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Volumn 197, Issue 8, 2015, Pages 1386-1393

Correction for Lo et al.: The bifunctional alcohol and aldehyde dehydrogenase Gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum (Journal of Bacteriology (2015) 197:8 (1386–1393) DOI: 10.1128/JB.02450-14);The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; ALCOHOL DEHYDROGENASE; ALDEHYDE; ALDEHYDE DEHYDROGENASE; BIOFUEL; FRUCTOSE 1,6 BISPHOSPHATE; LACTATE DEHYDROGENASE; LACTIC ACID; UBIQUINONE;

EID: 84924067126     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00405-18     Document Type: Erratum
Times cited : (77)

References (48)
  • 4
    • 84871402263 scopus 로고    scopus 로고
    • Redirecting carbon flux through exogenous pyruvate kinase to achieve high ethanol yields in Clostridium thermocellum
    • Deng Y, Olson DG, Zhou J, Herring CD, Joe Shaw A, Lynd LR. 2013. Redirecting carbon flux through exogenous pyruvate kinase to achieve high ethanol yields in Clostridium thermocellum. Metab Eng 15:151-158. http://dx.doi.org/10.1016/j.ymben.2012.11.006.
    • (2013) Metab Eng , vol.15 , pp. 151-158
    • Deng, Y.1    Olson, D.G.2    Zhou, J.3    Herring, C.D.4    Joe Shaw, A.5    Lynd, L.R.6
  • 5
    • 84888097068 scopus 로고    scopus 로고
    • Metabolic engineering of Thermoanaerobacterium saccharolyticum for nbutanol production
    • Bhandiwad A, Shaw AJ, Guss A, Guseva A, Bahl H, Lynd LR. 2014. Metabolic engineering of Thermoanaerobacterium saccharolyticum for nbutanol production. Metab Eng 21:17-25. http://dx.doi.org/10.1016/j.ymben.2013.10.012.
    • (2014) Metab Eng , vol.21 , pp. 17-25
    • Bhandiwad, A.1    Shaw, A.J.2    Guss, A.3    Guseva, A.4    Bahl, H.5    Lynd, L.R.6
  • 7
    • 79961084093 scopus 로고    scopus 로고
    • Redesigning Escherichia coli metabolism for anaerobic production of isobutanol
    • Trinh CT, Li J, Blanch HW, Clark DS. 2011. Redesigning Escherichia coli metabolism for anaerobic production of isobutanol. Appl Environ Microbiol 77:4894-4904. http://dx.doi.org/10.1128/AEM.00382-11.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 4894-4904
    • Trinh, C.T.1    Li, J.2    Blanch, H.W.3    Clark, D.S.4
  • 8
    • 0036180998 scopus 로고    scopus 로고
    • Molecular characterization and transcriptional analysis of adhE2, the gene encoding the NADH-dependent aldehyde/alcohol dehydrogenase responsible for butanol production in alcohologenic cultures of Clostridium acetobutylicum ATCC 824
    • Fontaine L, Meynial-Salles I, Girbal L, Yang X, Croux C, Soucaille P. 2002. Molecular characterization and transcriptional analysis of adhE2, the gene encoding the NADH-dependent aldehyde/alcohol dehydrogenase responsible for butanol production in alcohologenic cultures of Clostridium acetobutylicum ATCC 824. J Bacteriol 184:821-830. http://dx.doi.org/10.1128/JB.184.3.821-830.2002.
    • (2002) J Bacteriol , vol.184 , pp. 821-830
    • Fontaine, L.1    Meynial-Salles, I.2    Girbal, L.3    Yang, X.4    Croux, C.5    Soucaille, P.6
  • 9
    • 77957292723 scopus 로고    scopus 로고
    • Identification and overexpression of a bifunctional aldehyde/alcohol dehydrogenase responsible for ethanol production in Thermoanaerobacter mathranii
    • Yao S, Mikkelsen MJ. 2010. Identification and overexpression of a bifunctional aldehyde/alcohol dehydrogenase responsible for ethanol production in Thermoanaerobacter mathranii. J Mol Microbiol Biotechnol 19:123-133. http://dx.doi.org/10.1159/000321498.
    • (2010) J Mol Microbiol Biotechnol , vol.19 , pp. 123-133
    • Yao, S.1    Mikkelsen, M.J.2
  • 10
    • 84897840456 scopus 로고    scopus 로고
    • Metabolic Engineering of Thermoanaerobacterium thermosaccharolyticum for increased n-butanol production
    • Bhandiwad A, Guseva A, Lynd L. 2013. Metabolic Engineering of Thermoanaerobacterium thermosaccharolyticum for increased n-butanol production. AiM 3:46-51. http://dx.doi.org/10.4236/aim.2013.31007.
