메뉴 건너뛰기




Volumn 68, Issue , 2016, Pages 433-507

The Model [NiFe]-Hydrogenases of Escherichia coli

Author keywords

Bacterial membrane biology; Biohydrogen production; Escherichia coli; Formate hydrogenlyase; Respiratory hydrogen oxidation; NiFe hydrogenase

Indexed keywords

ARGININE; BACTERIAL ENZYME; CYTOCHROME B; ESCHERICHIA COLI PROTEIN; FORMATE DEHYDROGENASE; HYDROGEN; IRON; NICKEL IRON HYDROGENASE; NICKEL IRON HYDROGENASE 1; NICKEL IRON HYDROGENASE 2; NICKEL IRON HYDROGENASE 3; OXYGEN; SULFUR; UNCLASSIFIED DRUG; HYDROGENASE; NICKEL-IRON HYDROGENASE; OXIDOREDUCTASE; UPTAKE HYDROGENASE;

EID: 85027919878     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ampbs.2016.02.008     Document Type: Chapter
Times cited : (94)

References (282)
  • 1
    • 84905390614 scopus 로고    scopus 로고
    • Maturation of Rhizobium leguminosarum hydrogenase in the presence of oxygen requires the interaction of the chaperone HypC and the scaffolding protein HupK
    • Albareda, M., Pacios, L.F., Manyani, H., Rey, L., Brito, B., Imperial, J., et al. Maturation of Rhizobium leguminosarum hydrogenase in the presence of oxygen requires the interaction of the chaperone HypC and the scaffolding protein HupK. The Journal of Biological Chemistry 289 (2014), 21217–21229.
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 21217-21229
    • Albareda, M.1    Pacios, L.F.2    Manyani, H.3    Rey, L.4    Brito, B.5    Imperial, J.6
  • 3
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews, S.C., Berks, B.C., McClay, J., Ambler, A., Quail, M.A., Golby, P., et al. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143 (1997), 3633–3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6
  • 5
    • 0030609822 scopus 로고    scopus 로고
    • S and the transcriptional activator AppY on induction of the Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation
    • S and the transcriptional activator AppY on induction of the Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation. Journal of Bacteriology 179 (1997), 2141–2146.
    • (1997) Journal of Bacteriology , vol.179 , pp. 2141-2146
    • Atlung, T.1    Knudsen, K.2    Heerfordt, L.3    Brondsted, L.4
  • 6
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Molecular Systems Biology, 2(2006), 2006, 0008.
    • (2006) Molecular Systems Biology , vol.2 , Issue.2006 , pp. 0008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 7
    • 84858731069 scopus 로고    scopus 로고
    • Evolution of the metabolic and regulatory networks associated with oxygen availability in two phytopathogenic enterobacteria
    • Babujee, L., Apodaca, J., Balakrishnan, V., Liss, P., Kiley, P.J., Charkowski, A.O., et al. Evolution of the metabolic and regulatory networks associated with oxygen availability in two phytopathogenic enterobacteria. BMC Genomics, 13, 2012, 110.
    • (2012) BMC Genomics , vol.13 , pp. 110
    • Babujee, L.1    Apodaca, J.2    Balakrishnan, V.3    Liss, P.4    Kiley, P.J.5    Charkowski, A.O.6
  • 8
    • 0035218392 scopus 로고    scopus 로고
    • Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli
    • Bagramyan, K., Vassilian, A., Mnatsakanyan, N., Trchounian, A., Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli. Membrane & Cell Biology 14 (2001), 749–763.
    • (2001) Membrane & Cell Biology , vol.14 , pp. 749-763
    • Bagramyan, K.1    Vassilian, A.2    Mnatsakanyan, N.3    Trchounian, A.4
  • 9
    • 84865002188 scopus 로고    scopus 로고
    • Hydrogen production by overexpression of hydrogenase subunit in oxygen-tolerant Klebsiella oxytoca HP1
    • Bai, L., Wu, X., Jiang, L., Liu, J., Long, M., Hydrogen production by overexpression of hydrogenase subunit in oxygen-tolerant Klebsiella oxytoca HP1. International Journal of Hydrogen Energy 37 (2012), 13227–13233.
    • (2012) International Journal of Hydrogen Energy , vol.37 , pp. 13227-13233
    • Bai, L.1    Wu, X.2    Jiang, L.3    Liu, J.4    Long, M.5
  • 10
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • Ballantine, S.P., Boxer, D.H., Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. Journal of Bacteriology 163 (1985), 454–459.
    • (1985) Journal of Bacteriology , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 11
    • 0023049446 scopus 로고
    • Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli
    • Ballantine, S.P., Boxer, D.H., Isolation and characterisation of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. European Journal of Biochemistry 156 (1986), 277–284.
    • (1986) European Journal of Biochemistry , vol.156 , pp. 277-284
    • Ballantine, S.P.1    Boxer, D.H.2
  • 13
    • 84881648258 scopus 로고    scopus 로고
    • The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes
    • Batista, A.P., Marreiros, B.C., Pereira, M.M., The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes. Biological Chemistry 394 (2013), 659–666.
    • (2013) Biological Chemistry , vol.394 , pp. 659-666
    • Batista, A.P.1    Marreiros, B.C.2    Pereira, M.M.3
  • 14
    • 0029763232 scopus 로고    scopus 로고
    • Hydrogen biotechnology: Progress and prospects
    • Benemann, J., Hydrogen biotechnology: Progress and prospects. Nature Biotechnology 14 (1996), 1101–1103.
    • (1996) Nature Biotechnology , vol.14 , pp. 1101-1103
    • Benemann, J.1
  • 15
    • 84903370967 scopus 로고    scopus 로고
    • Twin-arginine translocation system in Helicobacter pylori: TatC, but not TatB, is essential for viability
    • Benoit, S.L., Maier, R.J., Twin-arginine translocation system in Helicobacter pylori: TatC, but not TatB, is essential for viability. mBio, 5, 2014, e01016-13.
    • (2014) mBio , vol.5 , pp. e01016-13
    • Benoit, S.L.1    Maier, R.J.2
  • 16
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B.C., A common export pathway for proteins binding complex redox cofactors?. Molecular Microbiology 22 (1996), 393–404.
    • (1996) Molecular Microbiology , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 18
    • 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. Journal of Bacteriology 178 (1996), 4522–4529.
    • (1996) Journal of Bacteriology , vol.178 , pp. 4522-4529
    • Bernhard, M.1    Schwartz, E.2    Rietdorf, J.3    Friedrich, B.4
  • 19
    • 84885083599 scopus 로고    scopus 로고
    • Effect of osmolytes on the fibrillation of HypF-N
    • Bhavsar, R.D., Prasad, S., Roy, I., Effect of osmolytes on the fibrillation of HypF-N. Biochimie 95 (2013), 2190–2193.
    • (2013) Biochimie , vol.95 , pp. 2190-2193
    • Bhavsar, R.D.1    Prasad, S.2    Roy, I.3
  • 20
    • 0030045930 scopus 로고    scopus 로고
    • Nickel incorporation into hydrogenase 3 from Escherichia coli requires the precursor form of the large subunit
    • Binder, U., Maier, T., Böck, A., Nickel incorporation into hydrogenase 3 from Escherichia coli requires the precursor form of the large subunit. Archives of Microbiology 165 (1996), 69–72.
    • (1996) Archives of Microbiology , vol.165 , pp. 69-72
    • Binder, U.1    Maier, T.2    Böck, A.3
  • 21
    • 33747093365 scopus 로고    scopus 로고
    • The effect of nutrient limitation on hydrogen production by batch cultures of Escherichia coli
    • Bisaillon, A., Turcot, J., Hallenbeck, P.C., The effect of nutrient limitation on hydrogen production by batch cultures of Escherichia coli. International Journal of Hydrogen Energy 31 (2006), 1504–1508.
    • (2006) International Journal of Hydrogen Energy , vol.31 , pp. 1504-1508
    • Bisaillon, A.1    Turcot, J.2    Hallenbeck, P.C.3
  • 22
    • 84939946161 scopus 로고    scopus 로고
    • Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system
    • Blanc, B., Gerez, C., Ollagnier de Choudens, S., Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system. Biochimica et Biophysica Acta 1853 (2015), 1436–1447.
    • (2015) Biochimica et Biophysica Acta , vol.1853 , pp. 1436-1447
    • Blanc, B.1    Gerez, C.2    Ollagnier de Choudens, S.3
  • 23
    • 84930944252 scopus 로고    scopus 로고
    • o-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N′-dicyclohexylcarbodiimide in the mutants lacking hydrogenases
    • o-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N′-dicyclohexylcarbodiimide in the mutants lacking hydrogenases. Archives of Biochemistry and Biophysics 579 (2015), 67–72.
    • (2015) Archives of Biochemistry and Biophysics , vol.579 , pp. 67-72
    • Blbulyan, S.1    Trchounian, A.2
  • 24
    • 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, S.P., Matzanke, B.F., Drapal, N.M., 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. Journal of Molecular Biology 344 (2004), 155–167.
    • (2004) Journal of Molecular Biology , 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
  • 25
    • 33745867578 scopus 로고    scopus 로고
    • Properties of the [NiFe]-hydrogenase maturation protein HypD
    • Blokesch, M., Böck, A., Properties of the [NiFe]-hydrogenase maturation protein HypD. FEBS Letters 580 (2006), 4065–4068.
    • (2006) FEBS Letters , vol.580 , pp. 4065-4068
    • Blokesch, M.1    Böck, A.2
  • 26
    • 0035048481 scopus 로고    scopus 로고
    • Interplay between the specific chaperone-like proteins HybG and HypC in maturation of hydrogenases 1, 2, and 3 from Escherichia coli
    • Blokesch, M., Magalon, A., Böck, A., Interplay between the specific chaperone-like proteins HybG and HypC in maturation of hydrogenases 1, 2, and 3 from Escherichia coli. Journal of Bacteriology 183 (2001), 2817–2822.
    • (2001) Journal of Bacteriology , vol.183 , pp. 2817-2822
    • Blokesch, M.1    Magalon, A.2    Böck, A.3
  • 27
    • 1942539935 scopus 로고    scopus 로고
    • HybF, a zinc-containing protein involved in NiFe hydrogenase maturation
    • Blokesch, M., Rohrmoser, M., Rode, S., Böck, A., HybF, a zinc-containing protein involved in NiFe hydrogenase maturation. Journal of Bacteriology 186 (2004), 2603–2611.
    • (2004) Journal of Bacteriology , vol.186 , pp. 2603-2611
    • Blokesch, M.1    Rohrmoser, M.2    Rode, S.3    Böck, A.4
  • 31
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch, E.G., Sargent, F., Stanley, N.R., Berks, B.C., Robinson, C., Palmer, T., An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. The Journal of Biological Chemistry 273 (1998), 18003–18006.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 32
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Bohm, R., Sauter, M., Böck, A., Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Molecular Microbiology 4 (1990), 231–243.
    • (1990) Molecular Microbiology , vol.4 , pp. 231-243
    • Bohm, R.1    Sauter, M.2    Böck, A.3
  • 33
    • 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, P.K., Parkin, A., Hunter, W.N., Sargent, F., How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase. The Biochemical Journal 458 (2014), 449–458.
