메뉴 건너뛰기




Volumn 82, Issue 24, 2016, Pages 7134-7141

Ferredoxin: NAD+ oxidoreductase of Thermoanaerobacterium saccharolyticum and its role in ethanol formation

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; GENES;

EID: 84997496802     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02130-16     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 84876787676 scopus 로고    scopus 로고
    • Plant type ferredoxins and ferredoxin-dependent metabolism
    • Hanke G, Mulo P. 2013. Plant type ferredoxins and ferredoxin-dependent metabolism. Plant Cell Environ 36:1071-1084. http://dx.doi.org/10.1111/pce.12046.
    • (2013) Plant Cell Environ , vol.36 , pp. 1071-1084
    • Hanke, G.1    Mulo, P.2
  • 2
    • 0000133490 scopus 로고
    • Ferredoxins as electrond carriers in photosynthesis and in the biological production and consumption of hydrogen gas
    • Tagawa K, Arnon DI. 1962. Ferredoxins as electrond carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature 195:537-543. http://dx.doi.org/10.1038/195537a0.
    • (1962) Nature , vol.195 , pp. 537-543
    • Tagawa, K.1    Arnon, D.I.2
  • 3
    • 84876863362 scopus 로고    scopus 로고
    • Metabolic engineering of Clostridium acetobutylicum ATCC 824 for the high-yield production of a biofuel composed of an isopropanol/butanol/ethanol mixture
    • Dusséaux S, Croux C, Soucaille P, Meynial-Salles I. 2013. Metabolic engineering of Clostridium acetobutylicum ATCC 824 for the high-yield production of a biofuel composed of an isopropanol/butanol/ethanol mixture. Metab Eng 18:1-8. http://dx.doi.org/10.1016/j.ymben.2013.03.003.
    • (2013) Metab Eng , vol.18 , pp. 1-8
    • Dusséaux, S.1    Croux, C.2    Soucaille, P.3    Meynial-Salles, I.4
  • 4
    • 70349971135 scopus 로고    scopus 로고
    • Metabolic pathways of clostridia for producing butanol
    • Gheshlaghi R, Scharer JM, Moo-Young M, Chou CP. 2009. Metabolic pathways of clostridia for producing butanol. Biotechnol Adv 27:764-781. http://dx.doi.org/10.1016/j.biotechadv.2009.06.002.
    • (2009) Biotechnol Adv , vol.27 , pp. 764-781
    • Gheshlaghi, R.1    Scharer, J.M.2    Moo-Young, M.3    Chou, C.P.4
  • 5
    • 0036010144 scopus 로고    scopus 로고
    • The role of glutamine synthetase and glutamate dehydrogenase in nitrogen assimilation and possibilities for improvement in the nitrogen utilization of crops
    • Miflin BJ, Habash DZ. 2002. The role of glutamine synthetase and glutamate dehydrogenase in nitrogen assimilation and possibilities for improvement in the nitrogen utilization of crops. J Exp Bot 53:979-987. http://dx.doi.org/10.1093/jexbot/53.370.979.
    • (2002) J Exp Bot , vol.53 , pp. 979-987
    • Miflin, B.J.1    Habash, D.Z.2
  • 6
    • 0034981635 scopus 로고    scopus 로고
    • Role of a ferredoxin gene cotranscribed with the nifHDK operon in N2 fixation and nitrogenase "switch-off" of Azoarcus sp. strain BH72
    • Egener T, Martin DE, Sarkar A, Reinhold-Hurek B. 2001. Role of a ferredoxin gene cotranscribed with the nifHDK operon in N2 fixation and nitrogenase "switch-off" of Azoarcus sp. strain BH72. J Bacteriol 183: 3752-3760. http://dx.doi.org/10.1128/JB.183.12.3752-3760.2001.
    • (2001) J Bacteriol , vol.183 , pp. 3752-3760
    • Egener, T.1    Martin, D.E.2    Sarkar, A.3    Reinhold-Hurek, B.4
  • 7
    • 84937516584 scopus 로고    scopus 로고
    • Development of a synthetic pathway to convert glucose to hydrogen using cell free extracts
    • Lu F, Smith PR, Mehta K, Swartz JR. 2015. Development of a synthetic pathway to convert glucose to hydrogen using cell free extracts. Int J Hydrogen Energy 40:9113-9124. http://dx.doi.org/10.1016/j.ijhydene.2015.05.121.
