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Volumn 40, Issue 30, 2015, Pages 9113-9124

Development of a synthetic pathway to convert glucose to hydrogen using cell free extracts

Author keywords

Biohydrogen; Cell free metabolic engineering; Ferredoxin; Ferredoxin NADP+ reductase; Hydrogenase; Synthetic enzyme pathway

Indexed keywords

CELLS; COST EFFECTIVENESS; COST ENGINEERING; CYTOLOGY; ENZYMES; FOSSIL FUELS; GLUCOSE; HYDROGEN; METABOLIC ENGINEERING;

EID: 84937516584     PISSN: 03603199     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijhydene.2015.05.121     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 78651403921 scopus 로고    scopus 로고
    • The hydrogen issue
    • N. Armaroli, and V. Balzani The hydrogen issue ChemSusChem 4 1 2011 21 36
    • (2011) ChemSusChem , vol.4 , Issue.1 , pp. 21-36
    • Armaroli, N.1    Balzani, V.2
  • 2
    • 77953912128 scopus 로고    scopus 로고
    • Hydrogen from biomass - Present scenario and future prospects
    • H. Balat, and E. KIrtay Hydrogen from biomass - present scenario and future prospects Int J Hydrogen Energy 35 14 2010 7416 7426
    • (2010) Int J Hydrogen Energy , vol.35 , Issue.14 , pp. 7416-7426
    • Balat, H.1    Kirtay, E.2
  • 3
    • 0032108850 scopus 로고    scopus 로고
    • An overview of industrial uses of hydrogen
    • R. Ramachandran, and R. Menon An overview of industrial uses of hydrogen Int J Hydrogen Energy 23 7 1998 593 598
    • (1998) Int J Hydrogen Energy , vol.23 , Issue.7 , pp. 593-598
    • Ramachandran, R.1    Menon, R.2
  • 4
    • 84855211682 scopus 로고    scopus 로고
    • U.S. Department of Energy R.D. Perlack and B.J. Stokes (Leads), ORNL/TM-2011/224 Oak Ridge National Laboratory Oak Ridge, TN
    • U.S. Department of Energy U.S. billion-ton update: biomass supply for a bioenergy and bioproducts industry R.D. Perlack and B.J. Stokes (Leads), ORNL/TM-2011/224 2011 Oak Ridge National Laboratory Oak Ridge, TN 227
    • (2011) U.S. Billion-ton Update: Biomass Supply for A Bioenergy and Bioproducts Industry , pp. 227
  • 5
    • 53049107739 scopus 로고    scopus 로고
    • Biomass-based energy fuel through biochemical routes: A review
    • R.C. Saxena, D.K. Adhikari, and H.B. Goyal Biomass-based energy fuel through biochemical routes: a review Renew Sustain Energy Rev 13 1 2009 167 178
    • (2009) Renew Sustain Energy Rev , vol.13 , Issue.1 , pp. 167-178
    • Saxena, R.C.1    Adhikari, D.K.2    Goyal, H.B.3
  • 7
    • 79958754584 scopus 로고    scopus 로고
    • Engineering a non-native hydrogen production pathway into Escherichia coli via a cyanobacterial [NiFe] hydrogenase
    • M.A. Wells, J. Mercer, R.A. Mott, A.G. Pereira-Medrano, A.M. Burja, H. Radianingtyas, and et al. Engineering a non-native hydrogen production pathway into Escherichia coli via a cyanobacterial [NiFe] hydrogenase Metab Eng 13 4 2011 445 453
    • (2011) Metab Eng , vol.13 , Issue.4 , pp. 445-453
    • Wells, M.A.1    Mercer, J.2    Mott, R.A.3    Pereira-Medrano, A.G.4    Burja, A.M.5    Radianingtyas, H.6
  • 8
    • 83055176726 scopus 로고    scopus 로고
    • Fermentative hydrogen production in recombinant Escherichia coli harboring a [FeFe]-hydrogenase gene isolated from Clostridium butyricum
    • S. Subudhi, and B. Lal Fermentative hydrogen production in recombinant Escherichia coli harboring a [FeFe]-hydrogenase gene isolated from Clostridium butyricum Int J Hydrogen Energy 36 21 2011 14024 14030
    • (2011) Int J Hydrogen Energy , vol.36 , Issue.21 , pp. 14024-14030
    • Subudhi, S.1    Lal, B.2
  • 9
    • 33750328012 scopus 로고    scopus 로고
    • Enhanced hydrogen production from glucose using ldh- and frd-inactivated Escherichia coli strains