    • (2014) The Biochemical Journal , 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
  • 34
    • 84884909648 scopus 로고    scopus 로고
    • A regulatory domain controls the transport activity of a twin-arginine signal peptide
    • Bowman, L., Palmer, T., Sargent, F., A regulatory domain controls the transport activity of a twin-arginine signal peptide. FEBS Letters 587 (2013), 3365–3370.
    • (2013) FEBS Letters , vol.587 , pp. 3365-3370
    • Bowman, L.1    Palmer, T.2    Sargent, F.3
  • 36
    • 0027980255 scopus 로고
    • Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli
    • Brondsted, L., Atlung, T., Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli. Journal of Bacteriology 176 (1994), 5423–5428.
    • (1994) Journal of Bacteriology , vol.176 , pp. 5423-5428
    • Brondsted, L.1    Atlung, T.2
  • 37
    • 0029866860 scopus 로고    scopus 로고
    • Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli
    • Brondsted, L., Atlung, T., Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli. Journal of Bacteriology 178 (1996), 1556–1564.
    • (1996) Journal of Bacteriology , vol.178 , pp. 1556-1564
    • Brondsted, L.1    Atlung, T.2
  • 40
    • 84869083333 scopus 로고    scopus 로고
    • Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state
    • Campioni, S., Mannini, B., Lopez-Alonso, J.P., Shalova, I.N., Penco, A., Mulvihill, E., et al. Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state. Journal of Molecular Biology 424 (2012), 132–149.
    • (2012) Journal of Molecular Biology , vol.424 , pp. 132-149
    • Campioni, S.1    Mannini, B.2    Lopez-Alonso, J.P.3    Shalova, I.N.4    Penco, A.5    Mulvihill, E.6
  • 42
    • 0031792216 scopus 로고    scopus 로고
    • Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli
    • Chanal, A., Santini, C., Wu, L., Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli. Molecular Microbiology 30 (1998), 674–676.
    • (1998) Molecular Microbiology , vol.30 , pp. 674-676
    • Chanal, A.1    Santini, C.2    Wu, L.3
  • 43
    • 52249089592 scopus 로고    scopus 로고
    • Structural characterization of a putative endogenous metal chelator in the periplasmic nickel transporter NikA
    • Cherrier, M.V., Cavazza, C., Bochot, C., Lemaire, D., Fontecilla-Camps, J.C., Structural characterization of a putative endogenous metal chelator in the periplasmic nickel transporter NikA. Biochemistry 47 (2008), 9937–9943.
    • (2008) Biochemistry , vol.47 , pp. 9937-9943
    • Cherrier, M.V.1    Cavazza, C.2    Bochot, C.3    Lemaire, D.4    Fontecilla-Camps, J.C.5
  • 46
    • 0032697047 scopus 로고    scopus 로고
    • NikR is a ribbon–helix–helix DNA-binding protein
    • Chivers, P.T., Sauer, R.T., NikR is a ribbon–helix–helix DNA-binding protein. Protein Science 8 (1999), 2494–2500.
    • (1999) Protein Science , vol.8 , pp. 2494-2500
    • Chivers, P.T.1    Sauer, R.T.2
  • 47
    • 0036774881 scopus 로고    scopus 로고
    • NikR repressor: High-affinity nickel binding to the C-terminal domain regulates binding to operator DNA
    • Chivers, P.T., Sauer, R.T., NikR repressor: High-affinity nickel binding to the C-terminal domain regulates binding to operator DNA. Chemistry & Biology 9 (2002), 1141–1148.
    • (2002) Chemistry & Biology , vol.9 , pp. 1141-1148
    • Chivers, P.T.1    Sauer, R.T.2
  • 50
    • 84922282570 scopus 로고    scopus 로고
    • What is the trigger mechanism for the reversal of electron flow in oxygen-tolerant [NiFe] hydrogenases?
    • Dance, I., What is the trigger mechanism for the reversal of electron flow in oxygen-tolerant [NiFe] hydrogenases?. Chemical Science 6 (2015), 1433–1443.
    • (2015) Chemical Science , vol.6 , pp. 1433-1443
    • Dance, I.1
  • 52
    • 35748956722 scopus 로고    scopus 로고
    • Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies
    • De Lacey, A.L., Fernandez, V.M., Rousset, M., Cammack, R., Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies. Chemical Reviews 107 (2007), 4304–4330.
    • (2007) Chemical Reviews , vol.107 , pp. 4304-4330
    • De Lacey, A.L.1    Fernandez, V.M.2    Rousset, M.3    Cammack, R.4
  • 54
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • DeLisa, M.P., Lee, P., Palmer, T., Georgiou, G., Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. Journal of Bacteriology 186 (2004), 366–373.
    • (2004) Journal of Bacteriology , vol.186 , pp. 366-373
    • DeLisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 55
    • 0028878506 scopus 로고
    • Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12
    • de Pina, K., Navarro, C., McWalter, L., Boxer, D.H., Price, N.C., Kelly, S.M., et al. Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12. European Journal of Biochemistry 227 (1995), 857–865.
    • (1995) European Journal of Biochemistry , vol.227 , pp. 857-865
    • de Pina, K.1    Navarro, C.2    McWalter, L.3    Boxer, D.H.4    Price, N.C.5    Kelly, S.M.6
  • 56
    • 33746868000 scopus 로고    scopus 로고
    • Anaerobic fermentation of glycerol by Escherichia coli: A new platform for metabolic engineering
    • Dharmadi, Y., Murarka, A., Gonzalez, R., Anaerobic fermentation of glycerol by Escherichia coli: A new platform for metabolic engineering. Biotechnology and Bioengineering 94 (2006), 821–829.
    • (2006) Biotechnology and Bioengineering , vol.94 , pp. 821-829
    • Dharmadi, Y.1    Murarka, A.2    Gonzalez, R.3
  • 57
    • 56249119177 scopus 로고    scopus 로고
    • Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB
    • Dias, A.V., Mulvihill, C.M., Leach, M.R., Pickering, I.J., George, G.N., Zamble, D.B., Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB. Biochemistry 47 (2008), 11981–11991.
    • (2008) Biochemistry , vol.47 , pp. 11981-11991
    • Dias, A.V.1    Mulvihill, C.M.2    Leach, M.R.3    Pickering, I.J.4    George, G.N.5    Zamble, D.B.6
  • 58
    • 84904246789 scopus 로고    scopus 로고
    • Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation
    • Doberenz, C., Zorn, M., Falke, D., Nannemann, D., Hunger, D., Beyer, L., et al. Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation. Journal of Molecular Biology 426 (2014), 2827–2839.
    • (2014) Journal of Molecular Biology , vol.426 , pp. 2827-2839
    • Doberenz, C.1    Zorn, M.2    Falke, D.3    Nannemann, D.4    Hunger, D.5    Beyer, L.6
  • 59
    • 0033851906 scopus 로고    scopus 로고
    • Deletion of the hmc operon of Desulfovibrio vulgaris subsp. Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment
    • Dolla, A., Pohorelic, B.K., Voordouw, J.K., Voordouw, G., Deletion of the hmc operon of Desulfovibrio vulgaris subsp. Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment. Archives of Microbiology 174 (2000), 143–151.
    • (2000) Archives of Microbiology , vol.174 , pp. 143-151
    • Dolla, A.1    Pohorelic, B.K.2    Voordouw, J.K.3    Voordouw, G.4
  • 60
    • 84883466577 scopus 로고    scopus 로고
    • Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins
    • Douglas, C.D., Ngu, T.T., Kaluarachchi, H., Zamble, D.B., Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins. Biochemistry 52 (2013), 6030–6039.
    • (2013) Biochemistry , vol.52 , pp. 6030-6039
    • Douglas, C.D.1    Ngu, T.T.2    Kaluarachchi, H.3    Zamble, D.B.4
  • 61
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
    • Drapal, N., Böck, A., Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry 37 (1998), 2941–2948.
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Böck, A.2
  • 63
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • Dubini, A., Pye, R.L., Jack, R.L., Palmer, T., Sargent, F., How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. International Journal of Hydrogen Energy 27 (2002), 1413–1420.
    • (2002) International Journal of Hydrogen Energy , vol.27 , pp. 1413-1420
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 64
    • 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 Letters 549 (2003), 141–146.
    • (2003) FEBS Letters , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 66
    • 84864659415 scopus 로고    scopus 로고
    • The coupling mechanism of respiratory complex I—A structural and evolutionary perspective
    • Efremov, R.G., Sazanov, L.A., The coupling mechanism of respiratory complex I—A structural and evolutionary perspective. Biochimica et Biophysica Acta 1817 (2012), 1785–1795.
    • (2012) Biochimica et Biophysica Acta , vol.1817 , pp. 1785-1795
    • Efremov, R.G.1    Sazanov, L.A.2
  • 67
    • 84949008127 scopus 로고    scopus 로고
    • TatE as a regular constituent of bacterial twin-arginine protein translocases
    • Eimer, E., Frobel, J., Blummel, A.S., Muller, M., TatE as a regular constituent of bacterial twin-arginine protein translocases. The Journal of Biological Chemistry 290:49 (2015), 29281–29289.
    • (2015) The Journal of Biological Chemistry , vol.290 , Issue.49 , pp. 29281-29289
    • Eimer, E.1    Frobel, J.2    Blummel, A.S.3    Muller, M.4
  • 69
    • 0016711942 scopus 로고
    • The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli
    • Enoch, H.G., Lester, R.L., The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. The Journal of Biological Chemistry 250 (1975), 6693–6705.
    • (1975) The Journal of Biological Chemistry , vol.250 , pp. 6693-6705
    • Enoch, H.G.1    Lester, R.L.2
  • 70
    • 49349107465 scopus 로고    scopus 로고
    • Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH: Ubiquinone oxidoreductase (Complex I)
    • Euro, L., Belevich, G., Verkhovsky, M.I., Wikstrom, M., Verkhovskaya, M., Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH: Ubiquinone oxidoreductase (Complex I). Biochimica et Biophysica Acta 1777 (2008), 1166–1172.
    • (2008) Biochimica et Biophysica Acta , vol.1777 , pp. 1166-1172
    • Euro, L.1    Belevich, G.2    Verkhovsky, M.I.3    Wikstrom, M.4    Verkhovskaya, M.5
  • 72
    • 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, R.M., Parkin, A., Roessler, M.M., Murphy, B.J., Adamson, H., Lukey, M.J., 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. Journal of the American Chemical Society 135 (2013), 2694–2707.
    • (2013) Journal of the American Chemical Society , vol.135 , pp. 2694-2707
    • Evans, R.M.1    Parkin, A.2    Roessler, M.M.3    Murphy, B.J.4    Adamson, H.5    Lukey, M.J.6
  • 73
    • 74349124142 scopus 로고    scopus 로고
    • Unexpected oligomeric structure of the FocA formate channel of Escherichia coli: A paradigm for the formate-nitrite transporter family of integral membrane proteins
    • Falke, D., Schulz, K., Doberenz, C., Beyer, L., Lilie, H., Thiemer, B., et al. Unexpected oligomeric structure of the FocA formate channel of Escherichia coli: A paradigm for the formate-nitrite transporter family of integral membrane proteins. FEMS Microbiology Letters 303 (2010), 69–75.