    • (2015) Int J Hydrogen Energy , vol.40 , pp. 9113-9124
    • Lu, F.1    Smith, P.R.2    Mehta, K.3    Swartz, J.R.4
  • 8
    • 84874639721 scopus 로고    scopus 로고
    • The Rnf complex of Clostridium ljungdahlii is a proton-translocating ferredoxin:NAD+ oxidoreductase essential for autotrophic growth
    • Tremblay P, Zhang T, Dar SA. 2012. The Rnf complex of Clostridium ljungdahlii is a proton-translocating ferredoxin:NAD+ oxidoreductase essential for autotrophic growth. mBio 4:e0040612. http://dx.doi.org/10.1128/mBio.00406-12.
    • (2012) mBio , vol.4
    • Tremblay, P.1    Zhang, T.2    Dar, S.A.3
  • 9
    • 84887087494 scopus 로고    scopus 로고
    • The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential
    • Hess V, Schuchmann K, Muller V. 2013. The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential. J Biol Chem 288: 31496-31502. http://dx.doi.org/10.1074/jbc.M113.510255.
    • (2013) J Biol Chem , vol.288 , pp. 31496-31502
    • Hess, V.1    Schuchmann, K.2    Muller, V.3
  • 10
    • 77957326597 scopus 로고    scopus 로고
    • NADP+ reduction with reduced ferredoxin and NADP+ reduction withNADHare 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 withNADHare 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
  • 11
    • 0034990899 scopus 로고    scopus 로고
    • Ferredoxin:NADP oxidoreductase from Pyro-coccus furiosus
    • Ma K, Adams MW. 2001. Ferredoxin:NADP oxidoreductase from Pyro-coccus furiosus. Methods Enzymol 334:40-45. http://dx.doi.org/10.1016/S0076-6879(01)34456-7.
    • (2001) Methods Enzymol , vol.334 , pp. 40-45
    • Ma, K.1    Adams, M.W.2
  • 12
    • 84905462797 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus
    • Skråmo S, Hersleth H-P, Hammerstad M, Andersson KK, Røhr ÅK. 2014. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus. Acta Crystallogr F Struct Biol Commun 70:777-780. http://dx.doi.org/10.1107/S2053230X14008334.
    • (2014) Acta Crystallogr F Struct Biol Commun , vol.70 , pp. 777-780
    • Skråmo, S.1    Hersleth, H.-P.2    Hammerstad, M.3    Andersson, K.K.4    Røhr, Å.K.5
  • 13
    • 78649656536 scopus 로고    scopus 로고
    • Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivity
    • Komori H, Seo D, Sakurai T, Higuchi Y. 2010. Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivity. Protein Sci 19:2279-2290. http://dx.doi.org/10.1002/pro.508.
    • (2010) Protein Sci , vol.19 , pp. 2279-2290
    • Komori, H.1    Seo, D.2    Sakurai, T.3    Higuchi, Y.4
  • 14
    • 77955279244 scopus 로고    scopus 로고
    • Asymmetric dimeric structure of ferredoxin-NAD(P)+ oxidoreductase from the green sulfur bacterium Chlorobaculum tepidum: implications for binding ferredoxin and NADP+
    • Muraki N, Seo D, Shiba T, Sakurai T, Kurisu G. 2010. Asymmetric dimeric structure of ferredoxin-NAD(P)+ oxidoreductase from the green sulfur bacterium Chlorobaculum tepidum: implications for binding ferredoxin and NADP_. J Mol Biol 401:403-414. http://dx.doi.org/10.1016/j.jmb.2010.06.024.
    • (2010) J Mol Biol , vol.401 , pp. 403-414
    • Muraki, N.1    Seo, D.2    Shiba, T.3    Sakurai, T.4    Kurisu, G.5
  • 15
    • 84871712835 scopus 로고    scopus 로고
    • Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
    • Buckel W, Thauer RK. 2013. Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation. Biochim Biophys Acta 1827:94-113. http://dx.doi.org/10.1016/j.bbabio.2012.07.002.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 94-113
    • Buckel, W.1    Thauer, R.K.2
  • 17
    • 79951579402 scopus 로고    scopus 로고
    • Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes
    • Biegel E, Schmidt S, González JM, Müller V. 2011. Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes. Cell Mol Life Sci 68:613-634. http://dx.doi.org/10.1007/s00018-010-0555-8.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 613-634
    • Biegel, E.1    Schmidt, S.2    González, J.M.3    Müller, V.4
  • 18
    • 78149247216 scopus 로고    scopus 로고
    • Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase
    • Biegel E, Müller V. 2010. Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase. Proc Natl Acad Sci U S A 107:18138-18142. http://dx.doi.org/10.1073/pnas.1010318107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18138-18142
    • Biegel, E.1    Müller, V.2
  • 19
  • 20
    • 84941312535 scopus 로고    scopus 로고
    • Insights into flavin-based electron bifurcation via the NADHdependent reduced ferredoxin:NADP oxidoreductase structure
    • Demmer JK, Huang H, Wang S, Demmer U, Thauer RK, Ermler U. 2015. Insights into flavin-based electron bifurcation via the NADHdependent reduced ferredoxin:NADP oxidoreductase structure. J Biol Chem 290:21985-21995. http://dx.doi.org/10.1074/jbc.M115.656520.