    • A. Yoshida, T. Nishimura, H. Kawaguchi, M. Inui, and H. Yukawa Enhanced hydrogen production from glucose using ldh- and frd-inactivated Escherichia coli strains Appl Microbiol Biotechnol 73 1 2006 67 72
    • (2006) Appl Microbiol Biotechnol , vol.73 , Issue.1 , pp. 67-72
    • Yoshida, A.1    Nishimura, T.2    Kawaguchi, H.3    Inui, M.4    Yukawa, H.5
  • 10
    • 0034729696 scopus 로고    scopus 로고
    • Biotechnology: Enzymatic production of biohydrogen
    • J. Woodward, M. Orr, K. Cordray, and E. Greenbaum Biotechnology: enzymatic production of biohydrogen Nature 405 2000 1014 1015
    • (2000) Nature , vol.405 , pp. 1014-1015
    • Woodward, J.1    Orr, M.2    Cordray, K.3    Greenbaum, E.4
  • 11
    • 55849139751 scopus 로고    scopus 로고
    • High-yield hydrogen production from starch and water by a synthetic enzymatic pathway
    • Y.H.P. Zhang, B.R. Evans, J.R. Mielenz, R.C. Hopkins, and M.W.W. Adams High-yield hydrogen production from starch and water by a synthetic enzymatic pathway PLoS One 2 2007 e456
    • (2007) PLoS One , vol.2 , pp. e456
    • Zhang, Y.H.P.1    Evans, B.R.2    Mielenz, J.R.3    Hopkins, R.C.4    Adams, M.W.W.5
  • 12
    • 84876470702 scopus 로고    scopus 로고
    • High-yield production of dihydrogen from xylose by using a synthetic enzyme cascade in a cell-free system
    • Y. Wang, W. Huang, N. Sathitsuksanoh, Z. Zhu, and Y.H.P. Zhang High-yield production of dihydrogen from xylose by using a synthetic enzyme cascade in a cell-free system Angew Chem Int Ed 52 17 2013 4587 4590
    • (2013) Angew Chem Int Ed , vol.52 , Issue.17 , pp. 4587-4590
    • Wang, Y.1    Huang, W.2    Sathitsuksanoh, N.3    Zhu, Z.4    Zhang, Y.H.P.5
  • 14
    • 84911440747 scopus 로고    scopus 로고
    • Assembly and multiple gene expression of thermophilic enzymes in Escherichia coli for in vitro metabolic engineering
    • P.H. Ninh, K. Honda, T. Sakai, K. Okana, and H. Ohtake Assembly and multiple gene expression of thermophilic enzymes in Escherichia coli for in vitro metabolic engineering Biotechnol Bioeng 112 2015 189 196
    • (2015) Biotechnol Bioeng , vol.112 , pp. 189-196
    • Ninh, P.H.1    Honda, K.2    Sakai, T.3    Okana, K.4    Ohtake, H.5
  • 15
    • 84901300506 scopus 로고    scopus 로고
    • In vitro metabolic engineering of hydrogen production at theoretical yield from sucrose
    • S. Myung, J. Rollin, C. You, F. Sun, S. Chandrayan, M.W. Adams, and et al. In vitro metabolic engineering of hydrogen production at theoretical yield from sucrose Metab Eng 24 2014 70 77
    • (2014) Metab Eng , vol.24 , pp. 70-77
    • Myung, S.1    Rollin, J.2    You, C.3    Sun, F.4    Chandrayan, S.5    Adams, M.W.6
  • 16
    • 84856261361 scopus 로고    scopus 로고
    • Catalytic turnover of [FeFe]-hydrogenase based on single-molecule imaging
    • C. Madden, M.D. Vaughn, I. Diez-Perez, K.A. Brown, P.W. King, D. Gust, and et al. Catalytic turnover of [FeFe]-hydrogenase based on single-molecule imaging J Am Chem Soc 134 2012 1577 1582
    • (2012) J Am Chem Soc , vol.134 , pp. 1577-1582
    • Madden, C.1    Vaughn, M.D.2    Diez-Perez, I.3    Brown, K.A.4    King, P.W.5    Gust, D.6
  • 17
    • 77956281768 scopus 로고    scopus 로고
    • Heterologous expression and maturation of an NADP-dependent [NiFe]-hydrogenase: A key enzyme in biofuel production
    • J. Sun, R.C. Hopkins, F.E. Jenney, P.M. McTernan, and M.W.W. Adams Heterologous expression and maturation of an NADP-dependent [NiFe]-hydrogenase: a key enzyme in biofuel production PLoS One 5 2010 e10526
    • (2010) PLoS One , vol.5 , pp. e10526
    • Sun, J.1    Hopkins, R.C.2    Jenney, F.E.3    McTernan, P.M.4    Adams, M.W.W.5
  • 19
    • 33646575654 scopus 로고    scopus 로고
    • Simultaneous expression and maturation of the iron-sulfur protein ferredoxin in a cell-free system
    • M.E. Boyer, C.-W. Wang, and J.R. Swartz Simultaneous expression and maturation of the iron-sulfur protein ferredoxin in a cell-free system Biotechnol Bioeng 94 2006 128e38
    • (2006) Biotechnol Bioeng , vol.94 , pp. 128e38
    • Boyer, M.E.1    Wang, C.-W.2    Swartz, J.R.3
  • 20
    • 84855825394 scopus 로고    scopus 로고
    • Generation of hydrogen from NADPH using an [FeFe] hydrogenase
    • P.R. Smith, A.S. Bingham, and J.R. Swartz Generation of hydrogen from NADPH using an [FeFe] hydrogenase Int J Hydrogen Energy 37 2012 2977 2983
    • (2012) Int J Hydrogen Energy , vol.37 , pp. 2977-2983
    • Smith, P.R.1    Bingham, A.S.2    Swartz, J.R.3
  • 21
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • D.M. Hoover, and J. Lubkowski DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis Nucleic Acids Res 30 2002 e43
    • (2002) Nucleic Acids Res , vol.30 , pp. e43
    • Hoover, D.M.1    Lubkowski, J.2
  • 22
    • 8144226497 scopus 로고    scopus 로고
    • Total synthesis of long DNA sequences: Synthesis of a contiguous 32-kb polyketide synthase gene cluster
    • S.J. Kodumal, K.G. Patel, R. Reid, H.G. Menzella, M. Welch, and D.V. Santi Total synthesis of long DNA sequences: synthesis of a contiguous 32-kb polyketide synthase gene cluster Proc Natl Acad Sci U S A 101 44 2004 15573 15578
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.44 , pp. 15573-15578
    • Kodumal, S.J.1    Patel, K.G.2    Reid, R.3    Menzella, H.G.4    Welch, M.5    Santi, D.V.6
  • 23
    • 0015910074 scopus 로고
    • The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite
    • D.O. Lambeth, and G. Palmer The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite J Biol Chem 248 17 1973 6095 6103
    • (1973) J Biol Chem , vol.248 , Issue.17 , pp. 6095-6103
    • Lambeth, D.O.1    Palmer, G.2
  • 24
    • 4043167104 scopus 로고    scopus 로고
    • Structural aspects of plant ferrodoxin:NADP+ oxidoreductase
    • A. Karplus, and R. Faber Structural aspects of plant ferrodoxin:NADP+ oxidoreductase Photosyn Res 81 2004 303 315
    • (2004) Photosyn Res , vol.81 , pp. 303-315
    • Karplus, A.1    Faber, R.2
  • 25
    • 0035807852 scopus 로고    scopus 로고
    • Biochemical and crystallographic characterization of ferredoxin-NADP+ reductase from nonphotosynthetic tissues
    • A. Aliverti, R. Faber, C. Finnerty, C. Ferioli, V. Pandini, A. Negri, and et al. Biochemical and crystallographic characterization of ferredoxin-NADP+ reductase from nonphotosynthetic tissues Bochemistry 40 2001 14501 14508
    • (2001) Bochemistry , vol.40 , pp. 14501-14508
    • Aliverti, A.1    Faber, R.2    Finnerty, C.3    Ferioli, C.4    Pandini, V.5    Negri, A.6
  • 26
    • 0038368151 scopus 로고    scopus 로고
    • Open questions in ferredoxin-NADP+ reductase catalytic mechanism
    • N. Carrillo, and E.A. Ceccarelli Open questions in ferredoxin-NADP+ reductase catalytic mechanism Eur J Biochem 270 9 2003 1900 1915
    • (2003) Eur J Biochem , vol.270 , Issue.9 , pp. 1900-1915
    • Carrillo, N.1    Ceccarelli, E.A.2
  • 27
    • 0032559059 scopus 로고    scopus 로고
    • Role of arg100 and arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer
    • M. Martínez-Júlvez, J. Hermoso, J.K. Hurley, T. Mayoral, J. Sanz-Aparicio, G. Tollin, and et al. Role of arg100 and arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer Biochemistry 37 51 1998 17680 17691
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17680-17691
    • Martínez-Júlvez, M.1    Hermoso, J.2    Hurley, J.K.3    Mayoral, T.4    Sanz-Aparicio, J.5    Tollin, G.6
  • 28
    • 0015581286 scopus 로고
    • Cytochrome c: A thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters
    • Rimona Margalit, and Abel Schejter Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters Eur J Biochem 32 1973 492 499
    • (1973) Eur J Biochem , vol.32 , pp. 492-499
    • Margalit, R.1    Schejter, A.2
  • 29
    • 0023654386 scopus 로고
    • Oxidation-reduction properties of the two Fe4S4 clusters in Clostridium pasteurianum ferredoxin
    • Roger C. Prince, and Michael W.W. Adams Oxidation-reduction properties of the two Fe4S4 clusters in Clostridium pasteurianum ferredoxin J Biol Chem 262 11 1987 5125 5128
    • (1987) J Biol Chem , vol.262 , Issue.11 , pp. 5125-5128
    • Prince, R.C.1    Adams, M.W.W.2
  • 30
    • 0033911508 scopus 로고    scopus 로고
    • Differential interaction of maize root Ferredoxin:NADP oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins
    • Yayoi Onda, Tomohiro Matsumura, Yoko Kimata-Ariga, Hitoshi Sakakibara, Tatsuo Sugiyama, and Toshiharu Hase Differential interaction of maize root Ferredoxin:NADP oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins Plant Physiol 123 July 2000 1037 1045
    • (2000) Plant Physiol , vol.123 , pp. 1037-1045
    • Onda, Y.1    Matsumura, T.2    Kimata-Ariga, Y.3    Sakakibara, H.4    Sugiyama, T.5    Hase, T.6
  • 31
    • 0030804062 scopus 로고    scopus 로고
    • Intramolecular electron transfer between [4fe-4s] clusters studied by proton magnetic resonance spectroscopy
    • P. Kyritsis, J.G. Huber, I. Quinkal, J. Gaillard, and J.M. Moulis Intramolecular electron transfer between [4fe-4s] clusters studied by proton magnetic resonance spectroscopy Biochemistry 36 25 1997 7839 7846
    • (1997) Biochemistry , vol.36 , Issue.25 , pp. 7839-7846
    • Kyritsis, P.1    Huber, J.G.2    Quinkal, I.3    Gaillard, J.4    Moulis, J.M.5
  • 32
    • 33646126496 scopus 로고    scopus 로고
    • Total amino acid stabilization during cell-free protein synthesis reactions
    • K.A. Calhoun, and J.R. Swartz Total amino acid stabilization during cell-free protein synthesis reactions J Biotechnol 123 2 2006 193 203
    • (2006) J Biotechnol , vol.123 , Issue.2 , pp. 193-203
    • Calhoun, K.A.1    Swartz, J.R.2
  • 33
    • 0015217267 scopus 로고
    • Sugar transport II characterization of constitutive membrane-bound enzymes II of the Esherichia coli phosphotransferase system
    • W. Kundig, and S. Roseman Sugar transport II characterization of constitutive membrane-bound enzymes II of the Esherichia coli phosphotransferase system J Biol Chem 246 1971 1407 1418
    • (1971) J Biol Chem , vol.246 , pp. 1407-1418
    • Kundig, W.1    Roseman, S.2
  • 34
    • 53949093950 scopus 로고    scopus 로고
    • An integrated cell-free metabolic platform for protein production and synthetic biology
    • M. Jewett, K. Calhoun, A. Voloshin, J. Wuu, and J. Swartz An integrated cell-free metabolic platform for protein production and synthetic biology Mol Syst Biol 4 2008 220
    • (2008) Mol Syst Biol , vol.4 , pp. 220
    • Jewett, M.1    Calhoun, K.2    Voloshin, A.3    Wuu, J.4    Swartz, J.5
  • 35
  • 36
    • 68149124672 scopus 로고    scopus 로고
    • Role of pretreatment and conditioning processes on toxicity of lignocellulosic biomass hydrolysates
    • P. Pienkos, and M. Zhang Role of pretreatment and conditioning processes on toxicity of lignocellulosic biomass hydrolysates Cellulose 16 4 August 2009 743 762
    • (2009) Cellulose , vol.16 , Issue.4 , pp. 743-762
    • Pienkos, P.1    Zhang, M.2
  • 38
    • 84869409254 scopus 로고    scopus 로고
    • Cell-free metabolic engineering: Production of chemicals by minimized reaction cascades
    • J.-K. Guterl, D. Garbe, J. Carsten, F. Steffler, B. Sommer, S. Reiße, and et al. Cell-free metabolic engineering: production of chemicals by minimized reaction cascades ChemSusChem 5 2012 2165 2172 10.1002/cssc.201200365
    • (2012) ChemSusChem , vol.5 , pp. 2165-2172
    • Guterl, J.-K.1    Garbe, D.2    Carsten, J.3    Steffler, F.4    Sommer, B.5    Reiße, S.6


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