    • (2010) FEMS Microbiology Letters , vol.303 , pp. 69-75
    • Falke, D.1    Schulz, K.2    Doberenz, C.3    Beyer, L.4    Lilie, H.5    Thiemer, B.6
  • 74
    • 84865491875 scopus 로고    scopus 로고
    • Concerted movement in pH-dependent gating of FocA from molecular dynamics simulations
    • Feng, Z., Hou, T., Li, Y., Concerted movement in pH-dependent gating of FocA from molecular dynamics simulations. Journal of Chemical Information and Modeling 52 (2012), 2119–2131.
    • (2012) Journal of Chemical Information and Modeling , vol.52 , pp. 2119-2131
    • Feng, Z.1    Hou, T.2    Li, Y.3
  • 75
    • 34250316617 scopus 로고    scopus 로고
    • The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase
    • Filenko, N., Spiro, S., Browning, D.F., Squire, D., Overton, T.W., Cole, J., et al. The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase. Journal of Bacteriology 189 (2007), 4410–4417.
    • (2007) Journal of Bacteriology , vol.189 , pp. 4410-4417
    • Filenko, N.1    Spiro, S.2    Browning, D.F.3    Squire, D.4    Overton, T.W.5    Cole, J.6
  • 76
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps, J.C., Volbeda, A., Cavazza, C., Nicolet, Y., Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chemical Reviews 107 (2007), 4273–4303.
    • (2007) Chemical Reviews , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 78
    • 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 50 (2011), 10836–10843.
    • (2011) Biochemistry , vol.50 , pp. 10836-10843
    • Frielingsdorf, S.1    Schubert, T.2    Pohlmann, A.3    Lenz, O.4    Friedrich, B.5
  • 79
    • 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. Journal of Bacteriology 193 (2011), 2487–2497.
    • (2011) Journal of Bacteriology , vol.193 , pp. 2487-2497
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 80
    • 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., Kroschinsky, S., Friedrich, B., Lenz, O., et al. The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre. Nature 479 (2011), 249–252.
    • (2011) Nature , vol.479 , pp. 249-252
    • Fritsch, J.1    Scheerer, P.2    Frielingsdorf, S.3    Kroschinsky, S.4    Friedrich, B.5    Lenz, O.6
  • 81
    • 0033591263 scopus 로고    scopus 로고
    • Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli
    • Fritsche, E., Paschos, A., Beisel, H.G., Böck, A., Huber, R., Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli. Journal of Molecular Biology 288 (1999), 989–998.
    • (1999) Journal of Molecular Biology , vol.288 , pp. 989-998
    • Fritsche, E.1    Paschos, A.2    Beisel, H.G.3    Böck, A.4    Huber, R.5
  • 82
    • 84871785408 scopus 로고    scopus 로고
    • Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB
    • Frobel, J., Rose, P., Lausberg, F., Blummel, A.S., Freudl, R., Muller, M., Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB. Nature Communications, 3, 2012, 1311.
    • (2012) Nature Communications , vol.3 , pp. 1311
    • Frobel, J.1    Rose, P.2    Lausberg, F.3    Blummel, A.S.4    Freudl, R.5    Muller, M.6
  • 85
    • 50249129588 scopus 로고    scopus 로고
    • A new model for the anaerobic fermentation of glycerol in enteric bacteria: Trunk and auxiliary pathways in Escherichia coli
    • Gonzalez, R., Murarka, A., Dharmadi, Y., Yazdani, S.S., A new model for the anaerobic fermentation of glycerol in enteric bacteria: Trunk and auxiliary pathways in Escherichia coli. Metabolic Engineering 10 (2008), 234–245.
    • (2008) Metabolic Engineering , vol.10 , pp. 234-245
    • Gonzalez, R.1    Murarka, A.2    Dharmadi, Y.3    Yazdani, S.S.4
  • 86
    • 79955072473 scopus 로고    scopus 로고
    • A unique iron–sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase
    • Goris, T., Wait, A.F., Saggu, M., Fritsch, J., Heidary, N., Stein, M., et al. A unique iron–sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nature Chemical Biology 7 (2011), 310–318.
    • (2011) Nature Chemical Biology , vol.7 , pp. 310-318
    • Goris, T.1    Wait, A.F.2    Saggu, M.3    Fritsch, J.4    Heidary, N.5    Stein, M.6
  • 88
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? The role of arginine in enzyme-catalyzed proton abstractions
    • Guillen Schlippe, Y.V., Hedstrom, L., A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Archives of Biochemistry and Biophysics 433 (2005), 266–278.
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , pp. 266-278
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 89
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • Hatzixanthis, K., Palmer, T., Sargent, F., A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Molecular Microbiology 49 (2003), 1377–1390.
    • (2003) Molecular Microbiology , vol.49 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 90
    • 0346118916 scopus 로고    scopus 로고
    • Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli
    • Heddle, J., Scott, D.J., Unzai, S., Park, S.Y., Tame, J.R., Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli. The Journal of Biological Chemistry 278 (2003), 50322–50329.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 50322-50329
    • Heddle, J.1    Scott, D.J.2    Unzai, S.3    Park, S.Y.4    Tame, J.R.5
  • 92
    • 84897972583 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R., Hall, J., Basu, P., The mononuclear molybdenum enzymes. Chemical Reviews 114 (2014), 3963–4038.
    • (2014) Chemical Reviews , vol.114 , pp. 3963-4038
    • Hille, R.1    Hall, J.2    Basu, P.3
  • 93
  • 94
    • 72949091838 scopus 로고    scopus 로고
    • An evolved Escherichia coli strain for producing hydrogen and ethanol from glycerol
    • Hu, H., Wood, T.K., An evolved Escherichia coli strain for producing hydrogen and ethanol from glycerol. Biochemical and Biophysical Research Communications 391 (2010), 1033–1038.
    • (2010) Biochemical and Biophysical Research Communications , vol.391 , pp. 1033-1038
    • Hu, H.1    Wood, T.K.2
  • 96
    • 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. Journal of Bacteriology 184 (2002), 3879–3885.
    • (2002) Journal of Bacteriology , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Böck, A.3
  • 97
    • 84904215415 scopus 로고    scopus 로고
    • Identification of key residues in the formate channel FocA that control import and export of formate
    • Hunger, D., Doberenz, C., Sawers, R.G., Identification of key residues in the formate channel FocA that control import and export of formate. Biological Chemistry 395 (2014), 813–825.
    • (2014) Biological Chemistry , vol.395 , pp. 813-825
    • Hunger, D.1    Doberenz, C.2    Sawers, R.G.3
  • 99
    • 84885381858 scopus 로고    scopus 로고
    • Signal peptide etiquette during assembly of a complex respiratory enzyme
    • James, M.J., Coulthurst, S.J., Palmer, T., Sargent, F., Signal peptide etiquette during assembly of a complex respiratory enzyme. Molecular Microbiology 90 (2013), 400–414.
    • (2013) Molecular Microbiology , vol.90 , pp. 400-414
    • James, M.J.1    Coulthurst, S.J.2    Palmer, T.3    Sargent, F.4
  • 100
    • 84942107138 scopus 로고    scopus 로고
    • Activation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3)
    • Jo, B.H., Cha, H.J., Activation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3). Microbial Cell Factories, 14, 2015, 151.
    • (2015) Microbial Cell Factories , vol.14 , pp. 151
    • Jo, B.H.1    Cha, H.J.2
  • 101
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka, M., Tornroth, S., Byrne, B., Iwata, S., Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N. Science 295 (2002), 1863–1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 103
    • 83455221556 scopus 로고    scopus 로고
    • Escherichia coli SlyD, more than a Ni(II) reservoir
    • Kaluarachchi, H., Zhang, J.W., Zamble, D.B., Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry 50 (2011), 10761–10763.
    • (2011) Biochemistry , vol.50 , pp. 10761-10763
    • Kaluarachchi, H.1    Zhang, J.W.2    Zamble, D.B.3
  • 104
    • 0021733814 scopus 로고
    • Molecular-cloning and physical mapping of the hyd gene of Escherichia coli K-12
    • Karube, I., Tomiyama, M., Kikuchi, A., Molecular-cloning and physical mapping of the hyd gene of Escherichia coli K-12. FEMS Microbiology Letters 25 (1984), 165–168.
    • (1984) FEMS Microbiology Letters , vol.25 , pp. 165-168
    • Karube, I.1    Tomiyama, M.2    Kikuchi, A.3
  • 105
    • 34547913808 scopus 로고    scopus 로고
    • Construction of consecutive deletions of the Escherichia coli chromosome
    • Kato, J., Hashimoto, M., Construction of consecutive deletions of the Escherichia coli chromosome. Molecular Systems Biology, 3, 2007, 132.
    • (2007) Molecular Systems Biology , vol.3 , pp. 132
    • Kato, J.1    Hashimoto, M.2
  • 106
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution
    • Katti, S.K., LeMaster, D.M., Eklund, H., Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. Journal of Molecular Biology 212 (1990), 167–184.
    • (1990) Journal of Molecular Biology , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 107
    • 84869146885 scopus 로고    scopus 로고
    • Co-operation between different targeting pathways during integration of a membrane protein
    • Keller, R., de Keyzer, J., Driessen, A.J., Palmer, T., Co-operation between different targeting pathways during integration of a membrane protein. The Journal of Cell Biology 199 (2012), 303–315.
    • (2012) The Journal of Cell Biology , vol.199 , pp. 303-315
    • Keller, R.1    de Keyzer, J.2    Driessen, A.J.3    Palmer, T.4
  • 108
    • 0032502268 scopus 로고    scopus 로고
    • Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer
    • Khangulov, S.V., Gladyshev, V.N., Dismukes, G.C., Stadtman, T.C., Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37 (1998), 3518–3528.
    • (1998) Biochemistry , vol.37 , pp. 3518-3528
    • Khangulov, S.V.1    Gladyshev, V.N.2    Dismukes, G.C.3    Stadtman, T.C.4
  • 109
    • 0027022263 scopus 로고
    • Families of twelve transmembrane domain transporters
    • Kilty, J.E., Amara, S.G., Families of twelve transmembrane domain transporters. Current Opinion in Biotechnology 3 (1992), 675–682.
    • (1992) Current Opinion in Biotechnology , vol.3 , pp. 675-682
    • Kilty, J.E.1    Amara, S.G.2
  • 110
    • 77955159360 scopus 로고    scopus 로고
    • Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in Escherichia coli
    • Kim, J.Y., Jo, B.H., Cha, H.J., Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in Escherichia coli. Microbial Cell Factories, 9, 2010, 54.
    • (2010) Microbial Cell Factories , vol.9 , pp. 54
    • Kim, J.Y.1    Jo, B.H.2    Cha, H.J.3
  • 111
    • 80052373534 scopus 로고    scopus 로고
    • Production of biohydrogen by heterologous expression of oxygen-tolerant Hydrogenovibrio marinus [NiFe]-hydrogenase in Escherichia coli
    • Kim, J.Y., Jo, B.H., Cha, H.J., Production of biohydrogen by heterologous expression of oxygen-tolerant Hydrogenovibrio marinus [NiFe]-hydrogenase in Escherichia coli. Journal of Biotechnology 155 (2011), 312–319.