    • (2013) AiM , vol.3 , pp. 46-51
    • Bhandiwad, A.1    Guseva, A.2    Lynd, L.3
  • 11
    • 0028074589 scopus 로고
    • Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase
    • Burdette D, Zeikus JG. 1994. Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase. Biochem J 302:163-170.
    • (1994) Biochem J , vol.302 , pp. 163-170
    • Burdette, D.1    Zeikus, J.G.2
  • 13
    • 77955657983 scopus 로고    scopus 로고
    • Thermoanaerobacter spp. control ethanol pathway via transcriptional regulation and versatility of key enzymes
    • Pei J, Zhou Q, Jiang Y, Le Y, Li H, Shao W, Wiegel J. 2010. Thermoanaerobacter spp. control ethanol pathway via transcriptional regulation and versatility of key enzymes. Metab Eng 12:420-428. http://dx.doi.org /10.1016/j.ymben.2010.06.001.
    • (2010) Metab Eng , vol.12 , pp. 420-428
    • Pei, J.1    Zhou, Q.2    Jiang, Y.3    Le, Y.4    Li, H.5    Shao, W.6    Wiegel, J.7
  • 15
    • 4344700076 scopus 로고    scopus 로고
    • A multisubunit membranebound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis
    • Soboh B, Linder D, Hedderich R. 2004. A multisubunit membranebound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis. Microbiology 150:2451-2463. http://dx.doi.org/10.1099/mic.0.27159-0.
    • (2004) Microbiology , vol.150 , pp. 2451-2463
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 16
    • 84866481432 scopus 로고    scopus 로고
    • Proteomic analysis of Clostridium thermocellum core metabolism: relative protein expression profiles and growth phase-dependent changes in protein expression
    • Rydzak T, McQueen PD, Krokhin OV, Spicer V, Ezzati P, Dwivedi RC, Shamshurin D, Levin DB, Wilkins JA, Sparling R. 2012. Proteomic analysis of Clostridium thermocellum core metabolism: relative protein expression profiles and growth phase-dependent changes in protein expression. BMC Microbiol 12:214. http://dx.doi.org/10.1186/1471-2180-12-214.
    • (2012) BMC Microbiol , vol.12 , pp. 214
    • Rydzak, T.1    McQueen, P.D.2    Krokhin, O.V.3    Spicer, V.4    Ezzati, P.5    Dwivedi, R.C.6    Shamshurin, D.7    Levin, D.B.8    Wilkins, J.A.9    Sparling, R.10
  • 17
    • 79953177901 scopus 로고    scopus 로고
    • Global gene expression patterns in Clostridium thermocellum as determined by microarray analysis of chemostat cultures on cellulose or cellobiose
    • Riederer A, Takasuka TE, Makino S, Stevenson DM, Bukhman YV, Elsen NL, Fox BG. 2011. Global gene expression patterns in Clostridium thermocellum as determined by microarray analysis of chemostat cultures on cellulose or cellobiose. Appl Environ Microbiol 77:1243-1253. http: //dx.doi.org/10.1128/AEM.02008-10.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 1243-1253
    • Riederer, A.1    Takasuka, T.E.2    Makino, S.3    Stevenson, D.M.4    Bukhman, Y.V.5    Elsen, N.L.6    Fox, B.G.7
  • 18
    • 79958270877 scopus 로고    scopus 로고
    • Transcriptomic analysis of Clostridium thermocellum ATCC 27405 cellulose fermentation
    • Raman B, McKeown CK, Rodriguez M, Brown SD, Mielenz JR. 2011. Transcriptomic analysis of Clostridium thermocellum ATCC 27405 cellulose fermentation. BMC Microbiol 11:134. http://dx.doi.org/10.1186 /1471-2180-11-134.
