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Volumn 13, Issue 1, 2012, Pages

The genome of Pelobacter carbinolicus reveals surprising metabolic capabilities and physiological features

Author keywords

2,3 butanediol; Genome; Geobacter; Metabolism; Pelobacter; Physiology

Indexed keywords

2,3 BUTANEDIOL; ACETOIN; ALCOHOL; ASPARAGINE; ASPARTATE AMMONIA LIGASE; CHOLINE; ETHANOLAMINE; ETHYLENE GLYCOL; GLUTAMATE DEHYDROGENASE; GLYCEROL; IRON HYDROGENASE; NANOWIRE; OXIDOREDUCTASE; PHOSPHOTRANSFERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRANSFER RNA;

EID: 84872415073     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-13-690     Document Type: Article
Times cited : (31)

References (105)
  • 1
    • 0021368804 scopus 로고
    • Fermentation of 2,3-butanediol by Pelobacter carbinolicus sp. nov. and Pelobacter propionicus sp. nov., and evidence for propionate formation from C2 compounds
    • Schink B. Fermentation of 2,3-butanediol by Pelobacter carbinolicus sp. nov. and Pelobacter propionicus sp. nov., and evidence for propionate formation from C2 compounds. Arch Microbiol 1984, 137(1):33-41.
    • (1984) Arch Microbiol , vol.137 , Issue.1 , pp. 33-41
    • Schink, B.1
  • 3
    • 5444244948 scopus 로고    scopus 로고
    • Comparison of 16S rRNA, nifD, recA, gyrB, rpoB and fusA genes within the family Geobacteraceae fam. nov
    • Holmes DE, Nevin KP, Lovley DR. Comparison of 16S rRNA, nifD, recA, gyrB, rpoB and fusA genes within the family Geobacteraceae fam. nov. Int J Syst Evol Microbiol 2004, 54(Pt 5):1591-1599.
    • (2004) Int J Syst Evol Microbiol , vol.54 , Issue.PART 5 , pp. 1591-1599
    • Holmes, D.E.1    Nevin, K.P.2    Lovley, D.R.3
  • 5
    • 0028077780 scopus 로고
    • Phylogenetic analysis of five strains of gram-negative, obligately anaerobic, sulfur-reducing bacteria and description of Desulfuromusa gen. nov., including Desulfuromusa kysingii sp. nov., Desulfuromusa bakii sp. nov., and Desulfuromusa succinoxidans sp. nov
    • Liesack W, Finster K. Phylogenetic analysis of five strains of gram-negative, obligately anaerobic, sulfur-reducing bacteria and description of Desulfuromusa gen. nov., including Desulfuromusa kysingii sp. nov., Desulfuromusa bakii sp. nov., and Desulfuromusa succinoxidans sp. nov. Int J Syst Bacteriol 1994, 44:753-758.
    • (1994) Int J Syst Bacteriol , vol.44 , pp. 753-758
    • Liesack, W.1    Finster, K.2
  • 6
    • 0001852583 scopus 로고    scopus 로고
    • Fe(III) and Mn(IV) reduction
    • Washington DC: American Society forMicrobiology, Lovley DR
    • Lovley DR. Fe(III) and Mn(IV) reduction. Environmental Microbe-Metal Interactions 2000, 3-29. Washington DC: American Society forMicrobiology, Lovley DR.
    • (2000) Environmental Microbe-Metal Interactions , pp. 3-29
    • Lovley, D.R.1
  • 7
    • 84963626037 scopus 로고
    • The phylogenetic status of Pelobacter acidigallici, Pelobacter venetianus, and Pelobacter carbinolicus
    • Stackebrandt E, Wehmeyer U, Schink B. The phylogenetic status of Pelobacter acidigallici, Pelobacter venetianus, and Pelobacter carbinolicus. Syst Appl Microbiol 1989, 11:257-260.
    • (1989) Syst Appl Microbiol , vol.11 , pp. 257-260
    • Stackebrandt, E.1    Wehmeyer, U.2    Schink, B.3
  • 9
    • 47749111026 scopus 로고    scopus 로고
    • Genome-wide gene expression patterns and growth requirements suggest that Pelobacter carbinolicus reduces Fe(III) indirectly via sulfide production
    • 10.1128/AEM.02901-07, 2493185, 18515480
    • Haveman SA, DiDonato RJ, Villanueva L, Shelobolina ES, Postier BL, Xu B, Liu A, Lovley DR. Genome-wide gene expression patterns and growth requirements suggest that Pelobacter carbinolicus reduces Fe(III) indirectly via sulfide production. Appl Environ Microbiol 2008, 74(14):4277-4284. 10.1128/AEM.02901-07, 2493185, 18515480.
    • (2008) Appl Environ Microbiol , vol.74 , Issue.14 , pp. 4277-4284
    • Haveman, S.A.1    DiDonato, R.J.2    Villanueva, L.3    Shelobolina, E.S.4    Postier, B.L.5    Xu, B.6    Liu, A.7    Lovley, D.R.8
  • 10
    • 78650389698 scopus 로고    scopus 로고
    • Constraint-based modeling analysis of the metabolism of two Pelobacter species
    • 10.1186/1752-0509-4-174, 3022650, 21182788
    • Sun J, Haveman SA, Bui O, Fahland TR, Lovley DR. Constraint-based modeling analysis of the metabolism of two Pelobacter species. BMC Syst Biol 2010, 4:174. 10.1186/1752-0509-4-174, 3022650, 21182788.
    • (2010) BMC Syst Biol , vol.4 , pp. 174
    • Sun, J.1    Haveman, S.A.2    Bui, O.3    Fahland, T.R.4    Lovley, D.R.5
  • 11
    • 65249191289 scopus 로고    scopus 로고
    • Evolution from a respiratory ancestor to fill syntrophic and fermentative niches: comparative fenomics of six Geobacteraceae species
    • 10.1186/1471-2164-10-103, 2669807, 19284579
    • Butler JE, Young ND, Lovley DR. Evolution from a respiratory ancestor to fill syntrophic and fermentative niches: comparative fenomics of six Geobacteraceae species. BMC Genomics 2009, 10:103. 10.1186/1471-2164-10-103, 2669807, 19284579.
    • (2009) BMC Genomics , vol.10 , pp. 103
    • Butler, J.E.1    Young, N.D.2    Lovley, D.R.3
  • 12
    • 77954948121 scopus 로고    scopus 로고
    • Interference with histidyl-tRNA synthetase by a CRISPR spacer sequence as a factor in the evolution of Pelobacter carbinolicus
    • 10.1186/1471-2148-10-230, 2923632, 20667132
    • Aklujkar M, Lovley DR. Interference with histidyl-tRNA synthetase by a CRISPR spacer sequence as a factor in the evolution of Pelobacter carbinolicus. BMC Evol Biol 2010, 10:230. 10.1186/1471-2148-10-230, 2923632, 20667132.
    • (2010) BMC Evol Biol , vol.10 , pp. 230
    • Aklujkar, M.1    Lovley, D.R.2
  • 13
    • 0030926016 scopus 로고    scopus 로고
    • The human RNA 3′-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea
    • 10.1093/emboj/16.10.2955, 1169903, 9184239
    • Genschik P, Billy E, Swianiewicz M, Filipowicz W. The human RNA 3′-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J 1997, 16(10):2955-2967. 10.1093/emboj/16.10.2955, 1169903, 9184239.