    • (2011) Journal of Biotechnology , vol.155 , pp. 312-319
    • Kim, J.Y.1    Jo, B.H.2    Cha, H.J.3
  • 112
    • 0032835259 scopus 로고    scopus 로고
    • Response of hya expression to external pH in Escherichia coli
    • King, P.W., Przybyla, A.E., Response of hya expression to external pH in Escherichia coli. Journal of Bacteriology 181 (1999), 5250–5256.
    • (1999) Journal of Bacteriology , vol.181 , pp. 5250-5256
    • King, P.W.1    Przybyla, A.E.2
  • 116
    • 84885457541 scopus 로고    scopus 로고
    • Identification of the set of genes, including nonannotated morA, under the direct control of ModE in Escherichia coli
    • Kurata, T., Katayama, A., Hiramatsu, M., Kiguchi, Y., Takeuchi, M., Watanabe, T., et al. Identification of the set of genes, including nonannotated morA, under the direct control of ModE in Escherichia coli. Journal of Bacteriology 195 (2013), 4496–4505.
    • (2013) Journal of Bacteriology , vol.195 , pp. 4496-4505
    • Kurata, T.1    Katayama, A.2    Hiramatsu, M.3    Kiguchi, Y.4    Takeuchi, M.5    Watanabe, T.6
  • 117
    • 84903600136 scopus 로고    scopus 로고
    • Selenoproteins: Molecular pathways and physiological roles
    • Labunskyy, V.M., Hatfield, D.L., Gladyshev, V.N., Selenoproteins: Molecular pathways and physiological roles. Physics Review 94 (2014), 739–777.
    • (2014) Physics Review , vol.94 , pp. 739-777
    • Labunskyy, V.M.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 118
    • 0035822537 scopus 로고    scopus 로고
    • 2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors
    • 2 consumption by Escherichia coli coupled via hydrogenase 1 or hydrogenase 2 to different terminal electron acceptors. FEMS Microbiology Letters 202 (2001), 121–124.
    • (2001) FEMS Microbiology Letters , vol.202 , pp. 121-124
    • Laurinavichene, T.V.1    Tsygankov, A.A.2
  • 119
    • 0036431454 scopus 로고    scopus 로고
    • Effect of redox potential on activity of hydrogenase 1 and hydrogenase 2 in Escherichia coli
    • Laurinavichene, T.V., Zorin, N.A., Tsygankov, A.A., Effect of redox potential on activity of hydrogenase 1 and hydrogenase 2 in Escherichia coli. Archives of Microbiology 178 (2002), 437–442.
    • (2002) Archives of Microbiology , vol.178 , pp. 437-442
    • Laurinavichene, T.V.1    Zorin, N.A.2    Tsygankov, A.A.3
  • 120
    • 84862746985 scopus 로고    scopus 로고
    • Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli
    • Lausberg, F., Fleckenstein, S., Kreutzenbeck, P., Frobel, J., Rose, P., Muller, M., et al. Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli. PLoS ONE, 7, 2012, e39867.
    • (2012) PLoS ONE , vol.7 , pp. e39867
    • Lausberg, F.1    Fleckenstein, S.2    Kreutzenbeck, P.3    Frobel, J.4    Rose, P.5    Muller, M.6
  • 122
    • 77952721977 scopus 로고    scopus 로고
    • Structure and function of enzymes in heme biosynthesis
    • Layer, G., Reichelt, J., Jahn, D., Heinz, D.W., Structure and function of enzymes in heme biosynthesis. Protein Science 19 (2010), 1137–1161.
    • (2010) Protein Science , vol.19 , pp. 1137-1161
    • Layer, G.1    Reichelt, J.2    Jahn, D.3    Heinz, D.W.4
  • 124
    • 24644474525 scopus 로고    scopus 로고
    • Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB
    • Leach, M.R., Sandal, S., Sun, H., Zamble, D.B., Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB. Biochemistry 44 (2005), 12229–12238.
    • (2005) Biochemistry , vol.44 , pp. 12229-12238
    • Leach, M.R.1    Sandal, S.2    Sun, H.3    Zamble, D.B.4
  • 125
    • 84908164053 scopus 로고    scopus 로고
    • Promiscuous nickel import in human pathogens: Structure, thermodynamics, and evolution of extracytoplasmic nickel-binding proteins
    • Lebrette, H., Brochier-Armanet, C., Zambelli, B., de Reuse, H., Borezee-Durant, E., Ciurli, S., et al. Promiscuous nickel import in human pathogens: Structure, thermodynamics, and evolution of extracytoplasmic nickel-binding proteins. Structure 22 (2014), 1421–1432.
    • (2014) Structure , vol.22 , pp. 1421-1432
    • Lebrette, H.1    Brochier-Armanet, C.2    Zambelli, B.3    de Reuse, H.4    Borezee-Durant, E.5    Ciurli, S.6
  • 127
  • 131
    • 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., Wisitruangsakul, N., Saggu, M., Strack, A., et al. Concerted action of two novel auxiliary proteins in assembly of the active site in a membrane-bound [NiFe] hydrogenase. The Journal of Biological Chemistry 284 (2009), 2159–2168.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 2159-2168
    • Ludwig, M.1    Schubert, T.2    Zebger, I.3    Wisitruangsakul, N.4    Saggu, M.5    Strack, A.6
  • 133
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [NiFe]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe–S cluster
    • Lukey, M.J., Roessler, M.M., Parkin, A., Evans, R.M., Davies, R.A., Lenz, O., et al. Oxygen-tolerant [NiFe]-hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe–S cluster. Journal of the American Chemical Society 133 (2011), 16881–16892.
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 16881-16892
    • Lukey, M.J.1    Roessler, M.M.2    Parkin, A.3    Evans, R.M.4    Davies, R.A.5    Lenz, O.6
  • 134
    • 0025975104 scopus 로고
    • Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • Lutz, S., Jacobi, A., Schlensog, V., Bohm, R., Sawers, G., Böck, A., Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Molecular Microbiology 5 (1991), 123–135.
    • (1991) Molecular Microbiology , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Bohm, R.4    Sawers, G.5    Böck, A.6
  • 135
    • 84890617295 scopus 로고    scopus 로고
    • Exploring the pH-dependent substrate transport mechanism of FocA using molecular dynamics simulation
    • Lv, X., Liu, H., Ke, M., Gong, H., Exploring the pH-dependent substrate transport mechanism of FocA using molecular dynamics simulation. Biophysical Journal 105 (2013), 2714–2723.
    • (2013) Biophysical Journal , vol.105 , pp. 2714-2723
    • Lv, X.1    Liu, H.2    Ke, M.3    Gong, H.4
  • 136
    • 36348955587 scopus 로고    scopus 로고
    • Enhanced hydrogen production from glucose by metabolically engineered Escherichia coli
    • Maeda, T., Sanchez-Torres, V., Wood, T.K., Enhanced hydrogen production from glucose by metabolically engineered Escherichia coli. Applied Microbiology and Biotechnology 77 (2007), 879–890.
    • (2007) Applied Microbiology and Biotechnology , vol.77 , pp. 879-890
    • Maeda, T.1    Sanchez-Torres, V.2    Wood, T.K.3
  • 137
    • 34548674731 scopus 로고    scopus 로고
    • Escherichia coli hydrogenase 3 is a reversible enzyme possessing hydrogen uptake and synthesis activities
    • Maeda, T., Sanchez-Torres, V., Wood, T.K., Escherichia coli hydrogenase 3 is a reversible enzyme possessing hydrogen uptake and synthesis activities. Applied Microbiology and Biotechnology 76 (2007), 1035–1042.
    • (2007) Applied Microbiology and Biotechnology , vol.76 , pp. 1035-1042
    • Maeda, T.1    Sanchez-Torres, V.2    Wood, T.K.3
  • 138
    • 77953564075 scopus 로고    scopus 로고
    • Metabolic engineering to enhance bacterial hydrogen production
    • Maeda, T., Sanchez-Torres, V., Wood, T.K., Metabolic engineering to enhance bacterial hydrogen production. Microbial Biotechnology 1 (2008), 30–39.
    • (2008) Microbial Biotechnology , vol.1 , pp. 30-39
    • Maeda, T.1    Sanchez-Torres, V.2    Wood, T.K.3
  • 141
    • 0029901484 scopus 로고    scopus 로고
    • Analysis of the hydA locus of Escherichia coli: Two genes (hydN and hypF) involved in formate and hydrogen metabolism
    • Maier, T., Binder, U., Böck, A., Analysis of the hydA locus of Escherichia coli: Two genes (hydN and hypF) involved in formate and hydrogen metabolism. Archives of Microbiology 165 (1996), 333–341.
    • (1996) Archives of Microbiology , vol.165 , pp. 333-341
    • Maier, T.1    Binder, U.2    Böck, A.3
  • 142
    • 0029757989 scopus 로고    scopus 로고
    • Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form
    • Maier, T., Böck, A., Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form. Biochemistry 35 (1996), 10089–10093.
    • (1996) Biochemistry , vol.35 , pp. 10089-10093
    • Maier, T.1    Böck, A.2
  • 143
    • 0027450599 scopus 로고
    • The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier, T., Jacobi, A., Sauter, M., Böck, A., The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein. Journal of Bacteriology 175 (1993), 630–635.
    • (1993) Journal of Bacteriology , vol.175 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Böck, A.4
  • 144
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier, T., Lottspeich, F., Böck, A., GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli. European Journal of Biochemistry 230 (1995), 133–138.
    • (1995) European Journal of Biochemistry , vol.230 , pp. 133-138
    • Maier, T.1    Lottspeich, F.2    Böck, A.3
  • 145
    • 26444605816 scopus 로고    scopus 로고
    • Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae
    • Manyani, H., Rey, L., Palacios, J.M., Imperial, J., Ruiz-Argueso, T., Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae. Journal of Bacteriology 187 (2005), 7018–7026.
    • (2005) Journal of Bacteriology , vol.187 , pp. 7018-7026
    • Manyani, H.1    Rey, L.2    Palacios, J.M.3    Imperial, J.4    Ruiz-Argueso, T.5
  • 147
    • 0038349356 scopus 로고    scopus 로고
    • Regulatory network of acid resistance genes in Escherichia coli
    • Masuda, N., Church, G.M., Regulatory network of acid resistance genes in Escherichia coli. Molecular Microbiology 48 (2003), 699–712.
    • (2003) Molecular Microbiology , vol.48 , pp. 699-712
    • Masuda, N.1    Church, G.M.2
  • 148
    • 84943197950 scopus 로고    scopus 로고
    • Dissection and engineering of the Escherichia coli formate hydrogenlyase complex
    • McDowall, J.S., Hjersing, M.C., Palmer, T., Sargent, F., Dissection and engineering of the Escherichia coli formate hydrogenlyase complex. FEBS Letters 589 (2015), 3141–3147.
    • (2015) FEBS Letters , vol.589 , pp. 3141-3147
    • McDowall, J.S.1    Hjersing, M.C.2    Palmer, T.3    Sargent, F.4
  • 152
    • 0028308306 scopus 로고
    • Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2
    • Menon, N.K., Chatelus, C.Y., Dervartanian, M., Wendt, J.C., Shanmugam, K.T., Peck, H.D. Jr., et al. Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2. Journal of Bacteriology 176 (1994), 4416–4423.
