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Volumn 4, Issue , 2014, Pages

Cell-secreted flavins bound to membrane cytochromes dictate electron transfer reactions to surfaces with diverse charge and pH

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; FLAVINE MONONUCLEOTIDE; RIBOFLAVIN; RIBOFLAVIN DERIVATIVE;

EID: 84904322163     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep05628     Document Type: Article
Times cited : (142)

References (58)
  • 1
    • 0028132223 scopus 로고
    • Iron and manganese in anaerobic respiration: Environmental significance, physiology, and regulation
    • Nealson, K. H. & Saffarini, D. Iron and manganese in anaerobic respiration: environmental significance, physiology, and regulation. Annu. Rev. Microbiol. 48, 311-343, DOI:10.1146/annurev.mi.48.100194.001523 (1994). (Pubitemid 24334100)
    • (1994) Annual Review of Microbiology , vol.48 , pp. 311-343
    • Nealson, K.H.1    Saffarini, D.2
  • 2
    • 78650173757 scopus 로고    scopus 로고
    • Microbial Electrosynthesis: Feeding Microbes Electricity to Convert Carbon Dioxide and Water to Multicarbon Extracellular Organic Compounds
    • DOI:10.1128/mBio.00103-10
    • Lovley, D. R., Nevin, K. P., Woodard, T. L., Franks, A. E. & Summers, Z. M. Microbial Electrosynthesis: Feeding Microbes Electricity To Convert Carbon Dioxide and Water to Multicarbon Extracellular Organic Compounds. mBio 1, 1-4, DOI:10.1128/mBio.00103-10 (2010).
    • (2010) MBio , vol.1 , pp. 1-4
    • Lovley, D.R.1    Nevin, K.P.2    Woodard, T.L.3    Franks, A.E.4    Summers, Z.M.5
  • 3
    • 33745225414 scopus 로고    scopus 로고
    • Bug juice: Harvesting electricity with microorganisms
    • DOI 10.1038/nrmicro1442, PII N1442
    • Lovley, D. R. Bug juice: harvesting electricity with microorganisms. Nat. Rev. Microbiol. 4, 497-508, DOI:nrmicro1442 (2006). (Pubitemid 43905609)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.7 , pp. 497-508
    • Lovley, D.R.1
  • 4
    • 84863216374 scopus 로고    scopus 로고
    • Marine sulfate-reducing bacteria cause serious corrosion of iron under electroconductive biogenic mineral crust
    • DOI:10.1111/j.1462-2920.2012.02778.x
    • Enning, D. et al. Marine sulfate-reducing bacteria cause serious corrosion of iron under electroconductive biogenic mineral crust. Environ. Microbiol. 14, 1772-1787, DOI:10.1111/j.1462-2920.2012.02778.x (2012).
    • (2012) Environ. Microbiol. , vol.14 , pp. 1772-1787
    • Enning, D.1
  • 5
    • 17744405443 scopus 로고    scopus 로고
    • A generation of microbial fuel cells with current outputs boosted by more than one order of magnitude
    • DOI 10.1002/anie.200350918
    • Schroder, U., Niessen, J. & Scholz, F. A generation of microbial fuel cells with current outputs boosted bymore than one order of magnitude. Angew. Chem. Int. Ed. 42, 2880-2883, doi:10.1002/anie.200350918 (2003). (Pubitemid 36876605)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.25 , pp. 2880-2883
    • Schroder, U.1    Niessen, J.2    Scholz, F.3
  • 7
    • 79959370190 scopus 로고    scopus 로고
    • Structure of a bacterial cell surface decaheme electron conduit
    • DOI:10.1073/pnas.1017200108
    • Clarke, T. A. et al. Structure of a bacterial cell surface decaheme electron conduit. P. Natl. Acad. Sci. USA 108, 9384-9389, DOI:10.1073/pnas. 1017200108 (2011).