    • (1997) EMBO J , vol.16 , Issue.10 , pp. 2955-2967
    • Genschik, P.1    Billy, E.2    Swianiewicz, M.3    Filipowicz, W.4
  • 14
    • 79953128577 scopus 로고    scopus 로고
    • RtcB is the RNA ligase component of an Escherichia coli RNA repair operon
    • 10.1074/jbc.C111.219022, 3048659, 21224389
    • Tanaka N, Shuman S. RtcB is the RNA ligase component of an Escherichia coli RNA repair operon. J Biol Chem 2011, 286(10):7727-7731. 10.1074/jbc.C111.219022, 3048659, 21224389.
    • (2011) J Biol Chem , vol.286 , Issue.10 , pp. 7727-7731
    • Tanaka, N.1    Shuman, S.2
  • 15
    • 0032566718 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli RNA 3′-terminal phosphate cyclase and its sigma54-regulated operon
    • 10.1074/jbc.273.39.25516, 9738023
    • Genschik P, Drabikowski K, Filipowicz W. Characterization of the Escherichia coli RNA 3′-terminal phosphate cyclase and its sigma54-regulated operon. J Biol Chem 1998, 273(39):25516-25526. 10.1074/jbc.273.39.25516, 9738023.
    • (1998) J Biol Chem , vol.273 , Issue.39 , pp. 25516-25526
    • Genschik, P.1    Drabikowski, K.2    Filipowicz, W.3
  • 16
    • 0030025487 scopus 로고    scopus 로고
    • An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • 10.1093/oxfordjournals.jbchem.a021198, 8907187
    • Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem 1996, 119(1):135-144. 10.1093/oxfordjournals.jbchem.a021198, 8907187.
    • (1996) J Biochem , vol.119 , Issue.1 , pp. 135-144
    • Okamoto, A.1    Kato, R.2    Masui, R.3    Yamagishi, A.4    Oshima, T.5    Kuramitsu, S.6
  • 17
    • 0037022651 scopus 로고    scopus 로고
    • Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation
    • 10.1073/pnas.012027399, 122407, 11880622
    • Min B, Pelaschier JT, Graham DE, Tumbula-Hansen D, Soll D. Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation. Proc Natl Acad Sci USA 2002, 99(5):2678-2683. 10.1073/pnas.012027399, 122407, 11880622.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.5 , pp. 2678-2683
    • Min, B.1    Pelaschier, J.T.2    Graham, D.E.3    Tumbula-Hansen, D.4    Soll, D.5
  • 18
    • 77951402073 scopus 로고
    • [Degradation metabolism of 2-3 butanediol and of acetoin by microorganisms; considerations on Neisseria winogradskyi. I. Investigations on 2-3 butanediol dehydrogenase]
    • Aubert JP, Gavard R. [Degradation metabolism of 2-3 butanediol and of acetoin by microorganisms; considerations on Neisseria winogradskyi. I. Investigations on 2-3 butanediol dehydrogenase]. Ann Inst Pasteur (Paris) 1953, 84(4):735-744.
    • (1953) Ann Inst Pasteur (Paris) , vol.84 , Issue.4 , pp. 735-744
    • Aubert, J.P.1    Gavard, R.2
  • 19
    • 84872403094 scopus 로고
    • Studies on the bacterial oxidation of 2,3-butanediol and related compounds
    • Stanier RY, Fratkin SB. Studies on the bacterial oxidation of 2,3-butanediol and related compounds. Can J Res 1944, 22b(5):140-153.
    • (1944) Can J Res , vol.22 b , Issue.5 , pp. 140-153
    • Stanier, R.Y.1    Fratkin, S.B.2
  • 20
    • 0001112921 scopus 로고
    • Stereoisomeric specificities of 2,3-butanediol dehydrogenases
    • 10.1016/0006-3002(60)90197-9, 13837186
    • Taylor MB, Juni E. Stereoisomeric specificities of 2,3-butanediol dehydrogenases. Biochim Biophys Acta 1960, 39:448-457. 10.1016/0006-3002(60)90197-9, 13837186.
    • (1960) Biochim Biophys Acta , vol.39 , pp. 448-457
    • Taylor, M.B.1    Juni, E.2
  • 21
    • 70349759561 scopus 로고    scopus 로고
    • Biotechnological production of 2,3-butanediol-current state and prospects
    • 10.1016/j.biotechadv.2009.05.002, 19442714
    • Celinska E, Grajek W. Biotechnological production of 2,3-butanediol-current state and prospects. Biotechnol Adv 2009, 27(6):715-725. 10.1016/j.biotechadv.2009.05.002, 19442714.
    • (2009) Biotechnol Adv , vol.27 , Issue.6 , pp. 715-725
    • Celinska, E.1    Grajek, W.2
  • 22
    • 79952694448 scopus 로고    scopus 로고
    • Microbial 2,3-butanediol production: a state-of-the-art review
    • 10.1016/j.biotechadv.2011.01.007, 21272631
    • Ji XJ, Huang H, Ouyang PK. Microbial 2,3-butanediol production: a state-of-the-art review. Biotechnol Adv 2011, 29(3):351-364. 10.1016/j.biotechadv.2011.01.007, 21272631.
    • (2011) Biotechnol Adv , vol.29 , Issue.3 , pp. 351-364
    • Ji, X.J.1    Huang, H.2    Ouyang, P.K.3
  • 23
    • 0017884543 scopus 로고
    • Bacterial 2,3-butanediol dehydrogenases
    • 10.1007/BF00406037, 25056
    • Hohn-Bentz H, Radler F. Bacterial 2,3-butanediol dehydrogenases. Arch Microbiol 1978, 116(2):197-203. 10.1007/BF00406037, 25056.
    • (1978) Arch Microbiol , vol.116 , Issue.2 , pp. 197-203
    • Hohn-Bentz, H.1    Radler, F.2
  • 24
    • 0001170661 scopus 로고
    • Mechanism for the formation of 2,3-butanediol stereoisomers in Bacillus polymyxa
    • Ui S, Masuda T, Masuda H, Muraki H. Mechanism for the formation of 2,3-butanediol stereoisomers in Bacillus polymyxa. J Ferment Technol 1986, 64(6):481-486.
    • (1986) J Ferment Technol , vol.64 , Issue.6 , pp. 481-486
    • Ui, S.1    Masuda, T.2    Masuda, H.3    Muraki, H.4
  • 25
    • 79960086791 scopus 로고    scopus 로고
    • Novel (2R,3R)-2,3-butanediol dehydrogenase from potential industrial strain Paenibacillus polymyxa ATCC 12321
    • 10.1128/AEM.02998-10, 3131630, 21531839
    • Yu B, Sun J, Bommareddy RR, Song L, Zeng AP. Novel (2R,3R)-2,3-butanediol dehydrogenase from potential industrial strain Paenibacillus polymyxa ATCC 12321. Appl Environ Microbiol 2011, 77(12):4230-4233. 10.1128/AEM.02998-10, 3131630, 21531839.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.12 , pp. 4230-4233
    • Yu, B.1    Sun, J.2    Bommareddy, R.R.3    Song, L.4    Zeng, A.P.5
  • 26
    • 55949101810 scopus 로고    scopus 로고
    • The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase
    • 10.1128/AEM.00881-08, 2583490, 18820069
    • Nicholson WL. The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase. Appl Environ Microbiol 2008, 74(22):6832-6838. 10.1128/AEM.00881-08, 2583490, 18820069.