    • (1994) Journal of Bacteriology , vol.176 , pp. 4416-4423
    • Menon, N.K.1    Chatelus, C.Y.2    Dervartanian, M.3    Wendt, J.C.4    Shanmugam, K.T.5    Peck, H.D.6
  • 153
    • 0025366313 scopus 로고
    • Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames
    • Menon, N.K., Robbins, J., Peck, H.D. Jr., Chatelus, C.Y., Choi, E.S., Przybyla, A.E., Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. Journal of Bacteriology 172 (1990), 1969–1977.
    • (1990) Journal of Bacteriology , vol.172 , pp. 1969-1977
    • Menon, N.K.1    Robbins, J.2    Peck, H.D.3    Chatelus, C.Y.4    Choi, E.S.5    Przybyla, A.E.6
  • 154
    • 0025914936 scopus 로고
    • Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1
    • Menon, N.K., Robbins, J., Wendt, J.C., Shanmugam, K.T., Przybyla, A.E., Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1. Journal of Bacteriology 173 (1991), 4851–4861.
    • (1991) Journal of Bacteriology , vol.173 , pp. 4851-4861
    • Menon, N.K.1    Robbins, J.2    Wendt, J.C.3    Shanmugam, K.T.4    Przybyla, A.E.5
  • 155
    • 0242721758 scopus 로고    scopus 로고
    • FNR-mediated regulation of hyp expression in Escherichia coli
    • Messenger, S.L., Green, J., FNR-mediated regulation of hyp expression in Escherichia coli. FEMS Microbiology Letters 228 (2003), 81–86.
    • (2003) FEMS Microbiology Letters , vol.228 , pp. 81-86
    • Messenger, S.L.1    Green, J.2
  • 157
    • 79961032041 scopus 로고    scopus 로고
    • The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits
    • Moparthi, V.K., Hagerhall, C., The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits. Journal of Molecular Evolution 72 (2011), 484–497.
    • (2011) Journal of Molecular Evolution , vol.72 , pp. 484-497
    • Moparthi, V.K.1    Hagerhall, C.2
  • 158
    • 84896967315 scopus 로고    scopus 로고
    • Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer
    • Murphy, B.J., Sargent, F., Armstrong, F.A., Transforming an oxygen-tolerant [NiFe] uptake hydrogenase into a proficient, reversible hydrogen producer. Energy & Environmental Science 7 (2014), 1426–1433.
    • (2014) Energy & Environmental Science , vol.7 , pp. 1426-1433
    • Murphy, B.J.1    Sargent, F.2    Armstrong, F.A.3
  • 159
    • 61349134073 scopus 로고    scopus 로고
    • Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe–S cluster ligation
    • Nesbit, A.D., Giel, J.L., Rose, J.C., Kiley, P.J., Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe–S cluster ligation. Journal of Molecular Biology 387 (2009), 28–41.
    • (2009) Journal of Molecular Biology , vol.387 , pp. 28-41
    • Nesbit, A.D.1    Giel, J.L.2    Rose, J.C.3    Kiley, P.J.4
  • 160
    • 72449155029 scopus 로고    scopus 로고
    • Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge
    • Nitschke, W., Russell, M.J., Hydrothermal focusing of chemical and chemiosmotic energy, supported by delivery of catalytic Fe, Ni, Mo/W, Co, S and Se, forced life to emerge. Journal of Molecular Evolution 69 (2009), 481–496.
    • (2009) Journal of Molecular Evolution , vol.69 , pp. 481-496
    • Nitschke, W.1    Russell, M.J.2
  • 161
    • 0026646678 scopus 로고
    • Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein
    • Niviere, V., Wong, S.L., Voordouw, G., Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein. Journal of General Microbiology 138 (1992), 2173–2183.
    • (1992) Journal of General Microbiology , vol.138 , pp. 2173-2183
    • Niviere, V.1    Wong, S.L.2    Voordouw, G.3
  • 162
    • 84928538572 scopus 로고    scopus 로고
    • Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase
    • Ogata, H., Nishikawa, K., Lubitz, W., Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase. Nature 520 (2015), 571–574.
    • (2015) Nature , vol.520 , pp. 571-574
    • Ogata, H.1    Nishikawa, K.2    Lubitz, W.3
  • 163
    • 78149416793 scopus 로고    scopus 로고
    • Towards an integrated system for bio-energy: Hydrogen production by Escherichia coli and use of palladium-coated waste cells for electricity generation in a fuel cell
    • Orozco, R.L., Redwood, M.D., Yong, P., Caldelari, I., Sargent, F., Macaskie, L.E., Towards an integrated system for bio-energy: Hydrogen production by Escherichia coli and use of palladium-coated waste cells for electricity generation in a fuel cell. Biotechnology Letters 32 (2010), 1837–1845.
    • (2010) Biotechnology Letters , vol.32 , pp. 1837-1845
    • Orozco, R.L.1    Redwood, M.D.2    Yong, P.3    Caldelari, I.4    Sargent, F.5    Macaskie, L.E.6
  • 164
    • 84926221250 scopus 로고    scopus 로고
    • Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the proteobacteria
    • Outten, W.F., Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the proteobacteria. Biochimica et Biophysica Acta 1853 (2015), 1464–1469.
    • (2015) Biochimica et Biophysica Acta , vol.1853 , pp. 1464-1469
    • Outten, W.F.1
  • 165
    • 84862501228 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) protein export pathway
    • Palmer, T., Berks, B.C., The twin-arginine translocation (Tat) protein export pathway. Nature Reviews Microbiology 10 (2012), 483–496.
    • (2012) Nature Reviews Microbiology , vol.10 , pp. 483-496
    • Palmer, T.1    Berks, B.C.2
  • 167
    • 57249113692 scopus 로고    scopus 로고
    • Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif
    • Parish, D., Benach, J., Liu, G., Singarapu, K.K., Xiao, R., Acton, T., et al. Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif. Journal of Structural and Functional Genomics 9 (2008), 41–49.
    • (2008) Journal of Structural and Functional Genomics , vol.9 , pp. 41-49
    • Parish, D.1    Benach, J.2    Liu, G.3    Singarapu, K.K.4    Xiao, R.5    Acton, T.6
  • 170
    • 33747640530 scopus 로고    scopus 로고
    • Inactivation of the Escherichia coli K-12 twin-arginine translocation system promotes increased hydrogen production
    • Penfold, D.W., Sargent, F., Macaskie, L.E., Inactivation of the Escherichia coli K-12 twin-arginine translocation system promotes increased hydrogen production. FEMS Microbiology Letters 262 (2006), 135–137.
    • (2006) FEMS Microbiology Letters , vol.262 , pp. 135-137
    • Penfold, D.W.1    Sargent, F.2    Macaskie, L.E.3
  • 172
    • 82955193806 scopus 로고    scopus 로고
    • Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites
    • Petkun, S., Shi, R., Li, Y., Asinas, A., Munger, C., Zhang, L., et al. Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites. Structure 19 (2011), 1773–1783.
    • (2011) Structure , vol.19 , pp. 1773-1783
    • Petkun, S.1    Shi, R.2    Li, Y.3    Asinas, A.4    Munger, C.5    Zhang, L.6
  • 173
    • 77956411916 scopus 로고    scopus 로고
    • Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli
    • Phillips, C.M., Schreiter, E.R., Stultz, C.M., Drennan, C.L., Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli. Biochemistry 49 (2010), 7830–7838.
    • (2010) Biochemistry , vol.49 , pp. 7830-7838
    • Phillips, C.M.1    Schreiter, E.R.2    Stultz, C.M.3    Drennan, C.L.4
  • 174
    • 79961064482 scopus 로고    scopus 로고
    • Metabolic deficiences revealed in the biotechnologically important model bacterium Escherichia coli BL21(DE3)
    • Pinske, C., Bonn, M., Kruger, S., Lindenstrauss, U., Sawers, R.G., Metabolic deficiences revealed in the biotechnologically important model bacterium Escherichia coli BL21(DE3). PLoS ONE, 6, 2011, e22830.
    • (2011) PLoS ONE , vol.6 , pp. e22830
    • Pinske, C.1    Bonn, M.2    Kruger, S.3    Lindenstrauss, U.4    Sawers, R.G.5
  • 176
    • 84857408142 scopus 로고    scopus 로고
    • Delivery of iron–sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA
    • Pinske, C., Sawers, R.G., Delivery of iron–sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA. PLoS ONE, 7, 2012, e31755.
    • (2012) PLoS ONE , vol.7 , pp. e31755
    • Pinske, C.1    Sawers, R.G.2
  • 177
    • 84896768069 scopus 로고    scopus 로고
    • The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases
    • Pinske, C., Sawers, R.G., The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases. Biomolecular Concepts 5 (2014), 55–70.
    • (2014) Biomolecular Concepts , vol.5 , pp. 55-70
    • Pinske, C.1    Sawers, R.G.2
  • 179
    • 0022451482 scopus 로고
    • Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris
    • Prickril, B.C., Czechowski, M.H., Przybyla, A.E., Peck, H.D. Jr., LeGall, J., Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris. Journal of Bacteriology 167 (1986), 722–725.
    • (1986) Journal of Bacteriology , vol.167 , pp. 722-725
    • Prickril, B.C.1    Czechowski, M.H.2    Przybyla, A.E.3    Peck, H.D.4    LeGall, J.5
  • 180
    • 84902665564 scopus 로고    scopus 로고
    • Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha
    • Radu, V., Frielingsdorf, S., Evans, S.D., Lenz, O., Jeuken, L.J., Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha. Journal of the American Chemical Society 136 (2014), 8512–8515.
    • (2014) Journal of the American Chemical Society , vol.136 , pp. 8512-8515
    • Radu, V.1    Frielingsdorf, S.2    Evans, S.D.3    Lenz, O.4    Jeuken, L.J.5
  • 182
    • 84877583210 scopus 로고    scopus 로고
    • The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation
    • Ramasamy, S., Abrol, R., Suloway, C.J., Clemons, W.M. Jr., The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation. Structure 21 (2013), 777–788.
    • (2013) Structure , vol.21 , pp. 777-788
    • Ramasamy, S.1    Abrol, R.2    Suloway, C.J.3    Clemons, W.M.4
  • 183
    • 38949209555 scopus 로고    scopus 로고
    • Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF
    • Rangarajan, E.S., Asinas, A., Proteau, A., Munger, C., Baardsnes, J., Iannuzzi, P., et al. Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF. Journal of Bacteriology 190 (2008), 1447–1458.
    • (2008) Journal of Bacteriology , vol.190 , pp. 1447-1458
    • Rangarajan, E.S.1    Asinas, A.2    Proteau, A.3    Munger, C.4    Baardsnes, J.5    Iannuzzi, P.6
  • 184
    • 0346890205 scopus 로고    scopus 로고
    • Taming of a poison: Biosynthesis of the NiFe-hydrogenase cyanide ligands
    • Reissmann, S., Hochleitner, E., Wang, H., Paschos, A., Lottspeich, F., Glass, R.S., et al. Taming of a poison: Biosynthesis of the NiFe-hydrogenase cyanide ligands. Science 299 (2003), 1067–1070.
