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Volumn 2011, Issue 1, 2011, Pages

Formate formation and formate conversion in biological fuels production

Author keywords

[No Author keywords available]

Indexed keywords

BIOFUEL; CARBON DIOXIDE; FORMATE DEHYDROGENASE; FORMIC ACID; HYDROGEN; LYASE; METHANE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVIC ACID;

EID: 84865694544     PISSN: 20900406     EISSN: 20900414     Source Type: Journal    
DOI: 10.4061/2011/532536     Document Type: Review
Times cited : (67)

References (50)
  • 1
    • 0003621959 scopus 로고    scopus 로고
    • USEIA, Washington, DC, USA Administration USEI
    • USEIA, Annual Energy Outlook 2010 Washington, DC, USA Administration USEI
    • (2010) Annual Energy Outlook
  • 2
    • 71649107594 scopus 로고    scopus 로고
    • Biomethane in the transport sector-an appraisal of the forgotten option
    • 2-s2.0-71649107594 10.1016/j.enpol.2009.09.007
    • Åhman M., Biomethane in the transport sector-an appraisal of the forgotten option. Energy Policy 2010 38 1 208 217 2-s2.0-71649107594 10.1016/j.enpol.2009.09.007
    • (2010) Energy Policy , vol.38 , Issue.1 , pp. 208-217
    • Åhman, M.1
  • 5
    • 0036803518 scopus 로고    scopus 로고
    • Comparative process stability and efficiency of anaerobic digestion; mesophilic vs. thermophilic
    • DOI 10.1016/S0043-1354(02)00147-1, PII S0043135402001471
    • Kim M., Ahn Y. H., Speece R. E., Comparative process stability and efficiency of anaerobic digestion; mesophilic vs. thermophilic. Water Research 2002 36 17 4369 4385 2-s2.0-0036803518 10.1016/S0043-1354(02)00147-1 (Pubitemid 35291165)
    • (2002) Water Research , vol.36 , Issue.17 , pp. 4369-4385
    • Kim, M.1    Ahn, Y.-H.2    Speece, R.E.3
  • 6
    • 0016294957 scopus 로고
    • Pyruvate formate lyase of Escherichia coli: The acetyl enzyme intermediate
    • 2-s2.0-0016294957
    • Knappe J., Blaschkowski H. P., Groebner P., Schmitt T., Pyruvate formate lyase of Escherichia coli: the acetyl enzyme intermediate. European Journal of Biochemistry 1974 50 1 253 263 2-s2.0-0016294957
    • (1974) European Journal of Biochemistry , vol.50 , Issue.1 , pp. 253-263
    • Knappe, J.1    Blaschkowski, H.P.2    Groebner, P.3    Schmitt, T.4
  • 9
    • 0001387326 scopus 로고
    • The anaerobic dissimilation of pyruvate by a cell-free extract of Escherichia coli
    • Kalnitsky G., Werkman C. H., The anaerobic dissimilation of pyruvate by a cell-free extract of Escherichia coli. Archives of Biochemistry 1943 2 113 124
    • (1943) Archives of Biochemistry , vol.2 , pp. 113-124
    • Kalnitsky, G.1    Werkman, C.H.2
  • 12
    • 0027320421 scopus 로고
    • Pyruvate formate-lyase mechanism involving the protein-based glycyl radical
    • Knappe J., Elbert S., Frey M., Wagner A. F. V., Pyruvate formate-lyase mechanism involving the protein-based glycyl radical. Biochemical Society Transactions 1993 21 3, part 3 731 734 2-s2.0-0027320421 (Pubitemid 23265773)
    • (1993) Biochemical Society Transactions , vol.21 , Issue.3 , pp. 731-734
    • Knappe, J.1    Elbert, S.2    Frey, M.3    Wagner, A.F.V.4
  • 13
    • 0032851377 scopus 로고    scopus 로고
    • Structure and mechanism of the glycyl radical enzyme pyruvate formate- lyase
    • DOI 10.1038/13341
    • Becker A., Fritz-Wolf K., Kabsch W., Knappe J., Schultz S., Volker Wagner A. F., Structure and mechanism of the glycyl radical enzyme pyruvate formate- lyase. Nature Structural Biology 1999 6 10 969 975 2-s2.0-0032851377 10.1038/13341 (Pubitemid 29463312)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 969-975