    • (2011) BMC Microbiol , vol.11 , pp. 134
    • Raman, B.1    McKeown, C.K.2    Rodriguez, M.3    Brown, S.D.4    Mielenz, J.R.5
  • 19
  • 21
    • 79953283525 scopus 로고    scopus 로고
    • Marker removal system for Thermoanaerobacterium saccharolyticum and development of a markerless ethanologen
    • Shaw AJ, Covalla SF, Hogsett DA, Herring CD. 2011. Marker removal system for Thermoanaerobacterium saccharolyticum and development of a markerless ethanologen. Appl Environ Microbiol 77:2534-2536. http: //dx.doi.org/10.1128/AEM.01731-10.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 2534-2536
    • Shaw, A.J.1    Covalla, S.F.2    Hogsett, D.A.3    Herring, C.D.4
  • 22
    • 6944242467 scopus 로고    scopus 로고
    • Cloning of L-lactate dehydrogenase and elimination of lactic acid production via gene knockout in Thermoanaerobacterium saccharolyticum JW/SL-YS485
    • Desai SG, Guerinot ML, Lynd LR. 2004. Cloning of L-lactate dehydrogenase and elimination of lactic acid production via gene knockout in Thermoanaerobacterium saccharolyticum JW/SL-YS485. Appl Microbiol Biotechnol 65:600-605. http://dx.doi.org/10.1007/s00253-004-1575-9.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 600-605
    • Desai, S.G.1    Guerinot, M.L.2    Lynd, L.R.3
  • 23
    • 84861156874 scopus 로고    scopus 로고
    • Transformation of Clostridium thermocellum by electroporation
    • Olson DG, Lynd LR. 2012. Transformation of Clostridium thermocellum by electroporation. Methods Enzymol 510:317-330. http://dx.doi.org/10.1016/B978-0-12-415931-0.00017-3.
    • (2012) Methods Enzymol , vol.510 , pp. 317-330
    • Olson, D.G.1    Lynd, L.R.2
  • 25
    • 84872191690 scopus 로고    scopus 로고
    • Dcm methylation is detrimental to plasmid transformation in Clostridium thermocellum
    • Guss AM, Olson DG, Caiazza NC, Lynd LR. 2012. Dcm methylation is detrimental to plasmid transformation in Clostridium thermocellum. Biotechnol Biofuels 5:30. http://dx.doi.org/10.1186/1754-6834-5-30.
    • (2012) Biotechnol Biofuels , vol.5 , pp. 30
    • Guss, A.M.1    Olson, D.G.2    Caiazza, N.C.3    Lynd, L.R.4
  • 29
    • 0033989579 scopus 로고    scopus 로고
    • Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis
    • Gupta S, Mat-Jan F, Latifi M, Clark DP. 2000. Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis. FEMS Microbiol Lett 182:51-55. http: //dx.doi.org/10.1111/j.1574-6968.2000.tb08872.x.
    • (2000) FEMS Microbiol Lett , vol.182 , pp. 51-55
    • Gupta, S.1    Mat-Jan, F.2    Latifi, M.3    Clark, D.P.4
  • 30
    • 0019291045 scopus 로고
    • Ethanol production by thermophilic bacteria: relationship between fermentation product yields of and catabolic enzyme activities in Clostridium thermocellum and Thermoanaerobium brockii
    • Lamed R, Zeikus JG. 1980. Ethanol production by thermophilic bacteria: relationship between fermentation product yields of and catabolic enzyme activities in Clostridium thermocellum and Thermoanaerobium brockii. J Bacteriol 144:569-578.
    • (1980) J Bacteriol , vol.144 , pp. 569-578
    • Lamed, R.1    Zeikus, J.G.2
  • 31
    • 84880826349 scopus 로고    scopus 로고
    • Development and evaluation of methods to infer biosynthesis and substrate consumption in cultures of cellulolytic microorganisms
    • Holwerda EK, Ellis LD, Lynd LR. 2013. Development and evaluation of methods to infer biosynthesis and substrate consumption in cultures of cellulolytic microorganisms. Biotechnol Bioeng 110:2380-2388. http://dx.doi.org/10.1002/bit.24915.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 2380-2388
    • Holwerda, E.K.1    Ellis, L.D.2    Lynd, L.R.3
  • 32
    • 14344260653 scopus 로고    scopus 로고
    • Cloning and expression of the Clostridium thermocellum L-lactate dehydrogenase gene in Escherichia coli and enzyme characterization
    • Ozkan M, Yilmaz EI, Lynd LR, Ozcengiz G, Özkan M, Ebru Y, Özcengiz G. 2004. Cloning and expression of the Clostridium thermocellum L-lactate dehydrogenase gene in Escherichia coli and enzyme characterization. Can J Microbiol 851:845-851. http://dx.doi.org/10.1139/w04-071.
    • (2004) Can J Microbiol , vol.851 , pp. 845-851
    • Ozkan, M.1    Yilmaz, E.I.2    Lynd, L.R.3    Ozcengiz, G.4    Özkan, M.5    Ebru, Y.6    Özcengiz, G.7
  • 33
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication
    • Collins MD, Jones D. 1981. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol Rev 45:316-354.