    • (2003) Science , vol.299 , pp. 1067-1070
    • Reissmann, S.1    Hochleitner, E.2    Wang, H.3    Paschos, A.4    Lottspeich, F.5    Glass, R.S.6
  • 185
    • 11144353842 scopus 로고    scopus 로고
    • Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
    • Relini, A., Torrassa, S., Rolandi, R., Gliozzi, A., Rosano, C., Canale, C., et al. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. Journal of Molecular Biology 338 (2004), 943–957.
    • (2004) Journal of Molecular Biology , vol.338 , pp. 943-957
    • Relini, A.1    Torrassa, S.2    Rolandi, R.3    Gliozzi, A.4    Rosano, C.5    Canale, C.6
  • 186
    • 0032873183 scopus 로고    scopus 로고
    • Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli
    • Richard, D.J., Sawers, G., Sargent, F., McWalter, L., Boxer, D.H., Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli. Microbiology 145 (1999), 2903–2912.
    • (1999) Microbiology , vol.145 , pp. 2903-2912
    • Richard, D.J.1    Sawers, G.2    Sargent, F.3    McWalter, L.4    Boxer, D.H.5
  • 187
    • 84872956374 scopus 로고    scopus 로고
    • Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
    • Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., Barras, F., Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity. Biochimica et Biophysica Acta 1827 (2013), 455–469.
    • (2013) Biochimica et Biophysica Acta , vol.1827 , pp. 455-469
    • Roche, B.1    Aussel, L.2    Ezraty, B.3    Mandin, P.4    Py, B.5    Barras, F.6
  • 188
    • 0030603123 scopus 로고    scopus 로고
    • Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli
    • Rodrigue, A., Boxer, D.H., Mandrand-Berthelot, M.A., Wu, L.F., Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli. FEBS Letters 392 (1996), 81–86.
    • (1996) FEBS Letters , vol.392 , pp. 81-86
    • Rodrigue, A.1    Boxer, D.H.2    Mandrand-Berthelot, M.A.3    Wu, L.F.4
  • 189
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway
    • Rodrigue, A., Chanal, A., Beck, K., Muller, M., Wu, L.F., Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. The Journal of Biological Chemistry 274 (1999), 13223–13228.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Muller, M.4    Wu, L.F.5
  • 190
    • 16844370956 scopus 로고    scopus 로고
    • Identification of rcnA (yohM), a nickel and cobalt resistance gene in Escherichia coli
    • Rodrigue, A., Effantin, G., Mandrand-Berthelot, M.A., Identification of rcnA (yohM), a nickel and cobalt resistance gene in Escherichia coli. Journal of Bacteriology 187 (2005), 2912–2916.
    • (2005) Journal of Bacteriology , vol.187 , pp. 2912-2916
    • Rodrigue, A.1    Effantin, G.2    Mandrand-Berthelot, M.A.3
  • 193
    • 84871007356 scopus 로고    scopus 로고
    • Structure of the TatC core of the twin-arginine protein transport system
    • Rollauer, S.E., Tarry, M.J., Graham, J.E., Jaaskelainen, M., Jager, F., Johnson, S., et al. Structure of the TatC core of the twin-arginine protein transport system. Nature 492 (2012), 210–214.
    • (2012) Nature , vol.492 , pp. 210-214
    • Rollauer, S.E.1    Tarry, M.J.2    Graham, J.E.3    Jaaskelainen, M.4    Jager, F.5    Johnson, S.6
  • 194
    • 84880969972 scopus 로고    scopus 로고
    • Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells
    • Rose, P., Frobel, J., Graumann, P.L., Muller, M., Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells. PLoS ONE, 8, 2013, e69488.
    • (2013) PLoS ONE , vol.8 , pp. e69488
    • Rose, P.1    Frobel, J.2    Graumann, P.L.3    Muller, M.4
  • 195
    • 0027323851 scopus 로고
    • The hmc operon of Desulfovibrio vulgaris subsp. Hildenborough encodes a potential transmembrane redox protein complex
    • Rossi, M., Pollock, W.B., Reij, M.W., Keon, R.G., Fu, R., Voordouw, G., The hmc operon of Desulfovibrio vulgaris subsp. Hildenborough encodes a potential transmembrane redox protein complex. Journal of Bacteriology 175 (1993), 4699–4711.
    • (1993) Journal of Bacteriology , vol.175 , pp. 4699-4711
    • Rossi, M.1    Pollock, W.B.2    Reij, M.W.3    Keon, R.G.4    Fu, R.5    Voordouw, G.6
  • 196
    • 0028832110 scopus 로고
    • Characterisation of a protease from Escherichia coli involved in hydrogenase maturation
    • Rossmann, R., Maier, T., Lottspeich, F., Böck, A., Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. European Journal of Biochemistry 227 (1995), 545–550.
    • (1995) European Journal of Biochemistry , vol.227 , pp. 545-550
    • Rossmann, R.1    Maier, T.2    Lottspeich, F.3    Böck, A.4
  • 197
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • Rossmann, R., Sauter, M., Lottspeich, F., Böck, A., Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. European Journal of Biochemistry 220 (1994), 377–384.
    • (1994) European Journal of Biochemistry , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Böck, A.4
  • 198
    • 0035088582 scopus 로고    scopus 로고
    • The diheme cytochrome b subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI): Structure, function, and interaction with quinols
    • Rothery, R.A., Blasco, F., Magalon, A., Weiner, J.H., The diheme cytochrome b subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI): Structure, function, and interaction with quinols. Journal of Molecular Microbiology and Biotechnology 3 (2001), 273–283.
    • (2001) Journal of Molecular Microbiology and Biotechnology , vol.3 , pp. 273-283
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Weiner, J.H.4
  • 200
    • 0004136246 scopus 로고    scopus 로고
    • Molecular cloning: A laboratory manual
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • Sambrook, J., Russell, D.W., Molecular cloning: A laboratory manual. 2001, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 201
    • 69449088007 scopus 로고    scopus 로고
    • Protein engineering of the transcriptional activator FhlA To enhance hydrogen production in Escherichia coli
    • Sanchez-Torres, V., Maeda, T., Wood, T.K., Protein engineering of the transcriptional activator FhlA To enhance hydrogen production in Escherichia coli. Applied and Environmental Microbiology 75 (2009), 5639–5646.
    • (2009) Applied and Environmental Microbiology , vol.75 , pp. 5639-5646
    • Sanchez-Torres, V.1    Maeda, T.2    Wood, T.K.3
  • 202
    • 33947370894 scopus 로고    scopus 로고
    • Constructing the wonders of the bacterial world: Biosynthesis of complex enzymes
    • Sargent, F., Constructing the wonders of the bacterial world: Biosynthesis of complex enzymes. Microbiology 153 (2007), 633–651.
    • (2007) Microbiology , vol.153 , pp. 633-651
    • Sargent, F.1
  • 203
    • 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, S.P., Rugman, P.A., Palmer, T., Boxer, D.H., 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. European Journal of Biochemistry 255 (1998), 746–754.
    • (1998) European Journal of Biochemistry , vol.255 , pp. 746-754
    • Sargent, F.1    Ballantine, S.P.2    Rugman, P.A.3    Palmer, T.4    Boxer, D.H.5
  • 204
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., Bogsch, E.G., Stanley, N.R., Wexler, M., Robinson, C., Berks, B.C., et al. Overlapping functions of components of a bacterial Sec-independent protein export pathway. The EMBO Journal 17 (1998), 3640–3650.
    • (1998) The EMBO Journal , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6
  • 205
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent, F., Stanley, N.R., Berks, B.C., Palmer, T., Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. The Journal of Biological Chemistry 274 (1999), 36073–36082.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 36073-36082
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 206
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • Sauter, M., Bohm, R., Böck, A., Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Molecular Microbiology 6 (1992), 1523–1532.
    • (1992) Molecular Microbiology , vol.6 , pp. 1523-1532
    • Sauter, M.1    Bohm, R.2    Böck, A.3
  • 207
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G., The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66 (1994), 57–88.
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 208
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R.G., Ballantine, S.P., Boxer, D.H., Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme. Journal of Bacteriology 164 (1985), 1324–1331.
    • (1985) Journal of Bacteriology , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 209
    • 0023049475 scopus 로고
    • Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12
    • Sawers, R.G., Boxer, D.H., Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grown Escherichia coli K12. European Journal of Biochemistry 156 (1986), 265–275.
    • (1986) European Journal of Biochemistry , vol.156 , pp. 265-275
    • Sawers, R.G.1    Boxer, D.H.2
  • 210
    • 0031866036 scopus 로고    scopus 로고
    • A glycyl radical solution: Oxygen-dependent interconversion of pyruvate formate-lyase
    • Sawers, G., Watson, G., A glycyl radical solution: Oxygen-dependent interconversion of pyruvate formate-lyase. Molecular Microbiology 29 (1998), 945–954.
    • (1998) Molecular Microbiology , vol.29 , pp. 945-954
    • Sawers, G.1    Watson, G.2
  • 211
    • 0025031657 scopus 로고
    • Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli
    • Schlensog, V., Böck, A., Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli. Molecular Microbiology 4 (1990), 1319–1327.
    • (1990) Molecular Microbiology , vol.4 , pp. 1319-1327
    • Schlensog, V.1    Böck, A.2
  • 212
    • 0028038237 scopus 로고
    • Purification and DNA-binding properties of FHLA, the transcriptional activator of the formate hydrogenlyase system from Escherichia coli
    • Schlensog, V., Lutz, S., Böck, A., Purification and DNA-binding properties of FHLA, the transcriptional activator of the formate hydrogenlyase system from Escherichia coli. The Journal of Biological Chemistry 269 (1994), 19590–19596.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 19590-19596
    • Schlensog, V.1    Lutz, S.2    Böck, A.3
  • 213
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: Variations on a theme
    • Schreiter, E.R., Drennan, C.L., Ribbon-helix-helix transcription factors: Variations on a theme. Nature Reviews Microbiology 5 (2007), 710–720.
    • (2007) Nature Reviews Microbiology , vol.5 , pp. 710-720
    • Schreiter, E.R.1    Drennan, C.L.2
  • 216
    • 34748882510 scopus 로고    scopus 로고
    • Chaperones specific for the membrane-bound [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 membrane-bound [NiFe]-hydrogenase interact with the Tat signal peptide of the small subunit precursor in Ralstonia eutropha H16. Molecular Microbiology 66 (2007), 453–467.
    • (2007) Molecular Microbiology , vol.66 , pp. 453-467
    • Schubert, T.1    Lenz, O.2    Krause, E.3    Volkmer, R.4    Friedrich, B.5
  • 217
    • 0032949461 scopus 로고    scopus 로고
    • Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli in response to molybdenum: ModE-molybdate, a repressor of the modABCD (molybdate transport) operon is a secondary transcriptional activator for the hyc and nar operons
    • Self, W.T., Grunden, A.M., Hasona, A., Shanmugam, K.T., Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli in response to molybdenum: ModE-molybdate, a repressor of the modABCD (molybdate transport) operon is a secondary transcriptional activator for the hyc and nar operons. Microbiology 145 (1999), 41–55.