    • (2008) Appl Environ Microbiol , vol.74 , Issue.22 , pp. 6832-6838
    • Nicholson, W.L.1
  • 27
    • 70349290656 scopus 로고    scopus 로고
    • Enantioselective synthesis of pure (R,R)-2,3-butanediol in Escherichia coli with stereospecific secondary alcohol dehydrogenases
    • 10.1039/b913501d, 19763290
    • Yan Y, Lee CC, Liao JC. Enantioselective synthesis of pure (R,R)-2,3-butanediol in Escherichia coli with stereospecific secondary alcohol dehydrogenases. Org Biomol Chem 2009, 7(19):3914-3917. 10.1039/b913501d, 19763290.
    • (2009) Org Biomol Chem , vol.7 , Issue.19 , pp. 3914-3917
    • Yan, Y.1    Lee, C.C.2    Liao, J.C.3
  • 28
    • 0342940779 scopus 로고    scopus 로고
    • Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli
    • Ui S, Okajima Y, Mimura A, Kanai H, Kobayashi T, Kudo T. Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli. J Ferment Bioeng 1997, 83(1):32-37.
    • (1997) J Ferment Bioeng , vol.83 , Issue.1 , pp. 32-37
    • Ui, S.1    Okajima, Y.2    Mimura, A.3    Kanai, H.4    Kobayashi, T.5    Kudo, T.6
  • 29
    • 0344936648 scopus 로고    scopus 로고
    • Cloning, expression and nucleotide sequence of the L-2,3-butanediol dehydrogenase gene from Brevibacterium saccharolyticum C-1012
    • Ui S, Otagiri M, Mimura A, Dohmae N, Takio K, Ohkuma M, Kudo T. Cloning, expression and nucleotide sequence of the L-2,3-butanediol dehydrogenase gene from Brevibacterium saccharolyticum C-1012. J Ferment Bioeng 1998, 86:290-295.
    • (1998) J Ferment Bioeng , vol.86 , pp. 290-295
    • Ui, S.1    Otagiri, M.2    Mimura, A.3    Dohmae, N.4    Takio, K.5    Ohkuma, M.6    Kudo, T.7
  • 30
    • 71549166006 scopus 로고    scopus 로고
    • Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
    • 10.1016/j.febslet.2009.11.068, 19941855
    • Otagiri M, Ui S, Takusagawa Y, Ohtsuki T, Kurisu G, Kusunoki M. Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases. FEBS Lett 2010, 584(1):219-223. 10.1016/j.febslet.2009.11.068, 19941855.
    • (2010) FEBS Lett , vol.584 , Issue.1 , pp. 219-223
    • Otagiri, M.1    Ui, S.2    Takusagawa, Y.3    Ohtsuki, T.4    Kurisu, G.5    Kusunoki, M.6
  • 31
    • 0035116878 scopus 로고    scopus 로고
    • Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms
    • 10.1093/oxfordjournals.jbchem.a002845, 11173520
    • Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M. Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms. J Biochem 2001, 129(2):205-208. 10.1093/oxfordjournals.jbchem.a002845, 11173520.
    • (2001) J Biochem , vol.129 , Issue.2 , pp. 205-208
    • Otagiri, M.1    Kurisu, G.2    Ui, S.3    Takusagawa, Y.4    Ohkuma, M.5    Kudo, T.6    Kusunoki, M.7
  • 32
    • 0022483598 scopus 로고
    • Characterization of two strains of Pelobacter carbinolicus isolated from anaerobic digesters
    • Dubourguier HC, Samain E, Prensier G, Albagnac G. Characterization of two strains of Pelobacter carbinolicus isolated from anaerobic digesters. Arch Microbiol 1986, 145:248-253.
    • (1986) Arch Microbiol , vol.145 , pp. 248-253
    • Dubourguier, H.C.1    Samain, E.2    Prensier, G.3    Albagnac, G.4
  • 33
    • 0028157328 scopus 로고
    • Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
    • 205071, 8110297
    • Oppermann FB, Steinbuchel A. Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J Bacteriol 1994, 176(2):469-485. 205071, 8110297.
    • (1994) J Bacteriol , vol.176 , Issue.2 , pp. 469-485
    • Oppermann, F.B.1    Steinbuchel, A.2
  • 34
    • 0035089028 scopus 로고    scopus 로고
    • Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis
    • 10.1128/JB.183.8.2497-2504.2001, 95166, 11274109
    • Ali NO, Bignon J, Rapoport G, Debarbouille M. Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J Bacteriol 2001, 183(8):2497-2504. 10.1128/JB.183.8.2497-2504.2001, 95166, 11274109.
    • (2001) J Bacteriol , vol.183 , Issue.8 , pp. 2497-2504
    • Ali, N.O.1    Bignon, J.2    Rapoport, G.3    Debarbouille, M.4
  • 35
    • 0026719281 scopus 로고
    • Identification of acoR, a regulatory gene for the expression of genes essential for acetoin catabolism in Alcaligenes eutrophus H16
    • 206224, 1378052
    • Kruger N, Steinbuchel A. Identification of acoR, a regulatory gene for the expression of genes essential for acetoin catabolism in Alcaligenes eutrophus H16. J Bacteriol 1992, 174(13):4391-4400. 206224, 1378052.
    • (1992) J Bacteriol , vol.174 , Issue.13 , pp. 4391-4400
    • Kruger, N.1    Steinbuchel, A.2
  • 36
    • 0022382034 scopus 로고
    • Fermentation of primary alcohols and diols and pure culture of syntrophically alcohol-oxidizing anaerobes
    • Eichler B, Schink B. Fermentation of primary alcohols and diols and pure culture of syntrophically alcohol-oxidizing anaerobes. Arch Microbiol 1985, 143:60-66.
    • (1985) Arch Microbiol , vol.143 , pp. 60-66
    • Eichler, B.1    Schink, B.2
  • 37
    • 0037966959 scopus 로고    scopus 로고
    • Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum
    • 10.1073/pnas.0734105100, 154289, 12704244
    • Raynaud C, Sarcabal P, Meynial-Salles I, Croux C, Soucaille P. Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum. Proc Natl Acad Sci USA 2003, 100(9):5010-5015. 10.1073/pnas.0734105100, 154289, 12704244.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.9 , pp. 5010-5015
    • Raynaud, C.1    Sarcabal, P.2    Meynial-Salles, I.3    Croux, C.4    Soucaille, P.5
  • 38
    • 33645644870 scopus 로고    scopus 로고
    • Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis
    • 10.1042/BJ20051525, 1409689, 16332250
    • Stines-Chaumeil C, Talfournier F, Branlant G. Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis. Biochem J 2006, 395(1):107-115. 10.1042/BJ20051525, 1409689, 16332250.