    • Becker, A.1    Fritz-Wolf, K.2    Kabsch, W.3    Knappe, J.4    Schultz, S.5    Volker Wagner, A.F.6
  • 14
    • 0037131403 scopus 로고    scopus 로고
    • X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage
    • DOI 10.1074/jbc.M205821200
    • Becker A., Kabsch W., X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage. Journal of Biological Chemistry 2002 277 42 40036 40042 2-s2.0-0037131403 10.1074/jbc.M205821200 (Pubitemid 35190993)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 40036-40042
    • Becker, A.1    Kabsch, W.2
  • 16
    • 6344286013 scopus 로고    scopus 로고
    • Catalytic mechanism of pyruvate-formate lyase revisited
    • 2-s2.0-6344286013 10.1021/jp0478054
    • Guo J. D., Himo F., Catalytic mechanism of pyruvate-formate lyase revisited. Journal of Physical Chemistry B 2004 108 39 15347 15354 2-s2.0-6344286013 10.1021/jp0478054
    • (2004) Journal of Physical Chemistry B , vol.108 , Issue.39 , pp. 15347-15354
    • Guo, J.D.1    Himo, F.2
  • 17
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • 2-s2.0-0028566978 10.1007/BF00871633
    • Sawers G., The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie van Leeuwenhoek 1994 66 1-3 57 88 2-s2.0-0028566978 10.1007/BF00871633
    • (1994) Antonie Van Leeuwenhoek , vol.66 , Issue.1-3 , pp. 57-88
    • Sawers, G.1
  • 18
    • 0031043109 scopus 로고    scopus 로고
    • 4 cluster
    • DOI 10.1126/science.275.5304.1305
    • Boyington J. C., Gladyshev V. N., Khangulov S. V., Stadtman T. C., Sun P. D., Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an FeS cluster. Science 1997 275 5304 1305 1308 2-s2.0-0031043109 10.1126/science.275.5304.1305 (Pubitemid 27114158)
    • (1997) Science , vol.275 , Issue.5304 , pp. 1305-1308
    • Boyington, J.C.1    Gladyshev, V.N.2    Khangulov, S.V.3    Stadtman, T.C.4    Sun, P.D.5
  • 19
    • 33748337941 scopus 로고    scopus 로고
    • Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of the crystal structure suggests a new reaction mechanism
    • DOI 10.1007/s00775-006-0129-2
    • Raaijmakers H. C. A., Romão M. J., Formate-reduced E. coli formate dehydrogenase H: the reinterpretation of the crystal structure suggests a new reaction mechanism. Journal of Biological Inorganic Chemistry 2006 11 7 849 854 2-s2.0-33748337941 10.1007/s00775-006-0129-2 (Pubitemid 44337586)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.7 , pp. 849-854
    • Raaijmakers, H.C.A.1    Romao, M.J.2
  • 20
    • 0028860781 scopus 로고
    • Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase
    • 2-s2.0-0028860781
    • Abaibou H., Pommier J., Benoit S., Giordano G., Mandrand-Berthelot M. A., Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. Journal of Bacteriology 1995 177 24 7141 7149 2-s2.0-0028860781
    • (1995) Journal of Bacteriology , vol.177 , Issue.24 , pp. 7141-7149
    • Abaibou, H.1    Pommier, J.2    Benoit, S.3    Giordano, G.4    Mandrand-Berthelot, M.A.5
  • 22
    • 10744223111 scopus 로고    scopus 로고
    • Energy conservation in acetogenic bacteria
    • DOI 10.1128/AEM.69.11.6345-6353.2003
    • Müller V., Energy conservation in acetogenic bacteria. Applied and Environmental Microbiology 2003 69 11 6345 6353 2-s2.0-10744223111 10.1128/AEM.69.11.6345-6353.2003 (Pubitemid 37420162)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.11 , pp. 6345-6353
