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Volumn , Issue , 2016, Pages 187-216

Microbial Redox Proteins and Protein Complexes for Extracellular Respiration

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EID: 85141055521     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b19087-12     Document Type: Chapter
Times cited : (5)

References (149)
  • 1
    • 36148976471 scopus 로고    scopus 로고
    • Anaerobic elemental sulfur reduction by fungus Fusarium oxysporum
    • Abe, T., Hoshino, T., Nakamura, A., and Takaya, N. (2007). Anaerobic elemental sulfur reduction by fungus Fusarium oxysporum. Biosci Biotechnol Biochem 71: 2402-2407.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 2402-2407
    • Abe, T.1    Hoshino, T.2    Nakamura, A.3    Takaya, N.4
  • 2
    • 84874772938 scopus 로고    scopus 로고
    • Proteins involved in electron transfer to Fe(III) and Mn(IV) oxides by Geobacter sulfurreducens and Geobacter uraniireducens
    • Aklujkar, M., Coppi, M. V., Leang, C., Kim, B. C., Chavan, M. A., Perpetua, L. A. et al. (2013). Proteins involved in electron transfer to Fe(III) and Mn(IV) oxides by Geobacter sulfurreducens and Geobacter uraniireducens. Microbiology 159: 515-535.
    • (2013) Microbiology , vol.159 , pp. 515-535
    • Aklujkar, M.1    Coppi, M.V.2    Leang, C.3    Kim, B.C.4    Chavan, M.A.5    Perpetua, L.A.6
  • 3
    • 0035093350 scopus 로고    scopus 로고
    • Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and bacteria
    • Amend, J. P., and Shock, E. L. (2001). Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and bacteria. FEMS Microbiol Rev 25: 175-243.
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 175-243
    • Amend, J.P.1    Shock, E.L.2
  • 4
    • 79960098417 scopus 로고    scopus 로고
    • Extracellular reduction of hexavalant chromium by cytochromes MtrC and OmcA of Shewanella oneidensis MR-1
    • Belchik, S. M., Kennedy, D. W, Dohnalkova, A. C., Wang, Y., Sevinc, P. C., Wu, H. et al. (2011). Extracellular reduction of hexavalant chromium by cytochromes MtrC and OmcA of Shewanella oneidensis MR-1. Appl Environ Microbiol 77: 4035-4041.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 4035-4041
    • Belchik, S.M.1    Kennedy, D.W.2    Dohnalkova, A.C.3    Wang, Y.4    Sevinc, P.C.5    Wu, H.6
  • 5
    • 84893120256 scopus 로고    scopus 로고
    • Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph Rhodopseudomonas palustris TIE-1
    • Bird, L. J., Saraiva, I. H., Park, S., Calcada, E. O., Salgueiro, C. A., Nitschke, W. et al. (2014). Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph Rhodopseudomonas palustris TIE-1. J Bacteriol 196: 850-858.
    • (2014) J Bacteriol , vol.196 , pp. 850-858
    • Bird, L.J.1    Saraiva, I.H.2    Park, S.3    Calcada, E.O.4    Salgueiro, C.A.5    Nitschke, W.6
  • 8
    • 58549098226 scopus 로고    scopus 로고
    • Bioreduction of hematite nanoparticles by the dissimilatory iron reducing bacterium Shewanella oneidensis MR-1
    • Bose, S., Hochella, M. F., Gorby, Y., Kennedy, D. W., McCready, D. E., Madded, A. S., and Lower, B. H. (2009). Bioreduction of hematite nanoparticles by the dissimilatory iron reducing bacterium Shewanella oneidensis MR-1. Geochim Cosmochim Acta 73: 962-976.