    • (2011) P. Natl. Acad. Sci. USA , vol.108 , pp. 9384-9389
    • Clarke, T.A.1
  • 8
    • 84862556362 scopus 로고    scopus 로고
    • Thermodynamics of electron flow in the bacterial deca-heme cytochrome MtrF
    • DOI:10.1021/ja3027696
    • Breuer, M., Zarzycki, P., Blumberger, J. & Rosso, K. M. Thermodynamics of electron flow in the bacterial deca-heme cytochrome MtrF. J. Am. Chem. Soc. 134, 9868-9871, DOI:10.1021/ja3027696 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 9868-9871
    • Breuer, M.1    Zarzycki, P.2    Blumberger, J.3    Rosso, K.M.4
  • 9
    • 0030903069 scopus 로고    scopus 로고
    • Outer membrane cytochromes of Shewanella putrefaciens MR-1: Spectral analysis, and purification of the 83-KDa c-type cytochrome
    • DOI 10.1016/S0005-2736(97)00034-5, PII S0005273697000345
    • Myers, C. R. & Myers, J. M. Outer membrane cytochromes of Shewanella putrefaciens MR-1: spectral analysis, and purification of the 83-kDa c-type cytochrome. Biochim. Biophys. Acta 1326, 307-318, DOI:S0005-2736(97)00034-5 (1997). (Pubitemid 27272135)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1326 , Issue.2 , pp. 307-318
    • Myers, C.R.1    Myers, J.M.2
  • 10
    • 70449714760 scopus 로고    scopus 로고
    • The roles of outer membrane cytochromes of Shewanella and Geobacter in extracellular electron transfer
    • DOI:10.1111/j.1758-2229.2009.00035.x
    • Shi, L. A. et al. The roles of outer membrane cytochromes of Shewanella and Geobacter in extracellular electron transfer. Env. Microbiol. Rep. 1, 220-227, DOI:10.1111/j.1758-2229.2009.00035.x (2009).
    • (2009) Env. Microbiol. Rep. , vol.1 , pp. 220-227
    • Shi, L.A.1
  • 11
    • 73349134931 scopus 로고    scopus 로고
    • Characterization of an electron conduit between bacteria and the extracellular environment
    • DOI:0900086106
    • Hartshorne, R. S. et al. Characterization of an electron conduit between bacteria and the extracellular environment. Proc. Natl. Acad. Sci. USA 106, 22169-22174, DOI:0900086106 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22169-22174
    • Hartshorne, R.S.1
  • 13
    • 45549088922 scopus 로고    scopus 로고
    • In vivo identification of the outer membrane protein omcA-mtrC interaction network in Shewanella oneidensis MR-1 cells using novel hydrophobic chemical cross-linkers
    • DOI:10.1021/Pr7007658
    • Zhang, H. Z. et al. In vivo identification of the outer membrane protein omcA-mtrC interaction network in Shewanella oneidensis MR-1 cells using novel hydrophobic chemical cross-linkers. J. Proteome Res. 7, 1712-1720, DOI:10.1021/Pr7007658 (2008).
    • (2008) J. Proteome Res. , vol.7 , pp. 1712-1720
    • Zhang, H.Z.1
  • 17
    • 84874582197 scopus 로고    scopus 로고
    • Flavin Electron Shuttles Dominate Extracellular Electron Transfer by Shewanella oneidensis
    • Kotloski, N. J. & Gralnick, J. A. Flavin Electron Shuttles Dominate Extracellular Electron Transfer by Shewanella oneidensis. mBio 4, 1-4 (2013).
    • (2013) MBio , vol.4 , pp. 1-4
    • Kotloski, N.J.1    Gralnick, J.A.2
  • 18
    • 84896955496 scopus 로고    scopus 로고
    • Uptake of Self-secreted Flavins as Bound Cofactors for Extracellular Electron Transfer in Geobacter Species
    • DOI:10.1039/C3EE43674H
    • Okamoto, A., Saito, K., Inoue, K., Nealson, H. K., Hashimoto, K. & Nakamura, R. Uptake of Self-secreted Flavins as Bound Cofactors for Extracellular Electron Transfer in Geobacter Species. Energy Environ. Sci. 7, 1357-1362, DOI:10.1039/C3EE43674H (2014).