    • Muller, V.1
  • 23
    • 41349119857 scopus 로고    scopus 로고
    • Enzymology of the Wood-Ljungdahl pathway of acetogenesis
    • DOI 10.1196/annals.1419.015, Incredible Anaerobes From Physiology to Genomics to Fuels
    • Ragsdale S. W., Enzymology of the Wood-Ljungdahl pathway of acetogenesis. Annals of the New York Academy of Sciences 2008 1125 129 136 2-s2.0-41349119857 10.1196/annals.1419.015 (Pubitemid 351451161)
    • (2008) Annals of the New York Academy of Sciences , vol.1125 , pp. 129-136
    • Ragsdale, S.W.1
  • 24
    • 54949153045 scopus 로고    scopus 로고
    • 2 fixation
    • 2-s2.0-54949153045 10.1016/j.bbapap.2008.08.012
    • 2 fixation. Biochimica et Biophysica Acta 2008 1784 12 1873 1898 2-s2.0-54949153045 10.1016/j.bbapap.2008.08.012
    • (2008) Biochimica et Biophysica Acta , vol.1784 , Issue.12 , pp. 1873-1898
    • Ragsdale, S.W.1    Pierce, E.2
  • 27
    • 0027937347 scopus 로고
    • NAD-dependent formate dehydrogenase
    • 2-s2.0-0027937347
    • Popov V. O., Lamzin V. S., NAD-dependent formate dehydrogenase. Biochemical Journal 1994 301 3 625 643 2-s2.0-0027937347
    • (1994) Biochemical Journal , vol.301 , Issue.3 , pp. 625-643
    • Popov, V.O.1    Lamzin, V.S.2
  • 28
    • 71949095378 scopus 로고    scopus 로고
    • Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: Towards understanding the mechanism of the closure of the interdomain cleft
    • 2-s2.0-71949095378 10.1107/S0907444909040773
    • Shabalin I. G., Filippova E. V., Polyakov K. M., Sadykhov E. G., Safonova T. N., Tikhonova T. V., Tishkov V. I., Popov V. O., Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleft. Acta Crystallographica Section D: Biological Crystallography 2009 65 12 1315 1325 2-s2.0-71949095378 10.1107/S0907444909040773
    • (2009) Acta Crystallographica Section D: Biological Crystallography , vol.65 , Issue.12 , pp. 1315-1325
    • Shabalin, I.G.1    Filippova, E.V.2    Polyakov, K.M.3    Sadykhov, E.G.4    Safonova, T.N.5    Tikhonova, T.V.6    Tishkov, V.I.7    Popov, V.O.8
  • 29
    • 11144247396 scopus 로고    scopus 로고
    • Catalytic mechanism and application of formate dehydrogenase
    • DOI 10.1007/s10541-005-0071-x
    • Tishkov V. I., Popov V. O., Catalytic mechanism and application of formate dehydrogenase. Biochemistry 2004 69 11 1252 1267 2-s2.0-11144247396 10.1007/s10541-005-0071-x (Pubitemid 40050044)
    • (2004) Biochemistry (Moscow) , vol.69 , Issue.11 , pp. 1252-1267
    • Tishkov, V.I.1    Popov, V.O.2
  • 30
    • 77952881357 scopus 로고    scopus 로고
    • Thermodynamic feasibility of enzymatic reduction of carbon dioxide to methanol
    • 2-s2.0-77952881357 10.1007/s12010-009-8758-x
    • Baskaya F. S., Zhao X., Flickinger M. C., Wang P., Thermodynamic feasibility of enzymatic reduction of carbon dioxide to methanol. Applied Biochemistry and Biotechnology 2010 162 2 391 398 2-s2.0-77952881357 10.1007/s12010-009-8758-x
    • (2010) Applied Biochemistry and Biotechnology , vol.162 , Issue.2 , pp. 391-398
    • Baskaya, F.S.1    Zhao, X.2    Flickinger, M.C.3    Wang, P.4
  • 31
    • 38449084922 scopus 로고    scopus 로고
    • 2 catalyzed by coimmobilized enzymes
    • DOI 10.1002/bit.21584
    • 2 catalyzed by coimmobilized enzymes. Biotechnology and Bioengineering 2008 99 3 508 514 2-s2.0-38449084922 10.1002/bit.21584 (Pubitemid 351158248)
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.3 , pp. 508-514
    • El-Zahab, B.1    Donnelly, D.2    Wang, P.3
  • 32
    • 0033616117 scopus 로고    scopus 로고
    • Enzymatic conversion of carbon dioxide to methanol: Enhanced methanol production in silica sol-gel matrices [5]
    • DOI 10.1021/ja991899r
    • Obert R., Dave B. C., Enzymatic conversion of carbon dioxide to methanol: enhanced methanol production in silica sol-gel matrices. Journal of the American Chemical Society 1999 121 51 12192 12193 2-s2.0-0033616117 10.1021/ja991899r (Pubitemid 30027799)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.51 , pp. 12192-12193
    • Obert, R.1    Dave, B.C.2
  • 33
    • 77956955599 scopus 로고    scopus 로고
    • Stability and reactivity of liposome-encapsulated formate dehydrogenase and cofactor system in carbon dioxide gas-liquid flow
    • yosimoto@yamaguchi-u.ac.jp 10.1002/btpr.409
    • Yoshimoto M., yosimoto@yamaguchi-u.ac.jp Yamashita T., Yamashiro T., Stability and reactivity of liposome-encapsulated formate dehydrogenase and cofactor system in carbon dioxide gas-liquid flow. Biotechnology Progress 2010 26 4 1047 1053 10.1002/btpr.409
    • (2010) Biotechnology Progress , vol.26 , Issue.4 , pp. 1047-1053
    • Yoshimoto, M.1    Yamashita, T.2    Yamashiro, T.3
  • 35
    • 44449149379 scopus 로고    scopus 로고
    • Life close to the thermodynamic limit: How methanogenic archaea conserve energy
    • vmueller@bio.uni-frankfurt.de 10.1007/4002006026
    • Deppenmeier U., Müller V., vmueller@bio.uni-frankfurt.de Life close to the thermodynamic limit: how methanogenic archaea conserve energy. Results and Problems in Cell Differentiation 2008 45 123 152 10.1007/4002006026
    • (2008) Results and Problems in Cell Differentiation , vol.45 , pp. 123-152
    • Deppenmeier, U.1    Müller, V.2
  • 37
    • 0024357888 scopus 로고
    • Formate auxotroph of Methanobacterium thermoautotrophicum Marburg
    • Tanner R. S., McInerney M. J., Nagle D. P., Formate auxotroph of Methanobacterium thermoautotrophicum Marburg. Journal of Bacteriology 1989 171 12 6534 6538 2-s2.0-0024357888 (Pubitemid 20006932)
    • (1989) Journal of Bacteriology , vol.171 , Issue.12 , pp. 6534-6538
    • Tanner, R.S.1    McInerney, M.J.2    Nagle Jr., D.P.3
  • 38
    • 47549119041 scopus 로고    scopus 로고
    • Methanogenic archaea: Ecologically relevant differences in energy conservation
    • 2-s2.0-47549119041 10.1038/nrmicro1931
    • Thauer R. K., Kaster A. K., Seedorf H., Buckel W., Hedderich R., Methanogenic archaea: ecologically relevant differences in energy conservation. Nature Reviews Microbiology 2008 6 8 579 591 2-s2.0-47549119041 10.1038/nrmicro1931
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.8 , pp. 579-591
    • Thauer, R.K.1    Kaster, A.K.2    Seedorf, H.3    Buckel, W.4    Hedderich, R.5
  • 40
    • 70449894893 scopus 로고    scopus 로고
    • Syntrophy in anaerobic global carbon cycles
    • 2-s2.0-70449894893 10.1016/j.copbio.2009.10.001
    • McInerney M. J., Sieber J. R., Gunsalus R. P., Syntrophy in anaerobic global carbon cycles. Current Opinion in Biotechnology 2009 20 6 623 632 2-s2.0-70449894893 10.1016/j.copbio.2009.10.001
    • (2009) Current Opinion in Biotechnology , vol.20 , Issue.6 , pp. 623-632
    • McInerney, M.J.1    Sieber, J.R.2    Gunsalus, R.P.3
  • 42
    • 42349106001 scopus 로고    scopus 로고
    • Syntrophism among prokaryotes
    • Schink B., Stams A. J. M., Syntrophism among prokaryotes. Prokaryotes 2006 2 309 335
    • (2006) Prokaryotes , vol.2 , pp. 309-335
    • Schink, B.1    Stams, A.J.M.2
  • 45
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer R. K., Jungermann K., Decker K., Energy conservation in chemotrophic anaerobic bacteria. Bacteriological Reviews 1977 41 1 100 180 2-s2.0-0017343370 (Pubitemid 8082287)
    • (1977) Bacteriological Reviews , vol.41 , Issue.1 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 46
    • 0014160647 scopus 로고
    • Methanobacillus omelianskii, a symbiotic association of two species of bacteria
    • 2-s2.0-0014160647 10.1007/BF00406313
    • Bryant M. P., Wolin E. A., Wolin M. J., Wolfe R. S., Methanobacillus omelianskii, a symbiotic association of two species of bacteria. Archiv für Mikrobiologie 1967 59 1-3 20 31 2-s2.0-0014160647 10.1007/BF00406313
    • (1967) Archiv für Mikrobiologie , vol.59 , Issue.1-3 , pp. 20-31
    • Bryant, M.P.1    Wolin, E.A.2    Wolin, M.J.3    Wolfe, R.S.4
  • 47
    • 0029562475 scopus 로고
    • Role of formate and hydrogen in the degradation of propionate and butyrate by defined suspended cocultures of acetogenic and methanogenic bacteria
    • DOI 10.1007/BF00874137
    • Stams A. J. M., Dong X., Role of formate and hydrogen in the degradation of propionate and butyrate by defined suspended cocultures of acetogenic and methanogenic bacteria. Antonie van Leeuwenhoek 1995 68 4 281 284 2-s2.0-0029562475 10.1007/BF00874137 (Pubitemid 26024797)
    • (1995) Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology , vol.68 , Issue.4 , pp. 281-284
    • Stams, A.J.M.1    Dong, X.2
  • 48
    • 58149279639 scopus 로고    scopus 로고
    • Effect of tungsten and molybdenum on growth of a syntrophic coculture of Syntrophobacter fumaroxidans and Methanospirillum hungatei
    • 2-s2.0-58149279639 10.1007/s00203-008-0428-9
    • Plugge C. M., Jiang BO., De Bok F. A. M., Tsai C., Stams A. J. M., Effect of tungsten and molybdenum on growth of a syntrophic coculture of Syntrophobacter fumaroxidans and Methanospirillum hungatei. Archives of Microbiology 2009 191 1 55 61 2-s2.0-58149279639 10.1007/s00203-008-0428-9
    • (2009) Archives of Microbiology , vol.191 , Issue.1 , pp. 55-61
    • Plugge, C.M.1    Jiang, B.O.2    De Bok, F.A.M.3    Tsai, C.4    Stams, A.J.M.5
  • 49
    • 78650720286 scopus 로고    scopus 로고
    • Growth- and substrate-dependent transcription of formate dehydrogenase and hydrogenase coding genes in Syntrophobacter fumaroxidans and Methanospirillum hungatei
    • caroline.plugge@wur.nl 10.1099/mic.0.043927-0
    • Worm P., Stams A. J.M., Cheng X., Plugge C. M., caroline.plugge@wur.nl Growth- and substrate-dependent transcription of formate dehydrogenase and hydrogenase coding genes in Syntrophobacter fumaroxidans and Methanospirillum hungatei. Microbiology 2011 157 1 280 289 10.1099/mic.0.043927-0
    • (2011) Microbiology , vol.157 , Issue.1 , pp. 280-289
    • Worm, P.1    Stams, A.J.M.2    Cheng, X.3    Plugge, C.M.4
  • 50
    • 77953564075 scopus 로고    scopus 로고
    • Metabolic engineering to enhance bacterial hydrogen production
    • 2-s2.0-77953564075 10.1111/j.1751-7915.2007.00003.x
    • Maeda T., Sanchez-Torres V., Wood T. K., Metabolic engineering to enhance bacterial hydrogen production. Microbial Biotechnology 2008 1 1 30 39 2-s2.0-77953564075 10.1111/j.1751-7915.2007.00003.x
    • (2008) Microbial Biotechnology , vol.1 , Issue.1 , pp. 30-39
    • Maeda, T.1    Sanchez-Torres, V.2    Wood, T.K.3


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