    • (2015) J Biol Chem , vol.290 , pp. 21985-21995
    • Demmer, J.K.1    Huang, H.2    Wang, S.3    Demmer, U.4    Thauer, R.K.5    Ermler, U.6
  • 22
    • 84936991306 scopus 로고    scopus 로고
    • Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutants of Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
    • Zheng T, Olson DG, Tian L, Bomble YJ, Himmel ME, Lo J, Hon S, Shaw AJ, van Dijken JP, Lynd LR. 2015. Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutants of Clostridium thermocellum and Thermoanaerobacterium saccharolyticum. J Bacteriol 197:2610-2619. http://dx.doi.org/10.1128/JB.00232-15.
    • (2015) J Bacteriol , vol.197 , pp. 2610-2619
    • Zheng, T.1    Olson, D.G.2    Tian, L.3    Bomble, Y.J.4    Himmel, M.E.5    Lo, J.6    Hon, S.7    Shaw, A.J.8    van Dijken, J.P.9    Lynd, L.R.10
  • 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
    • 84924067126 scopus 로고    scopus 로고
    • The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
    • Lo J, Zheng T, Hon S, Olson DG, Lynd LR. 2015. The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum. J Bacteriol 197:1386-1393. http://dx.doi.org/10.1128/JB.02450-14.
    • (2015) J Bacteriol , vol.197 , pp. 1386-1393
    • Lo, J.1    Zheng, T.2    Hon, S.3    Olson, D.G.4    Lynd, L.R.5
  • 26
    • 84969504536 scopus 로고    scopus 로고
    • A markerless gene deletion and integration system for Thermoanaerobacter ethanolicus
    • Shao X, Zhou J, Olson DG, Lynd LR. 2016. A markerless gene deletion and integration system for Thermoanaerobacter ethanolicus. Biotechnol Biofuels 9:100. http://dx.doi.org/10.1186/s13068-016-0514-1.
    • (2016) Biotechnol Biofuels , vol.9 , pp. 100
    • Shao, X.1    Zhou, J.2    Olson, D.G.3    Lynd, L.R.4
  • 27
    • 77954732186 scopus 로고    scopus 로고
    • Natural competence in Thermoanaerobacter and Thermoanaerobacterium species
    • Shaw AJ, Hogsett DA, Lynd LR. 2010. Natural competence in Thermoanaerobacter and Thermoanaerobacterium species. Appl Environ Microbiol 76:4713-4719. http://dx.doi.org/10.1128/AEM.00402-10.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4713-4719
    • Shaw, A.J.1    Hogsett, D.A.2    Lynd, L.R.3
  • 28
    • 0032725568 scopus 로고    scopus 로고
    • Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-0RF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli
    • Takahashi Y, Nakamura M. 1999. Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-0RF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J Biochem 126:917-926. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022535.
    • (1999) J Biochem , vol.126 , pp. 917-926
    • Takahashi, Y.1    Nakamura, M.2
  • 29
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster
    • Nakamura M, Saeki K, Takahashi Y. 1999. Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. J Biochem 126:10-18. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022409.
    • (1999) J Biochem , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 30
    • 84953875121 scopus 로고    scopus 로고
    • Heterologous overproduction of 2[4Fe4S]-and [2Fe2S]-type clostridial ferredoxins and [2Fe2S]-type agrobacterial ferredoxin
    • Huang H, Hu L, Yu W, Li H, Tao F, Xie H, Wang S. 2016. Heterologous overproduction of 2[4Fe4S]-and [2Fe2S]-type clostridial ferredoxins and [2Fe2S]-type agrobacterial ferredoxin. Protein Expr Purif 121:1-8. http://dx.doi.org/10.1016/j.pep.2015.12.019.
    • (2016) Protein Expr Purif , vol.121 , pp. 1-8
    • Huang, H.1    Hu, L.2    Yu, W.3    Li, H.4    Tao, F.5    Xie, H.6    Wang, S.7
  • 31
    • 36749053439 scopus 로고    scopus 로고
    • Carbon dioxide activation at the Ni,Fecluster of anaerobic carbon monoxide dehydrogenase
    • Jeoung J-H, Dobbek H. 2007. Carbon dioxide activation at the Ni,Fecluster of anaerobic carbon monoxide dehydrogenase. Science 318:1461-1464. http://dx.doi.org/10.1126/science.1148481.
    • (2007) Science , vol.318 , pp. 1461-1464
    • Jeoung, J.-H.1    Dobbek, H.2
  • 32
    • 84941563834 scopus 로고    scopus 로고
    • Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SLYS485
    • Zhou J, Olson DG, Lanahan AA, Tian L, Murphy SJ-L, Lo J, Lynd LR. 2015. Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SLYS485. Biotechnol Biofuels 8:138. http://dx.doi.org/10.1186/s13068-015-0304-1.
    • (2015) Biotechnol Biofuels , vol.8 , pp. 138
    • Zhou, J.1    Olson, D.G.2    Lanahan, A.A.3    Tian, L.4    Murphy, S.J.-L.5    Lo, J.6    Lynd, L.R.7
  • 34
    • 84874397485 scopus 로고    scopus 로고
    • Functional heterologous expression of an engineered full length CipA from Clostridium thermocellum in Thermoanaerobacterium saccharolyticum
    • Currie DH, Herring CD, Guss AM, Olson DG, Hogsett DA, Lynd LR. 2013. Functional heterologous expression of an engineered full length CipA from Clostridium thermocellum in Thermoanaerobacterium saccharolyticum. Biotechnol Biofuels 6:32. http://dx.doi.org/10.1186/1754-6834-6-32.
    • (2013) Biotechnol Biofuels , vol.6 , pp. 32
    • Currie, D.H.1    Herring, C.D.2    Guss, A.M.3    Olson, D.G.4    Hogsett, D.A.5    Lynd, L.R.6
  • 35
    • 0010184353 scopus 로고    scopus 로고
    • Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster
    • Rowland P, Nørager S, Jensen KF, Larsen S. 2000. Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster. Structure 8:1227-1238. http://dx.doi.org/10.1016/S0969-2126(00)00530-X.
    • (2000) Structure , vol.8 , pp. 1227-1238
    • Rowland, P.1    Nørager, S.2    Jensen, K.F.3    Larsen, S.4
  • 36
    • 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
  • 37
    • 84924047011 scopus 로고    scopus 로고
    • Ethanol production by engineered thermophiles
    • Olson DG, Sparling R, Lynd LR. 2015. Ethanol production by engineered thermophiles. Curr Opin Biotechnol 33:130-141. http://dx.doi.org/10.1016/j.copbio.2015.02.006.
    • (2015) Curr Opin Biotechnol , vol.33 , pp. 130-141
    • Olson, D.G.1    Sparling, R.2    Lynd, L.R.3
  • 38
    • 84997226657 scopus 로고    scopus 로고
    • Development of a plasmid-based expression system in Clostridium thermocellum and its use to screen heterologous expression of bifunctional alcohol dehydrogenases (adhEs)
    • Hon S, Lanahan AA, Tian L, Giannone RJ, Hettich RL, Olson DG, Lynd LR. 2016. Development of a plasmid-based expression system in Clostridium thermocellum and its use to screen heterologous expression of bifunctional alcohol dehydrogenases (adhEs). Metab Eng Commun 3:120-129. http://dx.doi.org/10.1016/j.meteno.2016.04.001.
    • (2016) Metab Eng Commun , vol.3 , pp. 120-129
    • Hon, S.1    Lanahan, A.A.2    Tian, L.3    Giannone, R.J.4    Hettich, R.L.5    Olson, D.G.6    Lynd, L.R.7
  • 39
    • 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
  • 40
    • 0030887230 scopus 로고    scopus 로고
    • Transformation of Thermoanaerobacterium sp. strain JW/SL-YS485 with plasmid pIKM1 conferring kanamycin resistance
    • Mai V, Lorenz WW, Wiegel J. 2006. Transformation of Thermoanaerobacterium sp. strain JW/SL-YS485 with plasmid pIKM1 conferring kanamycin resistance. FEMS Microbiol Lett 148:163-167. http://dx.doi.org/10.1111/j.1574-6968.1997.tb10283.x.
    • (2006) FEMS Microbiol Lett , vol.148 , pp. 163-167
    • Mai, V.1    Lorenz, W.W.2    Wiegel, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.