.
    • (2001) Mol Microbiol , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 60
    • 18344395352 scopus 로고    scopus 로고
    • Conservation and specialization in PAS domain dynamics
    • Pandini A, Bonati L: Conservation and specialization in PAS domain dynamics. Protein Eng Des Sel 2005;18:127-137.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 127-137
    • Pandini, A.1    Bonati, L.2
  • 61
    • 0037147254 scopus 로고    scopus 로고
    • HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation
    • Paschos A, Bauer A, Zimmermann A, Zehelein E, Böck A: HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation. J Biol Chem 2002;277:49945-49951.
    • (2002) J Biol Chem , vol.277 , pp. 49945-49951
    • Paschos, A.1    Bauer, A.2    Zimmermann, A.3    Zehelein, E.4    Böck, A.5
  • 62
    • 0035846848 scopus 로고    scopus 로고
    • Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases
    • Paschos A, Glass RS, Böck A: Carbamoylphosphate requirement for synthesis of the active center of [NiFe]-hydrogenases. FEBS Lett 2001;488:9-12.
    • (2001) FEBS Lett , vol.488 , pp. 9-12
    • Paschos, A.1    Glass, R.S.2    Böck, A.3
  • 63
    • 0026032458 scopus 로고
    • Relationship between NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington SJ, Skehel JM, Gennis RB, Walker JE: Relationship between NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 1991;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
  • 64
    • 0036166884 scopus 로고    scopus 로고
    • Expression of a functional NAD-reducing [NiFe] hydrogenase from the Gram-positive Rhodococcus opacus in the Gram-negative Ralstonia eutropha
    • Porthun A, Bernhard M, Friedrich B: Expression of a functional NAD-reducing [NiFe] hydrogenase from the Gram-positive Rhodococcus opacus in the Gram-negative Ralstonia eutropha. Arch Microbiol 2002;177:159-166.
    • (2002) Arch Microbiol , vol.177 , pp. 159-166
    • Porthun, A.1    Bernhard, M.2    Friedrich, B.3
  • 66
    • 0033573148 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the [NiFe] hydrogenase from the hyperthermophilic archaeon, Thermococcus litoralis
    • Rakhely G, Zhou ZH, Adams MW, Kovacs KL: Biochemical and molecular characterization of the [NiFe] hydrogenase from the hyperthermophilic archaeon, Thermococcus litoralis. Eur J Biochem 1999;266:1158-1165.
    • (1999) Eur J Biochem , vol.266 , pp. 1158-1165
    • Rakhely, G.1    Zhou, Z.H.2    Adams, M.W.3    Kovacs, K.L.4
  • 69
    • 11844252075 scopus 로고    scopus 로고
    • The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different
    • Roseboom W, Blokesch M, Böck A, Albracht SP: The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett 2005;579:469-472.
    • (2005) FEBS Lett , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Böck, A.3    Albracht, S.P.4
  • 70
    • 0032146314 scopus 로고    scopus 로고
    • Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit-identification of a soluble precursor of the small subunit in a hypB mutant
    • Sargent F, Ballantine SP, Rugman PA, Palmer T, Boxer DH: Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit- identification of a soluble precursor of the small subunit in a hypB mutant. Eur J Biochem 1998a;255:746-754.
    • (1998) Eur J Biochem , vol.255 , pp. 746-754
    • Sargent, F.1    Ballantine, S.P.2    Rugman, P.A.3    Palmer, T.4    Boxer, D.H.5
  • 72
    • 0018788563 scopus 로고
    • The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties
    • Schink B, Schlegel HG: The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties. Biochim Biophys Acta 1979;567:315-324.
    • (1979) Biochim Biophys Acta , vol.567 , pp. 315-324
    • Schink, B.1    Schlegel, H.G.2
  • 73
    • 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
  • 74
    • 0020807235 scopus 로고
    • Purification of hydrogenases by affinity chromatography on Procion Red-agarose
    • Schneider K, Pinkwart M, Jochim K: Purification of hydrogenases by affinity chromatography on Procion Red-agarose. Biochem J 1983;213:391-398.
    • (1983) Biochem J , vol.213 , pp. 391-398
    • Schneider, K.1    Pinkwart, M.2    Jochim, K.3
  • 75
    • 0017110320 scopus 로고
    • Purification and properties of the soluble hydrogenase from Alcaligenes eutrophus H16
    • Schneider K, Schlegel HG: Purification and properties of the 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
  • 83
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB: PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 1999;63:479-506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 84
    • 0000739582 scopus 로고    scopus 로고
    • Reactions with molecular hydrogen in microorganisms: Evidence for a purely organic hydrogenation catalyst
    • Thauer RK, Klein AR, Hartmann GC: Reactions with molecular hydrogen in microorganisms: evidence for a purely organic hydrogenation catalyst. Chem Rev 1996;96:3031-3042.
    • (1996) Chem Rev , vol.96 , pp. 3031-3042
    • Thauer, R.K.1    Klein, A.R.2    Hartmann, G.C.3
  • 85
    • 14644401765 scopus 로고    scopus 로고
    • [NiFe]-hydrogenase maturation endopeptidase: Structure and function
    • Theodoratou E, Huber R, Böck A: [NiFe]-hydrogenase maturation endopeptidase: structure and function. Biochem Soc Trans 2005;33:108-311.
    • (2005) Biochem Soc Trans , vol.33 , pp. 108-311
    • Theodoratou, E.1    Huber, R.2    Böck, A.3
  • 86
    • 0030012735 scopus 로고    scopus 로고
    • Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eu-trophus requires the hoxW gene product
    • Thiemermann S, Dernedde J, Bernhard M, Schroeder W, Massanz C, Friedrich B: Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eu-trophus requires the hoxW gene product. J Bacteriol 1996;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
  • 87
    • 0025291627 scopus 로고
    • Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
    • Tran-Betcke A, Warnecke U, Böcker C, Zaborosch C, Friedrich B: Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J Bacteriol 1990;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
  • 88
    • 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 SPJ: 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 2004a;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
  • 89
    • 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, Burgdorf T, Bernhard M, Friedrich B, Albracht SPJ: Selective release and function of one of the two FMN groups in the cytoplasmic NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha. Eur J Biochem 2004b;271:801-808.
    • (2004) Eur J Biochem , vol.271 , pp. 801-808
    • Van Der Linden, E.1    Faber, B.W.2    Bleijlevens, B.3    Burgdorf, T.4    Bernhard, M.5    Friedrich, B.6    Albracht, S.P.J.7
  • 91
    • 2142653130 scopus 로고    scopus 로고
    • Molecular biology of microbial hydrogenases
    • Vignais PM, Colbeau A: Molecular biology of microbial hydrogenases. Curr Issues Mol Biol 2004;6:159-188.
    • (2004) Curr Issues Mol Biol , vol.6 , pp. 159-188
    • Vignais, P.M.1    Colbeau, A.2
  • 100
    • 0031723783 scopus 로고    scopus 로고
    • Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16
    • Wolf I, Buhrke T, Dernedde J, Pohlmann A, Friedrich B: Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16. Arch Microbiol 1998;170:451-459.
    • (1998) Arch Microbiol , vol.170 , pp. 451-459
    • Wolf, I.1    Buhrke, T.2    Dernedde, J.3    Pohlmann, A.4    Friedrich, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.