    • (2014) Energy Environ. Sci. , vol.7 , pp. 1357-1362
    • Okamoto, A.1    Saito, K.2    Inoue, K.3    Nealson, H.K.4    Hashimoto, K.5    Nakamura, R.6
  • 20
    • 0034604081 scopus 로고    scopus 로고
    • A role for excreted quinones in extracellular electron transfer
    • DOI 10.1038/35011098
    • Newman, D. K. & Kolter, R. A role for excreted quinones in extracellular electron transfer. Nature 405, 94-97, DOI: 10.1038/35011098 (2000). (Pubitemid 30321822)
    • (2000) Nature , vol.405 , Issue.6782 , pp. 94-97
    • Newman, D.K.1    Kolter, R.2
  • 21
    • 0036252368 scopus 로고    scopus 로고
    • Mechanisms for Fe(III) oxide reduction in sedimentary environments
    • DOI 10.1080/01490450252864253
    • Nevin, K. P. & Lovley, D. R. Mechanisms for Fe(III) oxide reduction in sedimentary environments. Geomicrobiol. J. 19, 141-159, DOI: 10.1080/01490450252864253 (2002). (Pubitemid 34497662)
    • (2002) Geomicrobiology Journal , vol.19 , Issue.2 , pp. 141-159
    • Nevin, K.P.1    Lovley, D.R.2
  • 22
    • 23744478281 scopus 로고    scopus 로고
    • Shewanella oneidensis MR-1 uses overlapping pathways for iron reduction at a distance and by direct contact under conditions relevant for biofilms
    • DOI 10.1128/AEM.71.8.4414-4426.2005
    • Lies, D. P. et al. Shewanella oneidensis MR-1 uses overlapping pathways for iron reduction at a distance and by direct contact under conditions relevant for biofilms. Appl. Environ. Microbiol. 71, 4414-4426, DOI:10.1128/Aem.71.8. 4414-4426.2005 (2005). (Pubitemid 41129495)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.8 , pp. 4414-4426
    • Lies, D.P.1    Hernandez, M.E.2    Kappler, A.3    Mielke, R.E.4    Gralnick, J.A.5    Newman, D.K.6
  • 23
    • 78049289028 scopus 로고    scopus 로고
    • Probing electron transfer mechanisms in Shewanella oneidensis MR-1 using a nanoelectrode platform and single-cell imaging
    • DOI:10.1073/Pnas.1011699107
    • Jiang, X. C. et al. Probing electron transfer mechanisms in Shewanella oneidensis MR-1 using a nanoelectrode platform and single-cell imaging. P. Natl. Acad. Sci. USA 107, 16806-16810, DOI:10.1073/Pnas.1011699107 (2010).
    • (2010) P. Natl. Acad. Sci. USA , vol.107 , pp. 16806-16810
    • Jiang, X.C.1
  • 24
    • 84856242296 scopus 로고    scopus 로고
    • Shuttling happens: Soluble flavin mediators of extracellular electron transfer in Shewanella
    • DOI:10.1007/s00253-011-3653-0
    • Brutinel, E. D. & Gralnick, J. A. Shuttling happens: soluble flavin mediators of extracellular electron transfer in Shewanella. Appl. Environ. Microbiol. 93, 41-48, DOI:10.1007/s00253-011-3653-0 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.93 , pp. 41-48
    • Brutinel, E.D.1    Gralnick, J.A.2
  • 25
    • 84877334667 scopus 로고    scopus 로고
    • Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones
    • DOI:10.1073/pnas.1220823110
    • Okamoto, A., Hashimoto, K., Nealson, K. H. & Nakamura, R. Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones. P. Natl. Acad. Sci. USA 110, 7856-7861, DOI:10.1073/pnas. 1220823110 (2013).
    • (2013) P. Natl. Acad. Sci. USA , vol.110 , pp. 7856-7861
    • Okamoto, A.1    Hashimoto, K.2    Nealson, K.H.3    Nakamura, R.4
  • 26
    • 84863584372 scopus 로고    scopus 로고
    • The porin-cytochrome' model for microbe-to-mineral electron transfer
    • DOI:10.1111/j.1365-2958.2012.08088.x
    • Richardson, D. J. et al. The porin-cytochrome' model for microbe-to-mineral electron transfer. Mol. Microbiol. 85, 201-212, DOI:10.1111/j.1365-2958.2012.08088.x (2012).