    • (1999) Microbiology , vol.145 , pp. 41-55
    • Self, W.T.1    Grunden, A.M.2    Hasona, A.3    Shanmugam, K.T.4
  • 218
    • 0347285390 scopus 로고    scopus 로고
    • Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli
    • Self, W.T., Hasona, A., Shanmugam, K.T., Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli. Journal of Bacteriology 186 (2004), 580–587.
    • (2004) Journal of Bacteriology , vol.186 , pp. 580-587
    • Self, W.T.1    Hasona, A.2    Shanmugam, K.T.3
  • 219
    • 66149164338 scopus 로고    scopus 로고
    • Solution structure of the Escherichia coli HybE reveals a novel fold
    • Shao, X., Lu, J., Hu, Y., Xia, B., Jin, C., Solution structure of the Escherichia coli HybE reveals a novel fold. Proteins 75 (2009), 1051–1056.
    • (2009) Proteins , vol.75 , pp. 1051-1056
    • Shao, X.1    Lu, J.2    Hu, Y.3    Xia, B.4    Jin, C.5
  • 220
    • 67349164656 scopus 로고    scopus 로고
    • 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli
    • 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli. Biomolecular NMR Assignments 3 (2009), 129–131.
    • (2009) Biomolecular NMR Assignments , vol.3 , pp. 129-131
    • Shao, X.1    Lu, J.2    Xia, B.3    Jin, C.4
  • 221
    • 34247584487 scopus 로고    scopus 로고
    • NikA binds heme: A new role for an Escherichia coli periplasmic nickel-binding protein
    • Shepherd, M., Heath, M.D., Poole, R.K., NikA binds heme: A new role for an Escherichia coli periplasmic nickel-binding protein. Biochemistry 46 (2007), 5030–5037.
    • (2007) Biochemistry , vol.46 , pp. 5030-5037
    • Shepherd, M.1    Heath, M.D.2    Poole, R.K.3
  • 222
    • 84865239562 scopus 로고    scopus 로고
    • Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases
    • Shomura, Y., Higuchi, Y., Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases. The Journal of Biological Chemistry 287 (2012), 28409–28419.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 28409-28419
    • Shomura, Y.1    Higuchi, Y.2
  • 223
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe–3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Shomura, Y., Yoon, K.S., Nishihara, H., Higuchi, Y., Structural basis for a [4Fe–3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 479 (2011), 253–256.
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 225
    • 49249138553 scopus 로고    scopus 로고
    • Quinone-reactive proteins devoid of haem b form widespread membrane-bound electron transport modules in bacterial respiration
    • Simon, J., Kern, M., Quinone-reactive proteins devoid of haem b form widespread membrane-bound electron transport modules in bacterial respiration. Biochemical Society Transactions 36 (2008), 1011–1016.
    • (2008) Biochemical Society Transactions , vol.36 , pp. 1011-1016
    • Simon, J.1    Kern, M.2
  • 226
    • 56449092797 scopus 로고    scopus 로고
    • The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems
    • Simon, J., van Spanning, R.J., Richardson, D.J., The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochimica et Biophysica Acta 1777 (2008), 1480–1490.
    • (2008) Biochimica et Biophysica Acta , vol.1777 , pp. 1480-1490
    • Simon, J.1    van Spanning, R.J.2    Richardson, D.J.3
  • 227
    • 0036889035 scopus 로고    scopus 로고
    • Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR
    • Skibinski, D.A., Golby, P., Chang, Y.S., Sargent, F., Hoffman, R., Harper, R., et al. Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR. Journal of Bacteriology 184 (2002), 6642–6653.
    • (2002) Journal of Bacteriology , vol.184 , pp. 6642-6653
    • Skibinski, D.A.1    Golby, P.2    Chang, Y.S.3    Sargent, F.4    Hoffman, R.5    Harper, R.6
  • 228
    • 84911894921 scopus 로고    scopus 로고
    • [NiFe]-hydrogenase maturation in vitro: Analysis of the roles of the HybG and HypD accessory proteins1
    • Soboh, B., Lindenstrauss, U., Granich, C., Javed, M., Herzberg, M., Thomas, C., et al. [NiFe]-hydrogenase maturation in vitro: Analysis of the roles of the HybG and HypD accessory proteins1. The Biochemical Journal 464 (2014), 169–177.
    • (2014) The Biochemical Journal , vol.464 , pp. 169-177
    • Soboh, B.1    Lindenstrauss, U.2    Granich, C.3    Javed, M.4    Herzberg, M.5    Thomas, C.6
  • 229
    • 84881475601 scopus 로고    scopus 로고
    • The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins
    • Soboh, B., Stripp, S.T., Bielak, C., Lindenstrauss, U., Braussemann, M., Javaid, M., et al. The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins. FEBS Letters 587 (2013), 2512–2516.
    • (2013) FEBS Letters , vol.587 , pp. 2512-2516
    • Soboh, B.1    Stripp, S.T.2    Bielak, C.3    Lindenstrauss, U.4    Braussemann, M.5    Javaid, M.6
  • 231
    • 3543079953 scopus 로고
    • Hydrogenlyases: Further experiments on the formation of formic hydrogenlyase by Bact. coli
    • Stephenson, M., Stickland, L.H., Hydrogenlyases: Further experiments on the formation of formic hydrogenlyase by Bact. coli. The Biochemical Journal 27 (1933), 1528–1532.
    • (1933) The Biochemical Journal , vol.27 , pp. 1528-1532
    • Stephenson, M.1    Stickland, L.H.2
  • 232
    • 79951590036 scopus 로고    scopus 로고
    • Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli
    • Stourman, N.V., Branch, M.C., Schaab, M.R., Harp, J.M., Ladner, J.E., Armstrong, R.N., Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli. Biochemistry 50 (2011), 1274–1281.
    • (2011) Biochemistry , vol.50 , pp. 1274-1281
    • Stourman, N.V.1    Branch, M.C.2    Schaab, M.R.3    Harp, J.M.4    Ladner, J.E.5    Armstrong, R.N.6
  • 233
    • 84941349045 scopus 로고    scopus 로고
    • Identification of an isothiocyanate on the HypEF complex suggests a route for efficient cyanyl-group channeling during [NiFe]-hydrogenase cofactor generation
    • Stripp, S.T., Lindenstrauss, U., Sawers, R.G., Soboh, B., Identification of an isothiocyanate on the HypEF complex suggests a route for efficient cyanyl-group channeling during [NiFe]-hydrogenase cofactor generation. PLoS ONE, 10, 2015, e0133118.
    • (2015) PLoS ONE , vol.10 , pp. e0133118
    • Stripp, S.T.1    Lindenstrauss, U.2    Sawers, R.G.3    Soboh, B.4
  • 234
    • 84877733038 scopus 로고    scopus 로고
    • HypD is the scaffold protein for Fe-(CN)2CO cofactor assembly in [NiFe]-hydrogenase maturation
    • Stripp, S.T., Soboh, B., Lindenstrauss, U., Braussemann, M., Herzberg, M., Nies, D.H., et al. HypD is the scaffold protein for Fe-(CN)2CO cofactor assembly in [NiFe]-hydrogenase maturation. Biochemistry 52 (2013), 3289–3296.
    • (2013) Biochemistry , vol.52 , pp. 3289-3296
    • Stripp, S.T.1    Soboh, B.2    Lindenstrauss, U.3    Braussemann, M.4    Herzberg, M.5    Nies, D.H.6
  • 235
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W., Moffatt, B.A., Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. Journal of Molecular Biology 189 (1986), 113–130.
    • (1986) Journal of Molecular Biology , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 238
    • 84878954521 scopus 로고    scopus 로고
    • Amyloid-beta oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N
    • Tatini, F., Pugliese, A.M., Traini, C., Niccoli, S., Maraula, G., Ed Dami, T., et al. Amyloid-beta oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N. Neurobiology of Aging 34 (2013), 2100–2109.
    • (2013) Neurobiology of Aging , vol.34 , pp. 2100-2109
    • Tatini, F.1    Pugliese, A.M.2    Traini, C.3    Niccoli, S.4    Maraula, G.5    Ed Dami, T.6
  • 239
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R.K., Jungermann, K., Decker, K., Energy conservation in chemotrophic anaerobic bacteria. Bacteriological Reviews 41 (1977), 100–180.
    • (1977) Bacteriological Reviews , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 240
  • 241
    • 0033961397 scopus 로고    scopus 로고
    • Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli
    • Theodoratou, E., Paschos, A., Mintz, W., Böck, A., Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli. Archives of Microbiology 173 (2000), 110–116.
    • (2000) Archives of Microbiology , vol.173 , pp. 110-116
    • Theodoratou, E.1    Paschos, A.2    Mintz, W.3    Böck, A.4
  • 242
    • 84940421678 scopus 로고    scopus 로고
    • Coordination of synthesis and assembly of a modular membrane-associated [NiFe]-hydrogenase is determined by cleavage of the C-terminal peptide
    • Thomas, C., Muhr, E., Sawers, R.G., Coordination of synthesis and assembly of a modular membrane-associated [NiFe]-hydrogenase is determined by cleavage of the C-terminal peptide. Journal of Bacteriology 197 (2015), 2989–2998.
    • (2015) Journal of Bacteriology , vol.197 , pp. 2989-2998
    • Thomas, C.1    Muhr, E.2    Sawers, R.G.3
  • 243
    • 84856907383 scopus 로고    scopus 로고
    • A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli
    • Thome, R., Gust, A., Toci, R., Mendel, R., Bittner, F., Magalon, A., et al. A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli. The Journal of Biological Chemistry 287 (2012), 4671–4678.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 4671-4678
    • Thome, R.1    Gust, A.2    Toci, R.3    Mendel, R.4    Bittner, F.5    Magalon, A.6
  • 244
    • 84872371364 scopus 로고    scopus 로고
    • Quantification of flagellar motor stator dynamics through in vivo proton-motive force control
    • Tipping, M.J., Steel, B.C., Delalez, N.J., Berry, R.M., Armitage, J.P., Quantification of flagellar motor stator dynamics through in vivo proton-motive force control. Molecular Microbiology 87 (2013), 338–347.
    • (2013) Molecular Microbiology , vol.87 , pp. 338-347
    • Tipping, M.J.1    Steel, B.C.2    Delalez, N.J.3    Berry, R.M.4    Armitage, J.P.5
  • 246
    • 84900808181 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli to enhance hydrogen production from glycerol
    • Tran, K.T., Maeda, T., Wood, T.K., Metabolic engineering of Escherichia coli to enhance hydrogen production from glycerol. Applied Microbiology and Biotechnology 98 (2014), 4757–4770.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 4757-4770
    • Tran, K.T.1    Maeda, T.2    Wood, T.K.3
  • 247
    • 84878632648 scopus 로고    scopus 로고
    • Hydrogenase activity and proton-motive force generation by Escherichia coli during glycerol fermentation
    • Trchounian, K., Blbulyan, S., Trchounian, A., Hydrogenase activity and proton-motive force generation by Escherichia coli during glycerol fermentation. Journal of Bioenergetics and Biomembranes 45 (2013), 253–260.