    • (2009) Geochim Cosmochim Acta , vol.73 , pp. 962-976
    • Bose, S.1    Hochella, M.F.2    Gorby, Y.3    Kennedy, D.W.4    McCready, D.E.5    Madded, A.S.6    Lower, B.H.7
  • 9
    • 84892599448 scopus 로고    scopus 로고
    • Electron flow in multiheme bacterial cytochromes is a balancing act between heme electronic interaction and redox potentials
    • Breuer, M., Rosso, K. M., and Blumberger, J. (2014). Electron flow in multiheme bacterial cytochromes is a balancing act between heme electronic interaction and redox potentials. Proc Natl Acad Sci U S A 111: 611-616.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 611-616
    • Breuer, M.1    Rosso, K.M.2    Blumberger, J.3
  • 10
    • 84862556362 scopus 로고    scopus 로고
    • Thermodynamics of electron flow in the bacterial deca-heme cytochrome MtrF
    • (a)
    • Breuer, M., Zarzycki, P., Blumberger, J., and Rosso, K. M. (2012a). Thermodynamics of electron flow in the bacterial deca-heme cytochrome MtrF. J Am Chem Soc 134: 9868-9871.
    • (2012) J am Chem Soc , vol.134 , pp. 9868-9871
    • Breuer, M.1    Zarzycki, P.2    Blumberger, J.3    Rosso, K.M.4
  • 11
    • 84870192418 scopus 로고    scopus 로고
    • Molecular structure and free energy landscape for electron transport in the decahaem cytochrome MtrF
    • (b)
    • Breuer, M., Zarzycki, P., Shi, L., Clarke, T. A., Edwards, M. J., Butt, J. N. et al. (2012b). Molecular structure and free energy landscape for electron transport in the decahaem cytochrome MtrF. Biochem Soc Trans 40: 1198-1203.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1198-1203
    • Breuer, M.1    Zarzycki, P.2    Shi, L.3    Clarke, T.A.4    Edwards, M.J.5    Butt, J.N.6
  • 12
    • 84856242296 scopus 로고    scopus 로고
    • Shuttling happens: Soluble flavin mediators of extracellular electron transfer in Shewanella
    • Brutinel, E. D., and Gralnick, J. A. (2012). Shuttling happens: Soluble flavin mediators of extracellular electron transfer in Shewanella. Appl Microbiol Biotechnol 93: 41-48.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 41-48
    • Brutinel, E.D.1    Gralnick, J.A.2
  • 13
    • 68549130741 scopus 로고    scopus 로고
    • Anaerobic respiration of elemental sulfur and thiosul-fate by Shewanella oneidensis MR-1 requires psrA, a homolog of the phsA gene of Salmonella enterica serovar typhimurium LT2
    • Burns, J. L., and DiChristina, T. J. (2009). Anaerobic respiration of elemental sulfur and thiosul-fate by Shewanella oneidensis MR-1 requires psrA, a homolog of the phsA gene of Salmonella enterica serovar typhimurium LT2. Appl Environ Microbiol 75: 5209-5217.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5209-5217
    • Burns, J.L.1    Dichristina, T.J.2
  • 14
    • 77955297300 scopus 로고    scopus 로고
    • Complete genome sequence of the electricity-producing “Thermincola potens” strain JR
    • Byrne-Bailey, K. G., Wrighton, K. C., Melnyk, R. A., Agbo, P., Hazen, T. C., and Coates, J. D. (2010). Complete genome sequence of the electricity-producing “Thermincola potens” strain JR. J Bacteriol 192: 4078-4079.
    • (2010) J Bacteriol , vol.192 , pp. 4078-4079
    • Byrne-Bailey, K.G.1    Wrighton, K.C.2    Melnyk, R.A.3    Agbo, P.4    Hazen, T.C.5    Coates, J.D.6
  • 15
    • 0028050079 scopus 로고
    • Geobacter sulfurreducens sp. nov., a hydrogen- and acetate-oxidizing dissimilatory metal-reducing microorganism
    • Caccavo, F., Jr., Lonergan, D. J., Lovley, D. R., Davis, M., Stolz, J. F., and McInerney, M. J. (1994). Geobacter sulfurreducens sp. nov., a hydrogen- and acetate-oxidizing dissimilatory metal-reducing microorganism. Appl Environ Microbiol 60: 3752-3759.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3752-3759
    • Caccavo, F.1    Lonergan, D.J.2    Lovley, D.R.3    Davis, M.4    Stolz, J.F.5    McInerney, M.J.6
  • 16
    • 79959901624 scopus 로고    scopus 로고
    • Contribution of extracellular polymeric substances from Shewanella sp. HRCR-1 biofilms to U(VI) immobilization
    • (a)
    • Cao, B., Ahmed, B., Kennedy, D. W., Wang, Z., Shi, L., Marshall, M. J. et al. (2011a). Contribution of extracellular polymeric substances from Shewanella sp. HRCR-1 biofilms to U(VI) immobilization. Environ Sci Technol 45: 5483-5490.