    • (2012) Mol. Microbiol. , vol.85 , pp. 201-212
    • Richardson, D.J.1
  • 27
    • 0021102055 scopus 로고
    • Energetics of the One-Electron Reduction Steps of Riboflavin, Fmn and Fad toTheir Fully Reduced Forms
    • Anderson, R. F. Energetics of the One-Electron Reduction Steps of Riboflavin, Fmn and Fad toTheir Fully Reduced Forms. Biochim. Biophys. Acta 722, 158-162 (1983).
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 158-162
    • Anderson, R.F.1
  • 28
    • 0014670796 scopus 로고
    • The structure of a clostridial flavodoxin. I. Crystallographic characterization of the oxidized and semiquinone forms
    • Ludwig, M. L., Andersen, R. D., Mayhew, S. G. & Massey, V. The structure of a clostridial flavodoxin. I. Crystallographic characterization of the oxidized and semiquinone forms. J. Biol. Chem. 244, 6047-6048 (1969).
    • (1969) J. Biol. Chem. , vol.244 , pp. 6047-6048
    • Ludwig, M.L.1    Andersen, R.D.2    Mayhew, S.G.3    Massey, V.4
  • 29
    • 0030456586 scopus 로고    scopus 로고
    • The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hildenborough]
    • Zhou, Z. M. & Swenson, R. P. The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hildenborough]. Biochemistry 35, 15980-15988 (1996).
    • (1996) Biochemistry , vol.35 , pp. 15980-15988
    • Zhou, Z.M.1    Swenson, R.P.2
  • 31
    • 84864664396 scopus 로고    scopus 로고
    • Insights into the mechanism of electron transfer and sodium translocation of the Na(1)-pumping NADH:quinone oxidoreductase
    • DOI:10.1016/j.bbabio.2012.03.017
    • Juarez, O. & Barquera, B. Insights into the mechanism of electron transfer and sodium translocation of the Na(1)-pumping NADH:quinone oxidoreductase. Biochim. Biophys. Acta 1817, 1823-1832, DOI:10.1016/j.bbabio. 2012.03.017 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1823-1832
    • Juarez, O.1    Barquera, B.2
  • 32
    • 84863521885 scopus 로고    scopus 로고
    • The Crystal Structure of the Extracellular 11-heme Cytochrome UndA Reveals a Conserved 10-heme Motif and Defined Binding Site for Soluble Iron Chelates
    • DOI:10.1016/J.Str.2012.04.016
    • Edwards, M. J. et al. The Crystal Structure of the Extracellular 11-heme Cytochrome UndA Reveals a Conserved 10-heme Motif and Defined Binding Site for Soluble Iron Chelates. Structure 20, 1275-1284, DOI:10.1016/J.Str.2012.04.016 (2012).
    • (2012) Structure , vol.20 , pp. 1275-1284
    • Edwards, M.J.1
  • 33
    • 77953562742 scopus 로고    scopus 로고
    • Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry
    • DOI:10.1016/j.bpj.2010.03.049
    • Johs, A., Shi, L., Droubay, T., Ankner, J. F. & Liang, L. Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry. Biophys. J. 98, 3035-3043, DOI:10.1016/j.bpj.2010.03.049 (2010).
    • (2010) Biophys. J. , vol.98 , pp. 3035-3043
    • Johs, A.1    Shi, L.2    Droubay, T.3    Ankner, J.F.4    Liang, L.5
  • 34
    • 0027955916 scopus 로고
    • Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): Regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions
    • DOI 10.1021/bi00194a015
    • Swenson, R. P. & Krey, G. D. Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions. Biochemistry 33, 8505-8514 (1994). (Pubitemid 24242688)
    • (1994) Biochemistry , vol.33 , Issue.28 , pp. 8505-8514
    • Swenson, R.P.1    Krey, G.D.2
  • 35
    • 0345446815 scopus 로고
    • Analytical Evaluation of Differential Pulse Voltammetry at Stationary Electrodes Using Computer-Based Instrumentation
    • DOI:10.1021/Ac50008a031
    • Rifkin, S. C. & Evans, D. H. Analytical Evaluation of Differential Pulse Voltammetry at Stationary Electrodes Using Computer-Based Instrumentation. Anal. Chem. 48, 2174-2180, DOI:10.1021/Ac50008a031 (1976).