    • (1981) Microbiol Rev , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 34
    • 0032523196 scopus 로고    scopus 로고
    • Isoprenoid quinone, cellular fatty acid composition and diaminopimelic acid isomers of newly classified thermophilic anaerobic Gram-positive bacteria
    • Yamamoto K, Murakami R, Takamura Y. 1998. Isoprenoid quinone, cellular fatty acid composition and diaminopimelic acid isomers of newly classified thermophilic anaerobic Gram-positive bacteria. FEMS Microbiol Lett 161:351-358. http://dx.doi.org/10.1111/j.1574-6968.1998.tb12968.x.
    • (1998) FEMS Microbiol Lett , vol.161 , pp. 351-358
    • Yamamoto, K.1    Murakami, R.2    Takamura, Y.3
  • 35
    • 84855898276 scopus 로고    scopus 로고
    • Thiosulfate reduction in Salmonella enterica is driven by the proton motive force
    • Stoffels L, Krehenbrink M, Berks BC, Unden G. 2012. Thiosulfate reduction in Salmonella enterica is driven by the proton motive force. J Bacteriol 194:475-485. http://dx.doi.org/10.1128/JB.06014-11.
    • (2012) J Bacteriol , vol.194 , pp. 475-485
    • Stoffels, L.1    Krehenbrink, M.2    Berks, B.C.3    Unden, G.4
  • 36
    • 0027439895 scopus 로고
    • Taxonomic distinction of saccharolytic thermophilic anaerobes: description of Thermoanaerobacterium xylanolyticum gen. nov., sp. nov., and Thermoanaerobacterium saccharolyticum gen. nov., sp. nov.; reclassification of Thermoanaerobium brockii, Clostridium
    • Lee Y-E, Jain MK, Lee C, Zeikus JG. 1993. Taxonomic distinction of saccharolytic thermophilic anaerobes: description of Thermoanaerobacterium xylanolyticum gen. nov., sp. nov., and Thermoanaerobacterium saccharolyticum gen. nov., sp. nov.; reclassification of Thermoanaerobium brockii, Clostridium. Int J Syst Bacteriol 43:41-51. http://dx.doi.org/10.1099/00207713-43-1-41.
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 41-51
    • Lee, Y.-E.1    Jain, M.K.2    Lee, C.3    Zeikus, J.G.4
  • 37
    • 0034284035 scopus 로고    scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the primary alcohol dehydrogenase gene from Thermoanaerobacter ethanolicus JW200
    • Holt PJ, Williams RE, Jordan KN, Lowe CR, Bruce NC. 2000. Cloning, sequencing and expression in Escherichia coli of the primary alcohol dehydrogenase gene from Thermoanaerobacter ethanolicus JW200. FEMS Microbiol Lett 190:57-62. http://dx.doi.org/10.1111/j.1574-6968.2000.tb09262.x.
    • (2000) FEMS Microbiol Lett , vol.190 , pp. 57-62
    • Holt, P.J.1    Williams, R.E.2    Jordan, K.N.3    Lowe, C.R.4    Bruce, N.C.5
  • 38
    • 41149141711 scopus 로고    scopus 로고
    • End-product pathways in the xylose fermenting bacterium, Thermoanaerobacterium saccharolyticum
    • Shaw JA, Jenney FE, Adams MWW, Lynd LR. 2008. End-product pathways in the xylose fermenting bacterium, Thermoanaerobacterium saccharolyticum. Enzyme Microb Technol 42:453-458. http://dx.doi.org /10.1016/j.enzmictec.2008.01.005.
    • (2008) Enzyme Microb Technol , vol.42 , pp. 453-458
    • Shaw, J.A.1    Jenney, F.E.2    Adams, M.W.W.3    Lynd, L.R.4
  • 39
    • 70350455960 scopus 로고    scopus 로고
    • Identification of the [FeFe]-hydrogenase responsible for hydrogen generation in Thermoanaerobacterium saccharolyticum and demonstration of increased ethanol yield via hydrogenase knockout
    • Shaw AJ, Hogsett DA, Lynd LR. 2009. Identification of the [FeFe]-hydrogenase responsible for hydrogen generation in Thermoanaerobacterium saccharolyticum and demonstration of increased ethanol yield via hydrogenase knockout. J Bacteriol 191:6457-6464. http://dx.doi.org/10.1128/JB.00497-09.