    • (2011) Environ Sci Technol , vol.45 , pp. 5483-5490
    • Cao, B.1    Ahmed, B.2    Kennedy, D.W.3    Wang, Z.4    Shi, L.5    Marshall, M.J.6
  • 17
    • 79953277727 scopus 로고    scopus 로고
    • Extracellular polymeric substances from Shewanella sp. HRCR-1 biofilms: Characterization by infrared spectroscopy and proteomics
    • (b)
    • Cao, B., Shi, L., Brown, R. N., Xiong, Y., Fredrickson, J. K., Romine, M. F. et al. (2011b). Extracellular polymeric substances from Shewanella sp. HRCR-1 biofilms: Characterization by infrared spectroscopy and proteomics. Environ Microbiol 13: 1018-1031.
    • (2011) Environ Microbiol , vol.13 , pp. 1018-1031
    • Cao, B.1    Shi, L.2    Brown, R.N.3    Xiong, Y.4    Fredrickson, J.K.5    Romine, M.F.6
  • 18
    • 84857127335 scopus 로고    scopus 로고
    • Surface multiheme c-type cytochromes from Thermincola potens and implications for respiratory metal reduction by Gram-positive bacteria
    • Carlson, H. K., Iavarone, A. T., Gorur, A., Yeo, B. S., Tran, R., Melnyk, R. A. et al. (2012). Surface multiheme c-type cytochromes from Thermincola potens and implications for respiratory metal reduction by Gram-positive bacteria. Proc Natl Acad Sci U S A 109: 1702-1707.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1702-1707
    • Carlson, H.K.1    Iavarone, A.T.2    Gorur, A.3    Yeo, B.S.4    Tran, R.5    Melnyk, R.A.6
  • 19
    • 84883287892 scopus 로고    scopus 로고
    • Extraordinary phylogenetic diversity and metabolic versatility in aquifer sediment
    • Castelle, C. J., Hug, L. A., Wrighton, K. C., Thomas, B. C., Williams, K. H., Wu, D. et al. (2013). Extraordinary phylogenetic diversity and metabolic versatility in aquifer sediment. Nat Commun 4: 2120.
    • (2013) Nat Commun , vol.4 , pp. 2120
    • Castelle, C.J.1    Hug, L.A.2    Wrighton, K.C.3    Thomas, B.C.4    Williams, K.H.5    Wu, D.6
  • 20
    • 34547829281 scopus 로고    scopus 로고
    • The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA
    • Clarke, T. A., Cole, J. A., Richardson, D. J., and Hemmings, A. M. (2007). The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA. Biochem J406: 19-30.
    • (2007) Biochem , vol.J406 , pp. 19-30
    • Clarke, T.A.1    Cole, J.A.2    Richardson, D.J.3    Hemmings, A.M.4
  • 22
    • 80053080692 scopus 로고    scopus 로고
    • Extracellular reduction of uranium via Geobacter conductive pili as a protective cellular mechanism
    • Cologgi, D. L., Lampa-Pastirk, S., Speers, A. M., Kelly, S. D., and Reguera, G. (2011). Extracellular reduction of uranium via Geobacter conductive pili as a protective cellular mechanism. Proc Natl Acad Sci U S A 108: 15248-15252.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15248-15252
    • Cologgi, D.L.1    Lampa-Pastirk, S.2    Speers, A.M.3    Kelly, S.D.4    Reguera, G.5
  • 23
    • 73649141295 scopus 로고    scopus 로고
    • The Mtr respiratory pathway is essential for reducing flavins and electrodes in Shewanella oneidensis
    • Coursolle, D., Baron, D. B., Bond, D. R., and Gralnick, J. A. (2010). The Mtr respiratory pathway is essential for reducing flavins and electrodes in Shewanella oneidensis. JBacteriol 192: 467-474.