    • (1976) Anal. Chem. , vol.48 , pp. 2174-2180
    • Rifkin, S.C.1    Evans, D.H.2
  • 36
    • 37349000206 scopus 로고    scopus 로고
    • Binding and direct electrochemistry of OmcA, an outermembrane cytochrome fromaniron reducing bacterium, with oxide electrodes: A candidate biofuel cell system
    • DOI:10.1016/j.ica.2007.07.015
    • Eggleston, C. M. et al. Binding and direct electrochemistry of OmcA, an outermembrane cytochrome fromaniron reducing bacterium, with oxide electrodes: A candidate biofuel cell system. Inorg. Chim. Acta 361, 769-777, DOI:10.1016/j.ica.2007.07.015 (2008).
    • (2008) Inorg. Chim. Acta , vol.361 , pp. 769-777
    • Eggleston, C.M.1
  • 37
    • 78649371078 scopus 로고    scopus 로고
    • An essential role for UshA in processing of extracellular flavin electron shuttles by Shewanella oneidensis
    • DOI:10.1111/j.1365-2958.2010.07353.x
    • Covington, E. D., Gelbmann, C. B., Kotloski, N. J. & Gralnick, J. A. An essential role for UshA in processing of extracellular flavin electron shuttles by Shewanella oneidensis. Mol. Microbiol. 78, 519-532, DOI:10.1111/j.1365-2958.2010.07353.x (2010).
    • (2010) Mol. Microbiol. , vol.78 , pp. 519-532
    • Covington, E.D.1    Gelbmann, C.B.2    Kotloski, N.J.3    Gralnick, J.A.4
  • 38
    • 77955382673 scopus 로고    scopus 로고
    • Modularity of the Mtr respiratory pathway of Shewanella oneidensis strain MR-1
    • DOI:10.1111/j.1365-2958.2010.07266.x
    • Coursolle, D. & Gralnick, J. A. Modularity of the Mtr respiratory pathway of Shewanella oneidensis strain MR-1. Mol. Microbiol. 77, 995-1008, DOI:10.1111/j.1365-2958.2010.07266.x (2010).
    • (2010) Mol. Microbiol. , vol.77 , pp. 995-1008
    • Coursolle, D.1    Gralnick, J.A.2
  • 39
    • 79957791476 scopus 로고    scopus 로고
    • In-vivo identification of direct electron transfer from Shewanella oneidensis MR-1 to electrodes via outermembrane OmcA-MtrCAB protein complexes
    • DOI:10.1016/j.electacta.2011.03.076
    • Okamoto, A., Nakamura, R. & Hashimoto, K. In-vivo identification of direct electron transfer from Shewanella oneidensis MR-1 to electrodes via outermembrane OmcA-MtrCAB protein complexes. Electrochim. Acta 56, 5526-5531, DOI:10.1016/j.electacta.2011.03.076 (2011).
    • (2011) Electrochim. Acta , vol.56 , pp. 5526-5531
    • Okamoto, A.1    Nakamura, R.2    Hashimoto, K.3
  • 40
    • 78449295718 scopus 로고    scopus 로고
    • Redox-responsive switching in bacterial respiratory pathways involving extracellular electron transfer
    • DOI:10.1002/cssc.201000213
    • Liu, H., Matsuda, S., Kato, S., Hashimoto, K. & Nakanishi, S. Redox-responsive switching in bacterial respiratory pathways involving extracellular electron transfer. ChemSusChem 3, 1253-1256, DOI:10.1002/cssc. 201000213 (2010).