    • (2006) Biochem J , vol.395 , Issue.1 , pp. 107-115
    • Stines-Chaumeil, C.1    Talfournier, F.2    Branlant, G.3
  • 39
    • 1342288664 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the dhaT gene of the 1,3-propanediol regulon from Klebsiella pneumoniae
    • Yuanyuan Z, Yang C, Baishan F. Cloning and sequence analysis of the dhaT gene of the 1,3-propanediol regulon from Klebsiella pneumoniae. Biotechnol Lett 2004, 26(3):251-255.
    • (2004) Biotechnol Lett , vol.26 , Issue.3 , pp. 251-255
    • Yuanyuan, Z.1    Yang, C.2    Baishan, F.3
  • 40
    • 35448933577 scopus 로고    scopus 로고
    • Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction
    • Coppi MV, O'Neil RA, Leang C, Kaufmann F, Methe BA, Nevin KP, Woodard TL, Liu A, Lovley DR. Involvement of Geobacter sulfurreducens SfrAB in acetate metabolism rather than intracellular, respiration-linked Fe(III) citrate reduction. Microbiology 2007, 153(Pt 10):3572-3585.
    • (2007) Microbiology , vol.153 , Issue.PART 10 , pp. 3572-3585
    • Coppi, M.V.1    O'Neil, R.A.2    Leang, C.3    Kaufmann, F.4    Methe, B.A.5    Nevin, K.P.6    Woodard, T.L.7    Liu, A.8    Lovley, D.R.9
  • 41
    • 73649177916 scopus 로고
    • Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme
    • Lee HA, Abeles RH. Purification and properties of dioldehydrase, an enzyme requiring a cobamide coenzyme. J Biol Chem 1963, 238:2367-2373.
    • (1963) J Biol Chem , vol.238 , pp. 2367-2373
    • Lee, H.A.1    Abeles, R.H.2
  • 42
    • 2442545374 scopus 로고    scopus 로고
    • The effect of pfl gene knockout on the metabolism for optically pure D-lactate production by Escherichia coli
    • 10.1007/s00253-003-1499-9, 14673546
    • Zhu J, Shimizu K. The effect of pfl gene knockout on the metabolism for optically pure D-lactate production by Escherichia coli. Appl Microbiol Biotechnol 2004, 64(3):367-375. 10.1007/s00253-003-1499-9, 14673546.
    • (2004) Appl Microbiol Biotechnol , vol.64 , Issue.3 , pp. 367-375
    • Zhu, J.1    Shimizu, K.2
  • 43
    • 4944253783 scopus 로고    scopus 로고
    • Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase
    • 10.1128/JB.186.20.6845-6854.2004, 522198, 15466038
    • Mori K, Bando R, Hieda N, Toraya T. Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase. J Bacteriol 2004, 186(20):6845-6854. 10.1128/JB.186.20.6845-6854.2004, 522198, 15466038.
    • (2004) J Bacteriol , vol.186 , Issue.20 , pp. 6845-6854
    • Mori, K.1    Bando, R.2    Hieda, N.3    Toraya, T.4
  • 45
    • 0026563908 scopus 로고
    • Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes
    • 207405, 1385386
    • Walter KA, Bennett GN, Papoutsakis ET. Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes. J Bacteriol 1992, 174(22):7149-7158. 207405, 1385386.
    • (1992) J Bacteriol , vol.174 , Issue.22 , pp. 7149-7158
    • Walter, K.A.1    Bennett, G.N.2    Papoutsakis, E.T.3
  • 46
    • 0027131592 scopus 로고
    • Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase
    • Schmehl M, Jahn A, Meyer zu Vilsendorf A, Hennecke S, Masepohl B, Schuppler M, Marxer M, Oelze J, Klipp W. Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. Mol Gen Genet 1993, 241(5-6):602-615.
    • (1993) Mol Gen Genet , vol.241 , Issue.5-6 , pp. 602-615
    • Schmehl, M.1    Jahn, A.2    Meyer zu Vilsendorf, A.3    Hennecke, S.4    Masepohl, B.5    Schuppler, M.6    Marxer, M.7    Oelze, J.8    Klipp, W.9
  • 47
    • 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
    • 10.1128/JB.00612-10, 2944534, 20675474
    • Wang S, Huang H, Moll J, Thauer RK. NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri. J Bacteriol 2010, 192(19):5115-5123. 10.1128/JB.00612-10, 2944534, 20675474.
    • (2010) J Bacteriol , vol.192 , Issue.19 , pp. 5115-5123
    • Wang, S.1    Huang, H.2    Moll, J.3    Thauer, R.K.4
  • 48
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • 176931, 7751270
    • Malki S, Saimmaime I, De Luca G, Rousset M, Dermoun Z, Belaich JP. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J Bacteriol 1995, 177(10):2628-2636. 176931, 7751270.
    • (1995) J Bacteriol , vol.177 , Issue.10 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.P.6
  • 49
    • 34547732425 scopus 로고    scopus 로고
    • The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15
    • 10.1128/JB.00581-07, 1952053, 17545285
    • Pogoryelov D, Reichen C, Klyszejko AL, Brunisholz R, Muller DJ, Dimroth P, Meier T. The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. J Bacteriol 2007, 189(16):5895-5902. 10.1128/JB.00581-07, 1952053, 17545285.
    • (2007) J Bacteriol , vol.189 , Issue.16 , pp. 5895-5902
    • Pogoryelov, D.1    Reichen, C.2    Klyszejko, A.L.3    Brunisholz, R.4    Muller, D.J.5    Dimroth, P.6    Meier, T.7
  • 50
    • 0021744435 scopus 로고
    • Uncoupling by acetic acid limits growth of and acetogenesis by Clostridium thermoaceticum
    • 241699, 16346677
    • Baronofsky JJ, Schreurs WJ, Kashket ER. Uncoupling by acetic acid limits growth of and acetogenesis by Clostridium thermoaceticum. Appl Environ Microbiol 1984, 48(6):1134-1139. 241699, 16346677.
    • (1984) Appl Environ Microbiol , vol.48 , Issue.6 , pp. 1134-1139
    • Baronofsky, J.J.1    Schreurs, W.J.2    Kashket, E.R.3
  • 51
    • 0042838364 scopus 로고    scopus 로고
    • A tenth atp gene and the conserved atpI gene of a Bacillus atp operon have a role in Mg2+ uptake
    • 10.1073/pnas.1832982100, 193541, 12917488
    • Hicks DB, Wang Z, Wei Y, Kent R, Guffanti AA, Banciu H, Bechhofer DH, Krulwich TA. A tenth atp gene and the conserved atpI gene of a Bacillus atp operon have a role in Mg2+ uptake. Proc Natl Acad Sci USA 2003, 100(18):10213-10218. 10.1073/pnas.1832982100, 193541, 12917488.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.18 , pp. 10213-10218
    • Hicks, D.B.1    Wang, Z.2    Wei, Y.3    Kent, R.4    Guffanti, A.A.5    Banciu, H.6    Bechhofer, D.H.7    Krulwich, T.A.8
  • 52
    • 66749182726 scopus 로고    scopus 로고
    • Identification of ColR binding consensus and prediction of regulon of ColRS two-component system
    • 10.1186/1471-2199-10-46, 2689224, 19445690
    • Kivistik PA, Kivi R, Kivisaar M, Horak R. Identification of ColR binding consensus and prediction of regulon of ColRS two-component system. BMC Mol Biol 2009, 10:46. 10.1186/1471-2199-10-46, 2689224, 19445690.
    • (2009) BMC Mol Biol , vol.10 , pp. 46
    • Kivistik, P.A.1    Kivi, R.2    Kivisaar, M.3    Horak, R.4
  • 53
    • 3042513872 scopus 로고    scopus 로고
    • The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
    • 10.1128/JB.186.13.4124-4133.2004, 421605, 15205413
    • Lee H, Hsu FF, Turk J, Groisman EA. The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica. J Bacteriol 2004, 186(13):4124-4133. 10.1128/JB.186.13.4124-4133.2004, 421605, 15205413.
    • (2004) J Bacteriol , vol.186 , Issue.13 , pp. 4124-4133
    • Lee, H.1    Hsu, F.F.2    Turk, J.3    Groisman, E.A.4
  • 54
    • 77954202864 scopus 로고    scopus 로고
    • Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase
    • 10.1093/bioinformatics/btq234, 2881411, 20472544
    • Dibrova DV, Galperin MY, Mulkidjanian AY. Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase. Bioinformatics 2010, 26(12):1473-1476. 10.1093/bioinformatics/btq234, 2881411, 20472544.
    • (2010) Bioinformatics , vol.26 , Issue.12 , pp. 1473-1476
    • Dibrova, D.V.1    Galperin, M.Y.2    Mulkidjanian, A.Y.3
  • 55
    • 26444578862 scopus 로고    scopus 로고
    • The Mrp system: a giant among monovalent cation/proton antiporters?
    • 10.1007/s00792-005-0451-6, 15980940
    • Swartz TH, Ikewada S, Ishikawa O, Ito M, Krulwich TA. The Mrp system: a giant among monovalent cation/proton antiporters?. Extremophiles 2005, 9(5):345-354. 10.1007/s00792-005-0451-6, 15980940.
    • (2005) Extremophiles , vol.9 , Issue.5 , pp. 345-354
    • Swartz, T.H.1    Ikewada, S.2    Ishikawa, O.3    Ito, M.4    Krulwich, T.A.5
  • 56
    • 0025856542 scopus 로고
    • Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli
    • Taglicht D, Padan E, Schuldiner S. Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. J Biol Chem 1991, 266(17):11289-11294.
    • (1991) J Biol Chem , vol.266 , Issue.17 , pp. 11289-11294
    • Taglicht, D.1    Padan, E.2    Schuldiner, S.3
  • 57
    • 27744446090 scopus 로고    scopus 로고
    • The activity profile of the NhaD-type Na+(Li+)/H+ antiporter from the soda lake haloalkaliphile Alkalimonas amylolytica is adaptive for the extreme environment
    • 10.1128/JB.187.22.7589-7595.2005, 1280297, 16267283
    • Liu J, Xue Y, Wang Q, Wei Y, Swartz TH, Hicks DB, Ito M, Ma Y, Krulwich TA. The activity profile of the NhaD-type Na+(Li+)/H+ antiporter from the soda lake haloalkaliphile Alkalimonas amylolytica is adaptive for the extreme environment. J Bacteriol 2005, 187(22):7589-7595. 10.1128/JB.187.22.7589-7595.2005, 1280297, 16267283.
    • (2005) J Bacteriol , vol.187 , Issue.22 , pp. 7589-7595
    • Liu, J.1    Xue, Y.2    Wang, Q.3    Wei, Y.4    Swartz, T.H.5    Hicks, D.B.6    Ito, M.7    Ma, Y.8    Krulwich, T.A.9
  • 58
    • 0037312744 scopus 로고    scopus 로고
    • KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity
    • 10.1128/JB.185.4.1289-1298.2003, 142857, 12562800
    • Holtmann G, Bakker EP, Uozumi N, Bremer E. KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity. J Bacteriol 2003, 185(4):1289-1298. 10.1128/JB.185.4.1289-1298.2003, 142857, 12562800.
    • (2003) J Bacteriol , vol.185 , Issue.4 , pp. 1289-1298
    • Holtmann, G.1    Bakker, E.P.2    Uozumi, N.3    Bremer, E.4
  • 59
    • 10744232046 scopus 로고    scopus 로고
    • Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity
    • 10.1128/AEM.69.10.6047-6055.2003, 201229, 14532061
    • Pflüger K, Baumann S, Gottschalk G, Lin W, Santos H, Muller V. Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity. Appl Environ Microbiol 2003, 69(10):6047-6055. 10.1128/AEM.69.10.6047-6055.2003, 201229, 14532061.
    • (2003) Appl Environ Microbiol , vol.69 , Issue.10 , pp. 6047-6055
    • Pflüger, K.1    Baumann, S.2    Gottschalk, G.3    Lin, W.4    Santos, H.5    Muller, V.6
  • 61
    • 77957134413 scopus 로고    scopus 로고
    • A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG
    • 10.1016/j.febslet.2010.09.008, 20837009
    • Nicolet Y, Martin L, Tron C, Fontecilla-Camps JC. A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG. FEBS Lett 2010, 584(19):4197-4202. 10.1016/j.febslet.2010.09.008, 20837009.
    • (2010) FEBS Lett , vol.584 , Issue.19 , pp. 4197-4202
    • Nicolet, Y.1    Martin, L.2    Tron, C.3    Fontecilla-Camps, J.C.4
  • 62
    • 30744454041 scopus 로고    scopus 로고
    • Genetic characterization of a single bifunctional enzyme for fumarate reduction and succinate oxidation in Geobacter sulfurreducens and engineering of fumarate reduction in Geobacter metallireducens
    • 10.1128/JB.188.2.450-455.2006, 1347312, 16385034
    • Butler JE, Glaven RH, Esteve-Nunez A, Nunez C, Shelobolina ES, Bond DR, Lovley DR. Genetic characterization of a single bifunctional enzyme for fumarate reduction and succinate oxidation in Geobacter sulfurreducens and engineering of fumarate reduction in Geobacter metallireducens. J Bacteriol 2006, 188(2):450-455. 10.1128/JB.188.2.450-455.2006, 1347312, 16385034.
    • (2006) J Bacteriol , vol.188 , Issue.2 , pp. 450-455
    • Butler, J.E.1    Glaven, R.H.2    Esteve-Nunez, A.3    Nunez, C.4    Shelobolina, E.S.5    Bond, D.R.6    Lovley, D.R.7
  • 63
    • 22544440273 scopus 로고    scopus 로고
    • Functional characterization of a Na(+)-coupled dicarboxylate carrier protein from Staphylococcus aureus
    • 10.1128/JB.187.15.5189-5194.2005, 1196027, 16030212
    • Hall JA, Pajor AM. Functional characterization of a Na(+)-coupled dicarboxylate carrier protein from Staphylococcus aureus. J Bacteriol 2005, 187(15):5189-5194. 10.1128/JB.187.15.5189-5194.2005, 1196027, 16030212.
    • (2005) J Bacteriol , vol.187 , Issue.15 , pp. 5189-5194
    • Hall, J.A.1    Pajor, A.M.2
  • 64
    • 84868611178 scopus 로고    scopus 로고
    • Interspecies electron transfer via H2 and formate rather than direct electrical connections in co-cultures of Pelobacter carbinolicus and Geobacter sulfurreducens
    • 10.1128/AEM.01946-12, 22923399
    • Rotaru A-E, Shrestha PM, Liu F, Ueki T, Nevin K, Summers ZM, Lovley DR. Interspecies electron transfer via H2 and formate rather than direct electrical connections in co-cultures of Pelobacter carbinolicus and Geobacter sulfurreducens. Appl Environ Microbiol 2012, 78(21):7645-7651. 10.1128/AEM.01946-12, 22923399.
    • (2012) Appl Environ Microbiol , vol.78 , Issue.21 , pp. 7645-7651
    • Rotaru, A.-E.1    Shrestha, P.M.2    Liu, F.3    Ueki, T.4    Nevin, K.5    Summers, Z.M.6    Lovley, D.R.7
  • 65
    • 0036837968 scopus 로고    scopus 로고
    • Carbon monoxide cycling by Desulfovibrio vulgaris Hildenborough
    • 10.1128/JB.184.21.5903-5911.2002, 135394, 12374824
    • Voordouw G. Carbon monoxide cycling by Desulfovibrio vulgaris Hildenborough. J Bacteriol 2002, 184(21):5903-5911. 10.1128/JB.184.21.5903-5911.2002, 135394, 12374824.
    • (2002) J Bacteriol , vol.184 , Issue.21 , pp. 5903-5911
    • Voordouw, G.1
  • 67
    • 0030963841 scopus 로고    scopus 로고
    • Multiheme cytochromes from the sulfur-reducing bacterium Desulfuromonas acetoxidans
    • 10.1111/j.1432-1033.1997.00323.x, 9346284
    • Pereira IA, Pacheco I, Liu MY, Legall J, Xavier AV, Teixeira M. Multiheme cytochromes from the sulfur-reducing bacterium Desulfuromonas acetoxidans. Eur J Biochem 1997, 248(2):323-328. 10.1111/j.1432-1033.1997.00323.x, 9346284.
    • (1997) Eur J Biochem , vol.248 , Issue.2 , pp. 323-328
    • Pereira, I.A.1    Pacheco, I.2    Liu, M.Y.3    Legall, J.4    Xavier, A.V.5    Teixeira, M.6
  • 68
    • 34948894523 scopus 로고    scopus 로고
    • The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases
    • 10.1016/j.febslet.2007.09.008, 17888426
    • Pereira MM, Refojo PN, Hreggvidsson GO, Hjorleifsdottir S, Teixeira M. The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases. FEBS Lett 2007, 581(25):4831-4835. 10.1016/j.febslet.2007.09.008, 17888426.
    • (2007) FEBS Lett , vol.581 , Issue.25 , pp. 4831-4835
    • Pereira, M.M.1    Refojo, P.N.2    Hreggvidsson, G.O.3    Hjorleifsdottir, S.4    Teixeira, M.5
  • 69
    • 77955236947 scopus 로고    scopus 로고
    • Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus
    • 10.1021/bi100858k, 2914828, 20614874
    • Gao X, Xin Y, Bell PD, Wen J, Blankenship RE. Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus. Biochemistry 2010, 49(31):6670-6679. 10.1021/bi100858k, 2914828, 20614874.
    • (2010) Biochemistry , vol.49 , Issue.31 , pp. 6670-6679
    • Gao, X.1    Xin, Y.2    Bell, P.D.3    Wen, J.4    Blankenship, R.E.5
  • 70
    • 67650590854 scopus 로고    scopus 로고
    • The genome sequence of Geobacter metallireducens: features of metabolism, physiology and regulation common and dissimilar to Geobacter sulfurreducens
    • 10.1186/1471-2180-9-109, 2700814, 19473543
    • Aklujkar M, Krushkal J, DiBartolo G, Lapidus A, Land ML, Lovley DR. The genome sequence of Geobacter metallireducens: features of metabolism, physiology and regulation common and dissimilar to Geobacter sulfurreducens. BMC Microbiol 2009, 9:109. 10.1186/1471-2180-9-109, 2700814, 19473543.
    • (2009) BMC Microbiol , vol.9 , pp. 109
    • Aklujkar, M.1    Krushkal, J.2    DiBartolo, G.3    Lapidus, A.4    Land, M.L.5    Lovley, D.R.6
  • 72
    • 21344461500 scopus 로고    scopus 로고
    • Extracellular electron transfer via microbial nanowires
    • 10.1038/nature03661, 15973408
    • Reguera G, McCarthy KD, Mehta T, Nicoll JS, Tuominen MT, Lovley DR. Extracellular electron transfer via microbial nanowires. Nature 2005, 435(7045):1098-1101. 10.1038/nature03661, 15973408.
    • (2005) Nature , vol.435 , Issue.7045 , pp. 1098-1101
    • Reguera, G.1    McCarthy, K.D.2    Mehta, T.3    Nicoll, J.S.4    Tuominen, M.T.5    Lovley, D.R.6
  • 73
    • 33751014053 scopus 로고    scopus 로고
    • Biofilm and nanowire production leads to increased current in Geobacter sulfurreducens fuel cells
    • 10.1128/AEM.01444-06, 1636155, 16936064
    • Reguera G, Nevin KP, Nicoll JS, Covalla SF, Woodard TL, Lovley DR. Biofilm and nanowire production leads to increased current in Geobacter sulfurreducens fuel cells. Appl Environ Microbiol 2006, 72(11):7345-7348. 10.1128/AEM.01444-06, 1636155, 16936064.
    • (2006) Appl Environ Microbiol , vol.72 , Issue.11 , pp. 7345-7348
    • Reguera, G.1    Nevin, K.P.2    Nicoll, J.S.3    Covalla, S.F.4    Woodard, T.L.5    Lovley, D.R.6
  • 74
    • 84861842701 scopus 로고    scopus 로고
    • Microbial nanowires: a new paradigm for biological electron transfer and bioelectronics
    • 10.1002/cssc.201100733, 22614997
    • Malvankar NS, Lovley DR. Microbial nanowires: a new paradigm for biological electron transfer and bioelectronics. ChemSusChem 2012, 5(6):1039-1046. 10.1002/cssc.201100733, 22614997.
    • (2012) ChemSusChem , vol.5 , Issue.6 , pp. 1039-1046
    • Malvankar, N.S.1    Lovley, D.R.2
  • 75
    • 78649707496 scopus 로고    scopus 로고
    • Direct exchange of electrons within aggregates of an evolved syntrophic coculture of anaerobic bacteria
    • 10.1126/science.1196526, 21127257
    • Summers ZM, Fogarty HE, Leang C, Franks AE, Malvankar NS, Lovley DR. Direct exchange of electrons within aggregates of an evolved syntrophic coculture of anaerobic bacteria. Science 2010, 330(6009):1413-1415. 10.1126/science.1196526, 21127257.
    • (2010) Science , vol.330 , Issue.6009 , pp. 1413-1415
    • Summers, Z.M.1    Fogarty, H.E.2    Leang, C.3    Franks, A.E.4    Malvankar, N.S.5    Lovley, D.R.6
  • 76
    • 34548274490 scopus 로고    scopus 로고
    • Lack of electricity production by Pelobacter carbinolicus indicates that the capacity for Fe(III) oxide reduction does not necessarily confer electron transfer ability to fuel cell anodes
    • 10.1128/AEM.00804-07, 1950970, 17574993
    • Richter H, Lanthier M, Nevin KP, Lovley DR. Lack of electricity production by Pelobacter carbinolicus indicates that the capacity for Fe(III) oxide reduction does not necessarily confer electron transfer ability to fuel cell anodes. Appl Environ Microbiol 2007, 73(16):5347-5353. 10.1128/AEM.00804-07, 1950970, 17574993.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.16 , pp. 5347-5353
    • Richter, H.1    Lanthier, M.2    Nevin, K.P.3    Lovley, D.R.4
  • 77
    • 33747119626 scopus 로고    scopus 로고
    • A putative multicopper protein secreted by an atypical type II secretion system involved in the reduction of insoluble electron acceptors in Geobacter sulfurreducens
    • Mehta T, Childers SE, Glaven R, Lovley DR, Mester T. A putative multicopper protein secreted by an atypical type II secretion system involved in the reduction of insoluble electron acceptors in Geobacter sulfurreducens. Microbiology 2006, 152(Pt 8):2257-2264.
    • (2006) Microbiology , vol.152 , Issue.PART 8 , pp. 2257-2264
    • Mehta, T.1    Childers, S.E.2    Glaven, R.3    Lovley, D.R.4    Mester, T.5
  • 78
    • 37349093031 scopus 로고    scopus 로고
    • Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek
    • 10.1128/MMBR.00014-07, 2168650, 18063717
    • Nuccio SP, Baumler AJ. Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek. Microbiol Mol Biol Rev 2007, 71(4):551-575. 10.1128/MMBR.00014-07, 2168650, 18063717.
    • (2007) Microbiol Mol Biol Rev , vol.71 , Issue.4 , pp. 551-575
    • Nuccio, S.P.1    Baumler, A.J.2
  • 79
    • 55349091732 scopus 로고    scopus 로고
    • Comparative genomics of Geobacter chemotaxis genes reveals diverse signaling function
    • 10.1186/1471-2164-9-471, 2577667, 18844997
    • Tran HT, Krushkal J, Antommattei FM, Lovley DR, Weis RM. Comparative genomics of Geobacter chemotaxis genes reveals diverse signaling function. BMC Genomics 2008, 9:471. 10.1186/1471-2164-9-471, 2577667, 18844997.
    • (2008) BMC Genomics , vol.9 , pp. 471
    • Tran, H.T.1    Krushkal, J.2    Antommattei, F.M.3    Lovley, D.R.4    Weis, R.M.5
  • 80
    • 33847249975 scopus 로고    scopus 로고
    • Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors
    • 10.1073/pnas.0609359104, 1797150, 17299051
    • Alexander RP, Zhulin IB. Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors. Proc Natl Acad Sci USA 2007, 104(8):2885-2890. 10.1073/pnas.0609359104, 1797150, 17299051.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.8 , pp. 2885-2890
    • Alexander, R.P.1    Zhulin, I.B.2
  • 81
    • 0022628946 scopus 로고
    • ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans
    • Paulsen J, Kröger A, Thauer RK. ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans. Arch Microbiol 1986, 144:78-83.
    • (1986) Arch Microbiol , vol.144 , pp. 78-83
    • Paulsen, J.1    Kröger, A.2    Thauer, R.K.3
  • 82
    • 0031061563 scopus 로고    scopus 로고
    • Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications
    • Kort R, Liebl W, Labedan B, Forterre P, Eggen RI, de Vos WM. Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications. Extremophiles 1997, 1(1):52-60.
    • (1997) Extremophiles , vol.1 , Issue.1 , pp. 52-60
    • Kort, R.1    Liebl, W.2    Labedan, B.3    Forterre, P.4    Eggen, R.I.5    de Vos, W.M.6
  • 83
    • 0034671553 scopus 로고    scopus 로고
    • A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus
    • 10.1074/jbc.M005136200, 10924516
    • Minambres B, Olivera ER, Jensen RA, Luengo JM. A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. J Biol Chem 2000, 275(50):39529-39542. 10.1074/jbc.M005136200, 10924516.
    • (2000) J Biol Chem , vol.275 , Issue.50 , pp. 39529-39542
    • Minambres, B.1    Olivera, E.R.2    Jensen, R.A.3    Luengo, J.M.4
  • 84
    • 0033199239 scopus 로고    scopus 로고
    • Structural and kinetic studies of the pyruvate-ferredoxin oxidoreductase/ferredoxin complex from Desulfovibrio africanus
    • 10.1046/j.1432-1327.1999.00648.x, 10491097
    • Pieulle L, Charon MH, Bianco P, Bonicel J, Petillot Y, Hatchikian EC. Structural and kinetic studies of the pyruvate-ferredoxin oxidoreductase/ferredoxin complex from Desulfovibrio africanus. Eur J Biochem 1999, 264(2):500-508. 10.1046/j.1432-1327.1999.00648.x, 10491097.
    • (1999) Eur J Biochem , vol.264 , Issue.2 , pp. 500-508
    • Pieulle, L.1    Charon, M.H.2    Bianco, P.3    Bonicel, J.4    Petillot, Y.5    Hatchikian, E.C.6
  • 85
    • 0027167447 scopus 로고
    • Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin
    • 204803, 7685336
    • Renna MC, Najimudin N, Winik LR, Zahler SA. Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin. J Bacteriol 1993, 175(12):3863-3875. 204803, 7685336.
    • (1993) J Bacteriol , vol.175 , Issue.12 , pp. 3863-3875
    • Renna, M.C.1    Najimudin, N.2    Winik, L.R.3    Zahler, S.A.4
  • 86
    • 0039598454 scopus 로고    scopus 로고
    • The Genus Pelobacter
    • Springer, Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E, 3
    • Schink B. The Genus Pelobacter. The Prokaryotes 2006, 5-11. Springer, Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E, 3.
    • (2006) The Prokaryotes , pp. 5-11
    • Schink, B.1
  • 87
    • 0032549018 scopus 로고    scopus 로고
    • Isolation and characterization of the carbon-phosphorus bond-forming enzyme phosphoenolpyruvate mutase from the mollusk Mytilus edulis
    • 10.1074/jbc.273.8.4443, 9468496
    • Kim A, Kim J, Martin BM, Dunaway-Mariano D. Isolation and characterization of the carbon-phosphorus bond-forming enzyme phosphoenolpyruvate mutase from the mollusk Mytilus edulis. J Biol Chem 1998, 273(8):4443-4448. 10.1074/jbc.273.8.4443, 9468496.