    • (2010) Jbacteriol , vol.192 , pp. 467-474
    • Coursolle, D.1    Baron, D.B.2    Bond, D.R.3    Gralnick, J.A.4
  • 24
    • 77955382673 scopus 로고    scopus 로고
    • Modularity of the Mtr respiratory pathway of Shewanella oneidensis strain MR-1
    • Coursolle, D., and Gralnick, J. A. (2010). Modularity of the Mtr respiratory pathway of Shewanella oneidensis strain MR-1. Mol Microbiol 77: 995-1008.
    • (2010) Mol Microbiol , vol.77 , pp. 995-1008
    • Coursolle, D.1    Gralnick, J.A.2
  • 25
    • 33747872707 scopus 로고    scopus 로고
    • Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions
    • Craig, L., Volkmann, N., Arvai, A. S., Pique, M. E., Yeager, M., Egelman, E. H. and Tainer, J. A. (2006). Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions. Mol Cell 23: 651-662.
    • (2006) Mol Cell , vol.23 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, E.H.6    Tainer, J.A.7
  • 26
    • 0036135465 scopus 로고    scopus 로고
    • Dissimilatory Fe(III) and Mn(IV) reduction by Shewanella putrefaciens requires ferE, a homolog of the pulE (gspE) type II protein secretion gene
    • DiChristina, T. J., Moore, C. M., and Haller, C. A. (2002). Dissimilatory Fe(III) and Mn(IV) reduction by Shewanella putrefaciens requires ferE, a homolog of the pulE (gspE) type II protein secretion gene. J Bacteriol 184: 142-151.
    • (2002) J Bacteriol , vol.184 , pp. 142-151
    • Dichristina, T.J.1    Moore, C.M.2    Haller, C.A.3
  • 27
    • 33746072949 scopus 로고    scopus 로고
    • The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions
    • Ding, Y. H., Hixson, K. K., Giometti, C. S., Stanley, A., Esteve-Nunez, A., Khare, T. et al. (2006). The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions. Biochim Biophys Acta 1764: 1198-1206.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1198-1206
    • Ding, Y.H.1    Hixson, K.K.2    Giometti, C.S.3    Stanley, A.4    Esteve-Nunez, A.5    Khare, T.6
  • 29
    • 47249116228 scopus 로고    scopus 로고
    • The c-type cytochrome OmcA localizes to the outer membrane upon heterologous expression in Escherichia coli
    • Donald, J. W., Hicks, M. G., Richardson, D. J., and Palmer, T. (2008). The c-type cytochrome OmcA localizes to the outer membrane upon heterologous expression in Escherichia coli. J Bacteriol 190: 5127-5131.
    • (2008) J Bacteriol , vol.190 , pp. 5127-5131
    • Donald, J.W.1    Hicks, M.G.2    Richardson, D.J.3    Palmer, T.4
  • 30
    • 84900412960 scopus 로고    scopus 로고
    • The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface
    • Edwards, M. J., Baiden, N. A., Johs, A., Tomanicek, S. J., Liang, L., Shi, L. et al. (2014). The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface. FEBS Lett 588: 1886-1890.
    • (2014) FEBS Lett , vol.588 , pp. 1886-1890
    • Edwards, M.J.1    Baiden, N.A.2    Johs, A.3    Tomanicek, S.J.4    Liang, L.5    Shi, L.6
  • 31
    • 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
    • Edwards, M. J., Hall, A., Shi, L., Fredrickson, J. K., Zachara, J. M., Butt, J. N. et al. (2012). 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.
    • (2012) Structure , vol.20 , pp. 1275-1284
    • Edwards, M.J.1    Hall, A.2    Shi, L.3    Fredrickson, J.K.4    Zachara, J.M.5    Butt, J.N.6
  • 32
    • 46749105548 scopus 로고    scopus 로고
    • The molecular density of states in bacterial nanowires
    • El-Naggar, M. Y., Gorby, Y. A., Xia, W., and Nealson, K. H. (2008). The molecular density of states in bacterial nanowires. Biophys J 95: L10-L12.
    • (2008) Biophys J , vol.95 , pp. L10-L12
    • El-Naggar, M.Y.1    Gorby, Y.A.2    Xia, W.3    Nealson, K.H.4
  • 34
    • 84885414968 scopus 로고    scopus 로고
    • Comparative genomics of freshwater Fe-oxidizing bacteria: Implications for physiology, ecology, and systematics
    • Emerson, D., Field, E. K., Chertkov, O., Davenport, K. W., Goodwin, L., Munk, C. et al. (2013). Comparative genomics of freshwater Fe-oxidizing bacteria: Implications for physiology, ecology, and systematics. Front Microbiol 4: 254.