    • (2010) ChemSusChem , vol.3 , pp. 1253-1256
    • Liu, H.1    Matsuda, S.2    Kato, S.3    Hashimoto, K.4    Nakanishi, S.5
  • 41
    • 84877352937 scopus 로고    scopus 로고
    • Controlling electron transfer at the microbe-mineral interface
    • DOI:10.1073/pnas.1305244110
    • Richardson, D. J., Butt, J. N. & Clarke, T. A. Controlling electron transfer at the microbe-mineral interface. P. Natl. Acad. Sci. USA 110, 7537-7538, DOI:10.1073/pnas.1305244110 (2013).
    • (2013) P. Natl. Acad. Sci. USA , vol.110 , pp. 7537-7538
    • Richardson, D.J.1    Butt, J.N.2    Clarke, T.A.3
  • 42
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: Sequence, folding, binding, function and beyond
    • DOI 10.1007/s00018-005-5514-4
    • Sancho, J. Flavodoxins: sequence, folding, binding, function and beyond. Cell. Mol. Life Sci. 63, 855-864, DOI:10.1007/s00018-005-5514-4 (2006). (Pubitemid 43724075)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.7-8 , pp. 855-864
    • Sancho, J.1
  • 43
    • 37349000206 scopus 로고    scopus 로고
    • Binding and direct electrochemistry of OmcA, an outermembrane cytochrome from an iron reducing bacterium, with oxide electrodes: A candidate biofuel cell system
    • DOI:10.1016/j.ica.2007.07.015
    • Eggleston, C. M. et al. Binding and direct electrochemistry of OmcA, an outermembrane cytochrome from an iron reducing bacterium, with oxide electrodes: A candidate biofuel cell system. Inorg. Chim. Acta 361, 769-777, DOI:10.1016/j.ica.2007.07.015 (2008).
    • (2008) Inorg. Chim. Acta , vol.361 , pp. 769-777
    • Eggleston, C.M.1
  • 45
    • 78249277165 scopus 로고    scopus 로고
    • Electrical current generation across a black smoker chimney
    • DOI:10.1002/anie.201003311
    • Nakamura, R. et al. Electrical current generation across a black smoker chimney. Angew. Chem. 49, 7692-7694, DOI:10.1002/anie.201003311 (2010).
    • (2010) Angew. Chem. , vol.49 , pp. 7692-7694
    • Nakamura, R.1
  • 46
    • 58249100149 scopus 로고    scopus 로고
    • Self-constructed electrically conductive bacterial networks
    • DOI:10.1002/anie.200804750
    • Nakamura, R., Kai, F., Okamoto, A., Newton, G. J. & Hashimoto, K. Self-constructed electrically conductive bacterial networks. Angew. Chem. Int. Ed. 48, 508-511, DOI:10.1002/anie.200804750 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 508-511
    • Nakamura, R.1    Kai, F.2    Okamoto, A.3    Newton, G.J.4    Hashimoto, K.5
  • 48
    • 84870218813 scopus 로고    scopus 로고
    • Analysis of structural MtrC models based on homology with the crystal structure of MtrF
    • DOI:10.1042/BST20120132
    • Edwards, M. J., Fredrickson, J. K., Zachara, J. M., Richardson, D. J. & Clarke, T. A. Analysis of structural MtrC models based on homology with the crystal structure of MtrF. Biochem. Soc. Trans. 40, 1181-1185, DOI:10.1042/BST20120132 (2012).
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1181-1185
    • Edwards, M.J.1    Fredrickson, J.K.2    Zachara, J.M.3    Richardson, D.J.4    Clarke, T.A.5
  • 49
    • 0034623005 scopus 로고    scopus 로고
    • Coffee: A novel method for fast and accurate multiple sequence alignment
    • DOI:10.1006/jmbi.2000.4042
    • Notredame, C., Higgins, D. G. & Heringa, J.T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217, DOI:10.1006/jmbi.2000.4042 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.T.3
  • 50
    • 0031454750 scopus 로고    scopus 로고
    • A flavodoxin that is required for enzyme activation: The structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution
    • Hoover, D. M. & Ludwig, M. L. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution. Protein Sci. 6, 2525-2537, DOI:10.1002/pro.5560061205 (1997). (Pubitemid 28006690)
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2525-2537
    • Hoover, D.M.1    Ludwig, M.L.2
  • 51
    • 4744337841 scopus 로고    scopus 로고
    • Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 bioI
    • DOI 10.1021/bi049131t
    • Lawson, R. J., von Wachenfeldt, C., Haq, I., Perkins, J. & Munro, A. W. Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI. Biochemistry 43, 12390-12409, DOI:10.1021/bi049131t (2004). (Pubitemid 39314702)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12390-12409
    • Lawson, R.J.1    Von Wachenfeldt, C.2    Haq, I.3    Perkins, J.4    Munro, A.W.5
  • 52
    • 70350539306 scopus 로고    scopus 로고
    • &hashimoto K K.