    • (1998) J Biol Chem , vol.273 , Issue.8 , pp. 4443-4448
    • Kim, A.1    Kim, J.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 88
    • 0014897417 scopus 로고
    • Phosphodeoxyribomutase from Escherichia coli. Purification and some properties
    • 10.1111/j.1432-1033.1970.tb01179.x, 4992818
    • Hammer-Jespersen K, Munch-Petersen A. Phosphodeoxyribomutase from Escherichia coli. Purification and some properties. Eur J Biochem 1970, 17(3):397-407. 10.1111/j.1432-1033.1970.tb01179.x, 4992818.
    • (1970) Eur J Biochem , vol.17 , Issue.3 , pp. 397-407
    • Hammer-Jespersen, K.1    Munch-Petersen, A.2
  • 89
    • 0024977840 scopus 로고
    • Nucleotide sequence of the deoC gene of Mycoplasma pneumoniae
    • 10.1093/nar/17.2.801, 331626, 2492658
    • Loechel S, Inamine JM, Hu PC. Nucleotide sequence of the deoC gene of Mycoplasma pneumoniae. Nucleic Acids Res 1989, 17(2):801. 10.1093/nar/17.2.801, 331626, 2492658.
    • (1989) Nucleic Acids Res , vol.17 , Issue.2 , pp. 801
    • Loechel, S.1    Inamine, J.M.2    Hu, P.C.3
  • 90
    • 0024409274 scopus 로고
    • The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation
    • 10.1093/nar/17.12.4883, 318048, 2664711
    • Lu Z, Lin EC. The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation. Nucleic Acids Res 1989, 17(12):4883-4884. 10.1093/nar/17.12.4883, 318048, 2664711.
    • (1989) Nucleic Acids Res , vol.17 , Issue.12 , pp. 4883-4884
    • Lu, Z.1    Lin, E.C.2
  • 91
    • 0027417393 scopus 로고
    • Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-pyruvate oxidase family
    • Chang YY, Wang AY, Cronan JE. Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-pyruvate oxidase family. J Biol Chem 1993, 268(6):3911-3919.
    • (1993) J Biol Chem , vol.268 , Issue.6 , pp. 3911-3919
    • Chang, Y.Y.1    Wang, A.Y.2    Cronan, J.E.3
  • 92
    • 33748753075 scopus 로고    scopus 로고
    • Structural basis for the redox control of plant glutamate cysteine ligase
    • 10.1074/jbc.M602770200, 16766527
    • Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K. Structural basis for the redox control of plant glutamate cysteine ligase. J Biol Chem 2006, 281(37):27557-27565. 10.1074/jbc.M602770200, 16766527.
    • (2006) J Biol Chem , vol.281 , Issue.37 , pp. 27557-27565
    • Hothorn, M.1    Wachter, A.2    Gromes, R.3    Stuwe, T.4    Rausch, T.5    Scheffzek, K.6
  • 93
    • 0033923358 scopus 로고    scopus 로고
    • Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis
    • Kizil G, Wilks K, Wells D, Ala'Aldeen DA. Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis. J Med Microbiol 2000, 49(7):669-673.
    • (2000) J Med Microbiol , vol.49 , Issue.7 , pp. 669-673
    • Kizil, G.1    Wilks, K.2    Wells, D.3    Ala'Aldeen, D.A.4
  • 94
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing B, Green P. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res 1998, 8(3):186-194.
    • (1998) Genome Res , vol.8 , Issue.3 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 95
    • 0031955518 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. I. Accuracy assessment
    • Ewing B, Hillier L, Wendl MC, Green P. Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res 1998, 8(3):175-185.
    • (1998) Genome Res , vol.8 , Issue.3 , pp. 175-185
    • Ewing, B.1    Hillier, L.2    Wendl, M.C.3    Green, P.4
  • 96
    • 0031955116 scopus 로고    scopus 로고
    • Consed: a graphical tool for sequence finishing
    • Gordon D, Abajian C, Green P. Consed: a graphical tool for sequence finishing. Genome Res 1998, 8(3):195-202.
    • (1998) Genome Res , vol.8 , Issue.3 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 97
    • 34147132825 scopus 로고    scopus 로고
    • Identifying bacterial genes and endosymbiont DNA with Glimmer
    • 10.1093/bioinformatics/btm009, 2387122, 17237039
    • Delcher AL, Bratke KA, Powers EC, Salzberg SL. Identifying bacterial genes and endosymbiont DNA with Glimmer. Bioinformatics 2007, 23(6):673-679. 10.1093/bioinformatics/btm009, 2387122, 17237039.
    • (2007) Bioinformatics , vol.23 , Issue.6 , pp. 673-679
    • Delcher, A.L.1    Bratke, K.A.2    Powers, E.C.3    Salzberg, S.L.4
  • 98
    • 0032900737 scopus 로고    scopus 로고
    • CRITICA: coding region identification tool invoking comparative analysis
    • 10.1093/oxfordjournals.molbev.a026133, 10331277
    • Badger JH, Olsen GJ. CRITICA: coding region identification tool invoking comparative analysis. Mol Biol Evol 1999, 16(4):512-524. 10.1093/oxfordjournals.molbev.a026133, 10331277.
    • (1999) Mol Biol Evol , vol.16 , Issue.4 , pp. 512-524
    • Badger, J.H.1    Olsen, G.J.2
  • 99
    • 0030854739 scopus 로고    scopus 로고
    • TRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence
    • 146525, 9023104
    • Lowe TM, Eddy SR. tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res 1997, 25(5):955-964. 146525, 9023104.
    • (1997) Nucleic Acids Res , vol.25 , Issue.5 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 100
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • 10.1006/jmbi.2000.4315, 11152613
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001, 305(3):567-580. 10.1006/jmbi.2000.4315, 11152613.
    • (2001) J Mol Biol , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 101
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • 10.1016/j.jmb.2004.05.028, 15223320
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340(4):783-795. 10.1016/j.jmb.2004.05.028, 15223320.
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 102
    • 77956470482 scopus 로고    scopus 로고
    • The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of Geobacter species that predominate in Fe(III)-reducing subsurface environments
    • 10.1186/1471-2164-11-490, 2996986, 20828392
    • Aklujkar M, Young ND, Holmes D, Chavan M, Risso C, Kiss HE, Han CS, Land ML, Lovley DR. The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of Geobacter species that predominate in Fe(III)-reducing subsurface environments. BMC Genomics 2010, 11:490. 10.1186/1471-2164-11-490, 2996986, 20828392.
    • (2010) BMC Genomics , vol.11 , pp. 490
    • Aklujkar, M.1    Young, N.D.2    Holmes, D.3    Chavan, M.4    Risso, C.5    Kiss, H.E.6    Han, C.S.7    Land, M.L.8    Lovley, D.R.9
  • 104
    • 0141519279 scopus 로고    scopus 로고
    • OrthoMCL: identification of ortholog groups for eukaryotic genomes
    • 10.1101/gr.1224503, 403725, 12952885
    • Li L, Stoeckert CJ, Roos DS. OrthoMCL: identification of ortholog groups for eukaryotic genomes. Genome Res 2003, 13(9):2178-2189. 10.1101/gr.1224503, 403725, 12952885.
    • (2003) Genome Res , vol.13 , Issue.9 , pp. 2178-2189
    • Li, L.1    Stoeckert, C.J.2    Roos, D.S.3


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