    • (2009) J Bacteriol , vol.191 , pp. 6457-6464
    • Shaw, A.J.1    Hogsett, D.A.2    Lynd, L.R.3
  • 40
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution
    • Wigley DB, Gamblin SJ, Turkenburg JP, Dodson EJ, Piontek K, Muirhead H, Holbrook JJ. 1992. Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution. J Mol Biol 223:317-335. http://dx.doi.org/10.1016/0022-2836(92)90733-Z.
    • (1992) J Mol Biol , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7
  • 41
    • 0023221564 scopus 로고
    • A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure
    • Clarke AR, Wigley DB, Barstow DA, Chia WN, Atkinson T, Holbrook JJ. 1987. A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure. Biochim Biophys Acta 913:72-80. http://dx.doi.org/10.1016/0167-4838(87)90234-2.
    • (1987) Biochim Biophys Acta , vol.913 , pp. 72-80
    • Clarke, A.R.1    Wigley, D.B.2    Barstow, D.A.3    Chia, W.N.4    Atkinson, T.5    Holbrook, J.J.6
  • 42
    • 84917691493 scopus 로고    scopus 로고
    • Hydrogen formation and its regulation in Ruminococcus albus: involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non electron-bifurcating [FeFe]-hydrogenase and of a putative hydrogen-sensing [FeFe]-hydrogenase
    • Zheng Y, Kahnt J, Kwon IH, Mackie RI, Thauer RK. 2014. Hydrogen formation and its regulation in Ruminococcus albus: involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non electron-bifurcating [FeFe]-hydrogenase and of a putative hydrogen-sensing [FeFe]-hydrogenase. J Bacteriol 196:3840-3852. http://dx.doi.org/10.1128/JB.02070-14.
    • (2014) J Bacteriol , vol.196 , pp. 3840-3852
    • Zheng, Y.1    Kahnt, J.2    Kwon, I.H.3    Mackie, R.I.4    Thauer, R.K.5
  • 43
    • 67649413347 scopus 로고    scopus 로고
    • The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production
    • Schut GJ, Adams MWW. 2009. The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J Bacteriol 191:4451-4457. http://dx.doi.org/10.1128/JB.01582-08.
    • (2009) J Bacteriol , vol.191 , pp. 4451-4457
    • Schut, G.J.1    Adams, M.W.W.2
  • 44
    • 84903640402 scopus 로고    scopus 로고
    • Insights into electron flux through manipulation of fermentation conditions and assessment of protein expression profiles in Clostridium thermocellum
    • Rydzak T, Grigoryan M, Cunningham ZJ, Krokhin OV, Ezzati P, Cicek N, Levin DB, Wilkins JA, Sparling R. 2014. Insights into electron flux through manipulation of fermentation conditions and assessment of protein expression profiles in Clostridium thermocellum. Appl Microbiol Biotechnol 98:6497-6510. http://dx.doi.org/10.1007/s00253-014-5798-0.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 6497-6510
    • Rydzak, T.1    Grigoryan, M.2    Cunningham, Z.J.3    Krokhin, O.V.4    Ezzati, P.5    Cicek, N.6    Levin, D.B.7    Wilkins, J.A.8    Sparling, R.9
  • 45
    • 0017389068 scopus 로고
    • Fermentation of cellulose and cellobiose by Clostridium thermocellum in the absence of Methanobacterium thermoautotrophicum
    • Weimer P, Zeikus J. 1977. Fermentation of cellulose and cellobiose by Clostridium thermocellum in the absence of Methanobacterium thermoautotrophicum. Appl Environ Microbiol 33:289-297.
    • (1977) Appl Environ Microbiol , vol.33 , pp. 289-297
    • Weimer, P.1    Zeikus, J.2
  • 46
    • 0021207646 scopus 로고
    • Homoacetogenic fermentation of cellulose by a coculture of Clostridium thermocellum and Acetogenium kivui
    • Le Ruyet P, Dubourguier HC, Albagnac G. 1984. Homoacetogenic fermentation of cellulose by a coculture of Clostridium thermocellum and Acetogenium kivui. Appl Environ Microbiol 48:893-895.
    • (1984) Appl Environ Microbiol , vol.48 , pp. 893-895
    • Le Ruyet, P.1    Dubourguier, H.C.2    Albagnac, G.3
  • 48
    • 77957326597 scopus 로고    scopus 로고
    • NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri
    • Wang S, Huang H, Moll J, Thauer RK. 2010. NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri. J Bacteriol 192:5115-5123. http://dx.doi.org/10.1128/JB.00612-10.
    • (2010) J Bacteriol , vol.192 , pp. 5115-5123
    • Wang, S.1    Huang, H.2    Moll, J.3    Thauer, R.K.4


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