    • (2013) Journal of Bioenergetics and Biomembranes , vol.45 , pp. 253-260
    • Trchounian, K.1    Blbulyan, S.2    Trchounian, A.3
  • 248
    • 84857036850 scopus 로고    scopus 로고
    • 1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases 1 and 2 during glucose and glycerol fermentation at high and low pH in Escherichia coli
    • 1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases 1 and 2 during glucose and glycerol fermentation at high and low pH in Escherichia coli. Journal of Bioenergetics and Biomembranes 43 (2011), 645–650.
    • (2011) Journal of Bioenergetics and Biomembranes , vol.43 , pp. 645-650
    • Trchounian, K.1    Pinske, C.2    Sawers, R.G.3    Trchounian, A.4
  • 251
    • 40849141029 scopus 로고    scopus 로고
    • Hydrogen production by continuous cultures of Escherchia coli under different nutrient regimes
    • Turcot, J., Bisaillon, A., Hallenbeck, P.C., Hydrogen production by continuous cultures of Escherchia coli under different nutrient regimes. International Journal of Hydrogen Energy 33 (2008), 1465–1470.
    • (2008) International Journal of Hydrogen Energy , vol.33 , pp. 1465-1470
    • Turcot, J.1    Bisaillon, A.2    Hallenbeck, P.C.3
  • 252
    • 84933533873 scopus 로고    scopus 로고
    • Identification of enhanced hydrogen and ethanol Escherichia coli producer strains in a glycerol-based medium by screening in single-knock out mutant collections
    • Valle, A., Cabrera, G., Cantero, D., Bolivar, J., Identification of enhanced hydrogen and ethanol Escherichia coli producer strains in a glycerol-based medium by screening in single-knock out mutant collections. Microbial Cell Factories, 14, 2015, 93.
    • (2015) Microbial Cell Factories , vol.14 , pp. 93
    • Valle, A.1    Cabrera, G.2    Cantero, D.3    Bolivar, J.4
  • 253
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais, P.M., Billoud, B., Occurrence, classification, and biological function of hydrogenases: An overview. Chemical Reviews 107 (2007), 4206–4272.
    • (2007) Chemical Reviews , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 255
    • 84927556319 scopus 로고    scopus 로고
    • Formate hydrogen lyase mediates stationary-phase deacidification and increases survival during sugar fermentation in acetoin-producing enterobacteria
    • Vivijs, B., Haberbeck, L.U., Baiye Mfortaw Mbong, V., Bernaerts, K., Geeraerd, A.H., Aertsen, A., et al. Formate hydrogen lyase mediates stationary-phase deacidification and increases survival during sugar fermentation in acetoin-producing enterobacteria. Frontiers in Microbiology, 6, 2015, 150.
    • (2015) Frontiers in Microbiology , vol.6 , pp. 150
    • Vivijs, B.1    Haberbeck, L.U.2    Baiye Mfortaw Mbong, V.3    Bernaerts, K.4    Geeraerd, A.H.5    Aertsen, A.6
  • 259
    • 77955336661 scopus 로고    scopus 로고
    • Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst
    • Wait, A.F., Parkin, A., Morley, G.M., dos Santos, L., Armstrong, F.A., Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst. Journal of Physical Chemistry C 114 (2010), 12003–12009.
    • (2010) Journal of Physical Chemistry 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
  • 260
    • 70849106457 scopus 로고    scopus 로고
    • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel
    • Wang, Y., Huang, Y., Wang, J., Cheng, C., Huang, W., Lu, P., et al. Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel. Nature 462 (2009), 467–472.
    • (2009) Nature , vol.462 , pp. 467-472
    • Wang, Y.1    Huang, Y.2    Wang, J.3    Cheng, C.4    Huang, W.5    Lu, P.6
  • 262
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: Insights into cyanation reaction by thiol redox signaling
    • Watanabe, S., Matsumi, R., Arai, T., Atomi, H., Imanaka, T., Miki, K., Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: Insights into cyanation reaction by thiol redox signaling. Molecular Cell 27 (2007), 29–40.
    • (2007) Molecular Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 263
    • 84870548822 scopus 로고    scopus 로고
    • Crystal structures of the HypCD complex and the HypCDE ternary complex: Transient intermediate complexes during [NiFe] hydrogenase maturation
    • Watanabe, S., Matsumi, R., Atomi, H., Imanaka, T., Miki, K., Crystal structures of the HypCD complex and the HypCDE ternary complex: Transient intermediate complexes during [NiFe] hydrogenase maturation. Structure 20 (2012), 2124–2137.
    • (2012) Structure , vol.20 , pp. 2124-2137
    • Watanabe, S.1    Matsumi, R.2    Atomi, H.3    Imanaka, T.4    Miki, K.5
  • 264
    • 84869456872 scopus 로고    scopus 로고
    • Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
    • Watanabe, S., Sasaki, D., Tominaga, T., Miki, K., Structural basis of [NiFe] hydrogenase maturation by Hyp proteins. Biological Chemistry 393 (2012), 1089–1100.
    • (2012) Biological Chemistry , vol.393 , pp. 1089-1100
    • Watanabe, S.1    Sasaki, D.2    Tominaga, T.3    Miki, K.4
  • 265
    • 0022632813 scopus 로고
    • Pleiotropic hydrogenase mutants of Escherichia coli K12: Growth in the presence of nickel can restore hydrogenase activity
    • Waugh, R., Boxer, D.H., Pleiotropic hydrogenase mutants of Escherichia coli K12: Growth in the presence of nickel can restore hydrogenase activity. Biochimie 68 (1986), 157–166.
    • (1986) Biochimie , vol.68 , pp. 157-166
    • Waugh, R.1    Boxer, D.H.2
  • 266
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J.H., Bilous, P.T., Shaw, G.M., Lubitz, S.P., Frost, L., Thomas, G.H., et al. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93 (1998), 93–101.
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6
  • 267
    • 0009741233 scopus 로고
    • Hydrogenlyases: The synthesis of formic acid by bacteria
    • Woods, D.D., Hydrogenlyases: The synthesis of formic acid by bacteria. The Biochemical Journal 30 (1936), 515–527.
    • (1936) The Biochemical Journal , vol.30 , pp. 515-527
    • Woods, D.D.1
  • 268
    • 0034099642 scopus 로고    scopus 로고
    • Membrane targeting and translocation of bacterial hydrogenases
    • Wu, L.F., Chanal, A., Rodrigue, A., Membrane targeting and translocation of bacterial hydrogenases. Archives of Microbiology 173 (2000), 319–324.
    • (2000) Archives of Microbiology , vol.173 , pp. 319-324
    • Wu, L.F.1    Chanal, A.2    Rodrigue, A.3
  • 269
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • Wu, L.F., Mandrand, M.A., Microbial hydrogenases: Primary structure, classification, signatures and phylogeny. FEMS Microbiology Reviews 10 (1993), 243–269.
    • (1993) FEMS Microbiology Reviews , vol.10 , pp. 243-269
    • Wu, L.F.1    Mandrand, M.A.2
  • 270
    • 0022639247 scopus 로고
    • Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity
    • Wu, L.F., Mandrand-Berthelot, M.A., Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity. Biochimie 68 (1986), 167–179.
    • (1986) Biochimie , vol.68 , pp. 167-179
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 271
    • 0024836127 scopus 로고
    • Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli
    • Wu, L.F., Mandrand-Berthelot, M.A., Waugh, R., Edmonds, C.J., Holt, S.E., Boxer, D.H., Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli. Molecular Microbiology 3 (1989), 1709–1718.
    • (1989) Molecular Microbiology , vol.3 , pp. 1709-1718
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2    Waugh, R.3    Edmonds, C.J.4    Holt, S.E.5    Boxer, D.H.6
  • 272
    • 0025984451 scopus 로고
    • The hydC region contains a multi-cistronic operon (nik) involved in nickel transport in Escherichia coli
    • Wu, L.F., Navarro, C., Mandrand-Berthelot, M.A., The hydC region contains a multi-cistronic operon (nik) involved in nickel transport in Escherichia coli. Gene 107 (1991), 37–42.
    • (1991) Gene , vol.107 , pp. 37-42
    • Wu, L.F.1    Navarro, C.2    Mandrand-Berthelot, M.A.3
  • 275
    • 33947536028 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: Implications for mechanism of the [NiFe] hydrogenase maturation
    • Yang, F., Hu, W., Xu, H., Li, C., Xia, B., Jin, C., Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: Implications for mechanism of the [NiFe] hydrogenase maturation. The Journal of Biological Chemistry 282 (2007), 3856–3863.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 3856-3863
    • Yang, F.1    Hu, W.2    Xu, H.3    Li, C.4    Xia, B.5    Jin, C.6
  • 276
    • 32044471535 scopus 로고    scopus 로고
    • Enhanced hydrogen production from formic acid by formate hydrogen lyase-overexpressing Escherichia coli strains
    • Yoshida, A., Nishimura, T., Kawaguchi, H., Inui, M., Yukawa, H., Enhanced hydrogen production from formic acid by formate hydrogen lyase-overexpressing Escherichia coli strains. Applied and Environmental Microbiology 71 (2005), 6762–6768.
    • (2005) Applied and Environmental Microbiology , vol.71 , pp. 6762-6768
    • Yoshida, A.1    Nishimura, T.2    Kawaguchi, H.3    Inui, M.4    Yukawa, H.5
  • 278
    • 33847279870 scopus 로고    scopus 로고
    • Efficient induction of formate hydrogen lyase of aerobically grown Escherichia coli in a three-step biohydrogen production process
    • Yoshida, A., Nishimura, T., Kawaguchi, H., Inui, M., Yukawa, H., Efficient induction of formate hydrogen lyase of aerobically grown Escherichia coli in a three-step biohydrogen production process. Applied Microbiology and Biotechnology 74 (2007), 754–760.
    • (2007) Applied Microbiology and Biotechnology , vol.74 , pp. 754-760
    • Yoshida, A.1    Nishimura, T.2    Kawaguchi, H.3    Inui, M.4    Yukawa, H.5
  • 279
    • 84905454613 scopus 로고    scopus 로고
    • Structural basis for TatA oligomerization: An NMR study of Escherichia coli TatA dimeric structure
    • Zhang, Y., Hu, Y., Li, H., Jin, C., Structural basis for TatA oligomerization: An NMR study of Escherichia coli TatA dimeric structure. PLoS ONE, 9, 2014, e103157.
    • (2014) PLoS ONE , vol.9 , pp. e103157
    • Zhang, Y.1    Hu, Y.2    Li, H.3    Jin, C.4
  • 280
    • 84899038051 scopus 로고    scopus 로고
    • Solution structure of the TatB component of the twin-arginine translocation system
    • Zhang, Y., Wang, L., Hu, Y., Jin, C., Solution structure of the TatB component of the twin-arginine translocation system. Biochimica et Biophysica Acta 1838 (2014), 1881–1888.
    • (2014) Biochimica et Biophysica Acta , vol.1838 , pp. 1881-1888
    • Zhang, Y.1    Wang, L.2    Hu, Y.3    Jin, C.4
  • 282
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli
    • Zinoni, F., Birkmann, A., Stadtman, T.C., Böck, A., Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 83 (1986), 4650–4654.
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Böck, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.