    • (2013) Front Microbiol , vol.4 , pp. 254
    • Emerson, D.1    Field, E.K.2    Chertkov, O.3    Davenport, K.W.4    Goodwin, L.5    Munk, C.6
  • 35
    • 80053126368 scopus 로고    scopus 로고
    • Solution-based structural analysis of the decaheme cytochrome, MtrA, by small angle X-ray scattering and analytical ultracentrifugation
    • Firer-Sherwood, M. A., Ando, N., Drennan, C. L., and Elliott, S. J. (2011). Solution-based structural analysis of the decaheme cytochrome, MtrA, by small angle X-ray scattering and analytical ultracentrifugation. J Phys Chem B 115: 11208-11214.
    • (2011) J Phys Chem B , vol.115 , pp. 11208-11214
    • Firer-Sherwood, M.A.1    Ando, N.2    Drennan, C.L.3    Elliott, S.J.4
  • 36
    • 79953797707 scopus 로고    scopus 로고
    • Tools for resolving complexity in the electron transfer networks of multiheme cytochromes c
    • Firer-Sherwood, M. A., Bewley, K. D., Mock, J. Y., and Elliott, S. J. (2011). Tools for resolving complexity in the electron transfer networks of multiheme cytochromes c. Metallomics 3: 344-348.
    • (2011) Metallomics , vol.3 , pp. 344-348
    • Firer-Sherwood, M.A.1    Bewley, K.D.2    Mock, J.Y.3    Elliott, S.J.4
  • 37
    • 84870912011 scopus 로고    scopus 로고
    • Mind the gap: Cytochrome interactions reveal electron pathways across the periplasm of Shewanella oneidensis MR-1
    • Fonseca, B. M., Paquete, C. M., Neto, S. E., Pacheco, I., Soares, C. M., and Louro, R. O. (2013). Mind the gap: Cytochrome interactions reveal electron pathways across the periplasm of Shewanella oneidensis MR-1. Biochem J 449: 101-108.
    • (2013) Biochem J , vol.449 , pp. 101-108
    • Fonseca, B.M.1    Paquete, C.M.2    Neto, S.E.3    Pacheco, I.4    Soares, C.M.5    Louro, R.O.6
  • 39
    • 84865828790 scopus 로고    scopus 로고
    • Fe(III) oxide reduction a Gram-positive thermophile: Physiological mechanisms for dissimilatory reduction of poorly crystalline Fe(III) oxide by a thermophilic Gram-positive bacterium Carboxydothermus ferrireducens
    • Gavrilov, S. N., Lloyd, J. R., Kostrikina, N. A., and Slobodkin, A. I. (2012). Fe(III) oxide reduction a Gram-positive thermophile: Physiological mechanisms for dissimilatory reduction of poorly crystalline Fe(III) oxide by a thermophilic Gram-positive bacterium Carboxydothermus ferrireducens. Geomicrobiol J 29: 804-819.
    • (2012) Geomicrobiol J , vol.29 , pp. 804-819
    • Gavrilov, S.N.1    Lloyd, J.R.2    Kostrikina, N.A.3    Slobodkin, A.I.4
  • 41
    • 33746624663 scopus 로고    scopus 로고
    • Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms
    • Gorby, Y. A., Yanina, S., McLean, J. S., Rosso, K. M., Moyles, D., Dohnalkova, A. et al. (2006). Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms. Proc Natl Acad Sci U S A 103: 11358-11363.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11358-11363
    • Gorby, Y.A.1    Yanina, S.2    McLean, J.S.3    Rosso, K.M.4    Moyles, D.5    Dohnalkova, A.6
  • 42
    • 34250667826 scopus 로고    scopus 로고
    • Extracellular respiration
    • Gralnick, J. A., and Newman, D. K. (2007). Extracellular respiration. Mol Microbiol 65: 1-11.
    • (2007) Mol Microbiol , vol.65 , pp. 1-11
    • Gralnick, J.A.1    Newman, D.K.2
  • 43
    • 33645224039 scopus 로고    scopus 로고
    • Extracellular respiration of dimethyl sulfoxide by Shewanella oneidensis strain MR-1
    • Gralnick, J. A., Vali, H., Lies, D. P., and Newman, D. K. (2006). Extracellular respiration of dimethyl sulfoxide by Shewanella oneidensis strain MR-1. Proc Natl Acad Sci U S A 103: 4669-4674.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4669-4674
    • Gralnick, J.A.1    Vali, H.2    Lies, D.P.3    Newman, D.K.4
  • 44
    • 34548393635 scopus 로고    scopus 로고
    • Characterization of Shewanella oneidensis MtrC: A cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors
    • Hartshorne, R. S., Jepson, B. N., Clarke, T. A., Field, S. J., Fredrickson, J., Zachara, J. et al. (2007). Characterization of Shewanella oneidensis MtrC: A cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors. J Biol Inorg Chem 12: 1083-1094.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 1083-1094
    • Hartshorne, R.S.1    Jepson, B.N.2    Clarke, T.A.3    Field, S.J.4    Fredrickson, J.5    Zachara, J.6
  • 45
  • 46
    • 46249094501 scopus 로고    scopus 로고
    • Genes for two multicopper proteins required for Fe(III) oxide reduction in Geobacter sulfurre-ducens have different expression patterns both in the subsurface and on energy-harvesting electrodes
    • Holmes, D. E., Mester, T., O’Neil, R. A., Perpetua, L. A., Larrahondo, M. J., Glaven, R. et al. (2008). Genes for two multicopper proteins required for Fe(III) oxide reduction in Geobacter sulfurre-ducens have different expression patterns both in the subsurface and on energy-harvesting electrodes. Microbiology 154: 1422-1435.
    • (2008) Microbiology , vol.154 , pp. 1422-1435
    • Holmes, D.E.1    Mester, T.2    O’Neil, R.A.3    Perpetua, L.A.4    Larrahondo, M.J.5    Glaven, R.6
  • 47
    • 79951630868 scopus 로고    scopus 로고
    • Specific localization of the c-type cytochrome OmcZ at the anode surface in current-producing biofilms of Geobacter sulfurreducens
    • Inoue, K., Leang, C., Franks, A. E., Woodard, T. L., Nevin, K. P., and Lovley, D. R. (2011). Specific localization of the c-type cytochrome OmcZ at the anode surface in current-producing biofilms of Geobacter sulfurreducens. Environ Microbiol Rep 3: 211-217.
    • (2011) Environ Microbiol Rep , vol.3 , pp. 211-217
    • Inoue, K.1    Leang, C.2    Franks, A.E.3    Woodard, T.L.4    Nevin, K.P.5    Lovley, D.R.6
  • 48
    • 77953637460 scopus 로고    scopus 로고
    • Purification and characterization of OmcZ, an outer-surface, octaheme c-type cytochrome essential for optimal current production by Geobacter sulfurreducens
    • Inoue, K., Qian, X., Morgado, L., Kim, B. C., Mester, T., Izallalen, M. et al. (2010). Purification and characterization of OmcZ, an outer-surface, octaheme c-type cytochrome essential for optimal current production by Geobacter sulfurreducens. Appl Environ Microbiol 76: 3999-4007.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3999-4007
    • Inoue, K.1    Qian, X.2    Morgado, L.3    Kim, B.C.4    Mester, T.5    Izallalen, M.6
  • 49
    • 33947358262 scopus 로고    scopus 로고
    • The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1
    • Jiao, Y., and Newman, D. K. (2007). The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1. JBacteriol 189: 1765-1773.
    • (2007) Jbacteriol , vol.189 , pp. 1765-1773
    • Jiao, Y.1    Newman, D.K.2
  • 50
    • 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
    • Johs, A., Shi, L., Droubay, T., Ankner, J. F., and Liang, L. (2010). Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry. Biophys J98: 3035-3043.
    • (2010) Biophys , vol.J98 , pp. 3035-3043
    • Johs, A.1    Shi, L.2    Droubay, T.3    Ankner, J.F.4    Liang, L.5
  • 53
    • 24344443251 scopus 로고    scopus 로고
    • Adaptation to disruption of the electron transfer pathway for Fe(III) reduction in Geobacter sulfurreducens
    • