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Volumn 105, Issue 31, 2008, Pages 10654-10658

Reversible interconversion of carbon dioxide and formate by an electroactive enzyme

Author keywords

Carbon dioxide reduction; Electrocatalysis; Formate dehydrogenase; Formate oxidation; Protein film voltammetry

Indexed keywords

CARBON DIOXIDE; FORMATE DEHYDROGENASE; FORMIC ACID;

EID: 49449111220     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0801290105     Document Type: Article
Times cited : (453)

References (34)
  • 1
    • 0003652043 scopus 로고    scopus 로고
    • United Nations Development Programme, United Nations Department of Economic and Social Affairs, and World Energy Council , United Nations Development Programme, New York
    • United Nations Development Programme, United Nations Department of Economic and Social Affairs, and World Energy Council (2000) World Energy Assessment: Energy and the Challenge of Sustainability (United Nations Development Programme, New York).
    • (2000) World Energy Assessment: Energy and the Challenge of Sustainability
  • 2
    • 34547774971 scopus 로고    scopus 로고
    • Intergovernmental Panel on Climate Change , Cambridge Univ Press, Cambridge, UK
    • Intergovernmental Panel on Climate Change (2007) Fourth Assessment Report: Climate Change 2007 (Cambridge Univ Press, Cambridge, UK).
    • (2007) Fourth Assessment Report: Climate Change 2007
  • 3
    • 0348041366 scopus 로고
    • Mechanisms of the electrochemical reduction of carbon dioxide catalyzed by transition metal complexes
    • eds Sullivan BP, Krist K, Guard HE Elsevier, Amsterdam, pp
    • Keene FR, Sullivan BP (1993) Mechanisms of the electrochemical reduction of carbon dioxide catalyzed by transition metal complexes, in Electrochemical and Electrocatalytic Reactions of Carbon Dioxide, eds Sullivan BP, Krist K, Guard HE (Elsevier, Amsterdam), pp 118-144.
    • (1993) Electrochemical and Electrocatalytic Reactions of Carbon Dioxide , pp. 118-144
    • Keene, F.R.1    Sullivan, B.P.2
  • 4
    • 34548229516 scopus 로고    scopus 로고
    • Electrochemical reactions of carbon dioxide
    • eds Bard AJ, Stratmann M, Wiley-VCH, Weinheim, Germany, pp
    • DuBois DL (2006) Electrochemical reactions of carbon dioxide, in Encyclopaedia of Electrochemistry, eds Bard AJ, Stratmann M. (Wiley-VCH, Weinheim, Germany), pp 202-225.
    • (2006) Encyclopaedia of Electrochemistry , pp. 202-225
    • DuBois, D.L.1
  • 5
    • 2442440676 scopus 로고
    • Homogeneous catalytic hydrogenation of supercritical carbon dioxide
    • Jessop PG, Ikariya T, Noyori R (1994) Homogeneous catalytic hydrogenation of supercritical carbon dioxide. Nature 368:231-233.
    • (1994) Nature , vol.368 , pp. 231-233
    • Jessop, P.G.1    Ikariya, T.2    Noyori, R.3
  • 6
    • 30544433415 scopus 로고    scopus 로고
    • 2-reduction catalyzed by metal electrodes
    • eds Vielstich W, Gasteiger HA, Lamm A Wiley, Chichester, UK
    • 2-reduction catalyzed by metal electrodes, in Handbook of Fuel Cells - Fundamentals, Technology and Applications, eds Vielstich W, Gasteiger HA, Lamm A (Wiley, Chichester, UK), Vol 2, pp 720-733.
    • (2003) Handbook of Fuel Cells - Fundamentals, Technology and Applications , vol.2 , pp. 720-733
    • Hori, Y.1
  • 8
    • 33744974026 scopus 로고    scopus 로고
    • Characterization of a high performing passive direct formic acid fuel cell
    • Ha S, Dunbar Z, Masel RI (2006) Characterization of a high performing passive direct formic acid fuel cell. J Power Sources 158:129-136.
    • (2006) J Power Sources , vol.158 , pp. 129-136
    • Ha, S.1    Dunbar, Z.2    Masel, R.I.3
  • 9
    • 3142629049 scopus 로고
    • 2 in Clostridium thermoaceticum
    • 2 in Clostridium thermoaceticum. FEBS Lett 27:111-115.
    • (1972) FEBS Lett , vol.27 , pp. 111-115
    • Thauer, R.K.1
  • 11
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka M, Törnroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Törnroth, S.2    Byrne, B.3    Iwata, S.4
  • 12
    • 0036711479 scopus 로고    scopus 로고
    • Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas
    • Raaijmakers H, et al. (2002) Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure (London) 10:1261-1272.
    • (2002) Structure (London) , vol.10 , pp. 1261-1272
    • Raaijmakers, H.1
  • 13
    • 0036366810 scopus 로고    scopus 로고
    • Molybdenum and tungsten enzymes in C1 metabolism
    • eds Siegel A, Siegel H Dekker, New York
    • Vorholt JA, Thauer RK (2002) Molybdenum and tungsten enzymes in C1 metabolism, in Metal Ions in Biological Systems, eds Siegel A, Siegel H (Dekker, New York), Vol 39, pp 571-619.
    • (2002) Metal Ions in Biological Systems , vol.39 , pp. 571-619
    • Vorholt, J.A.1    Thauer, R.K.2
  • 15
    • 0038054187 scopus 로고    scopus 로고
    • 2-reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans
    • 2-reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans. Eur J Biochem 270:2476-2485.
    • (2003) Eur J Biochem , vol.270 , pp. 2476-2485
    • de Bok, F.A.M.1
  • 16
    • 0036731743 scopus 로고    scopus 로고
    • Biochemical evidence for formate transfer in syntrophic propionate-oxidizing cocultures of Syntrophobacter fumaroxidans and Methanospirillum hungatei
    • de Bok FAM, Luijten MLGC, Stams AJM (2002) Biochemical evidence for formate transfer in syntrophic propionate-oxidizing cocultures of Syntrophobacter fumaroxidans and Methanospirillum hungatei. Appl Environ Microbiol 68:4247-4252.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4247-4252
    • de Bok, F.A.M.1    Luijten, M.L.G.C.2    Stams, A.J.M.3
  • 17
    • 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 TC, Böck A (1986) Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 83:4650-4654.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Böck, A.4
  • 18
    • 0041318860 scopus 로고    scopus 로고
    • Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
    • Bertero MG, et al. (2003) Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat Struct Biol 10:681-687.
    • (2003) Nat Struct Biol , vol.10 , pp. 681-687
    • Bertero, M.G.1
  • 19
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC (1996) Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination. Science 272:1615-1621.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 20
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov LA, Hinchliffe P (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311:1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 21
    • 0038967617 scopus 로고
    • The chemistry of metal carbonato and carbon dioxide complexes
    • Palmer DA, van Eldik R (1983) The chemistry of metal carbonato and carbon dioxide complexes. Chem Rev 83:651-731.
    • (1983) Chem Rev , vol.83 , pp. 651-731
    • Palmer, D.A.1    van Eldik, R.2
  • 22
    • 18744432274 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms
    • Lëger C, et al. (2003) Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms. Biochemistry 42:8653-8662.
    • (2003) Biochemistry , vol.42 , pp. 8653-8662
    • Lëger, C.1
  • 23
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • Vincent KA, Parkin A, Armstrong FA (2007) Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem Rev 107:4366-4413.
    • (2007) Chem Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 24
    • 33644508034 scopus 로고    scopus 로고
    • Interpreting the catalytic voltammetry of an adsorbed enzyme by considering substrate mass transfer, enzyme turnover, and interfacial electron transport
    • Reda T, Hirst J (2006) Interpreting the catalytic voltammetry of an adsorbed enzyme by considering substrate mass transfer, enzyme turnover, and interfacial electron transport. J Phys Chem B 110:1394-1404.
    • (2006) J Phys Chem B , vol.110 , pp. 1394-1404
    • Reda, T.1    Hirst, J.2
  • 25
    • 0000289261 scopus 로고
    • Photoelectrochemical pumping of enzymatic CO2 reduction
    • Parkinson BA, Weaver PF (1984) Photoelectrochemical pumping of enzymatic CO2 reduction. Nature 309:148-149.
    • (1984) Nature , vol.309 , pp. 148-149
    • Parkinson, B.A.1    Weaver, P.F.2
  • 26
    • 70049105003 scopus 로고    scopus 로고
    • Standard, formal, and other characteristic potentials of selected electrode reactions
    • eds Bard AJ, Stratmann M Wiley-VCH, Weinheim, Germany, pp
    • Inzelt, G (2006) Standard, formal, and other characteristic potentials of selected electrode reactions, in Encyclopaedia of Electrochemistry, eds Bard AJ, Stratmann M (Wiley-VCH, Weinheim, Germany), pp 17-76.
    • (2006) Encyclopaedia of Electrochemistry , pp. 17-76
    • Inzelt, G.1
  • 28
    • 33646583168 scopus 로고    scopus 로고
    • Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
    • Tcherkez GGB, Farquhar GD, Andrews TJ (2006) Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized. Proc Natl Acad Sci USA 103:7246-7251.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7246-7251
    • Tcherkez, G.G.B.1    Farquhar, G.D.2    Andrews, T.J.3
  • 31
    • 34249677218 scopus 로고    scopus 로고
    • Synthesis and structures of bis(dithiolene)-tungsten(IV,VI) thiolate and selenolate compounds: Approaches to the active sites of molybdenum and tungsten formate dehydrogenases
    • Groysman S, Holm RH (2007) Synthesis and structures of bis(dithiolene)-tungsten(IV,VI) thiolate and selenolate compounds: approaches to the active sites of molybdenum and tungsten formate dehydrogenases. Inorg Chem 46:4090-4102.
    • (2007) Inorg Chem , vol.46 , pp. 4090-4102
    • Groysman, S.1    Holm, R.H.2
  • 32
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • Kisker C, Schindelin H, Rees DC (1997) Molybdenum-cofactor-containing enzymes: Structure and mechanism. Annu Rev Biochem 66:233-267.
    • (1997) Annu Rev Biochem , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 33
    • 33845556423 scopus 로고
    • Facile reduction of carbon dioxide by anionic group 6B metal hydrides. Chemistry relevant to catalysis of the water-gas shift reaction
    • DarensbourgMY
    • Darensbourg DJ, Rokicki A, DarensbourgMY(1981) Facile reduction of carbon dioxide by anionic group 6B metal hydrides. Chemistry relevant to catalysis of the water-gas shift reaction. J Am Chem Soc 103:3223-3224.
    • (1981) J Am Chem Soc , vol.103 , pp. 3223-3224
    • Darensbourg, D.J.1    Rokicki, A.2


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