    • DOI:10.1002/cbic.200900422
    • Okamoto, A., Nakamura, R., Ishii, K. &Hashimoto, K. In vivo electrochemistry of C-type cytochrome-mediated electron-transfer with chemical marking. ChemBioChem 10, 2329-2332, DOI:10.1002/cbic.200900422 (2009).
    • (2009) ChemBioChem , vol.10 , pp. 2329-2332
    • Okamoto, A.1    Nakamura, R.2    Ishii3
  • 53
    • 65549089956 scopus 로고    scopus 로고
    • Antibody Recognition Force Microscopy Shows that Outer Membrane Cytochromes OmcA and MtrC Are Expressed on the Exterior Surface of Shewanella oneidensis MR-1
    • DOI:10.1128/Aem.02108-08
    • Lower, B. H. et al. Antibody Recognition Force Microscopy Shows that Outer Membrane Cytochromes OmcA and MtrC Are Expressed on the Exterior Surface of Shewanella oneidensis MR-1. Appl. Environ. Microbiol. 75, 2931-2935, DOI:10.1128/Aem.02108-08 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2931-2935
    • Lower, B.H.1
  • 54
    • 73649141295 scopus 로고    scopus 로고
    • The Mtr Respiratory Pathway Is Essential for Reducing Flavins and Electrodes in Shewanella oneidensis
    • Coursoll, D., Baron, B. D., Bond, D. R., Gralnick, A. J. The Mtr Respiratory Pathway Is Essential for Reducing Flavins and Electrodes in Shewanella oneidensis. J. Bacteirol. 192, 467-474 (2010).
    • (2010) J. Bacteirol. , vol.192 , pp. 467-474
    • Coursoll, D.1    Baron, B.D.2    Bond, D.R.3    Gralnick, A.J.4
  • 55
    • 70349278381 scopus 로고    scopus 로고
    • Role of iron-reducing bacteira in corrosion and protection of carbon steel
    • Herrera, K. L. & Videla, A. H. Role of iron-reducing bacteira in corrosion and protection of carbon steel. Int. Biodeterior. Biodegrad. 63, 891-895 (2009).
    • (2009) Int. Biodeterior. Biodegrad. , vol.63 , pp. 891-895
    • Herrera, K.L.1    Videla, A.H.2
  • 56
    • 79957791476 scopus 로고    scopus 로고
    • In-vivo identification of direct electron transfer from Shewanella oneidensis MR-1 to electrodes via outermembrane OmcA-MtrCAB protein complexes
    • DOI:10.1002/cbic.200900422
    • Okamoto, A., Nakamura, R. & Hashimoto, K. In-vivo identification of direct electron transfer from Shewanella oneidensis MR-1 to electrodes via outermembrane OmcA-MtrCAB protein complexes. Electrochim. Acta 56, 5526-5531, DOI:10.1002/cbic.200900422 (2011).
    • (2011) Electrochim. Acta , vol.56 , pp. 5526-5531
    • Okamoto, A.1    Nakamura, R.2    Hashimoto, K.3
  • 58
    • 68549123548 scopus 로고    scopus 로고
    • SOAS: A free program to analyze electrochemical data and other one-dimensional signals
    • DOI:10.1016/j.bioelechem.2009.02.010
    • Fourmond, V. et al. SOAS: a free program to analyze electrochemical data and other one-dimensional signals. Bioelectrochemistry 76, 141-147, DOI:10.1016/j.bioelechem.2009.02.010 (2009).
    • (2009) Bioelectrochemistry , vol.76 , pp. 141-147
    • Fourmond, V.1


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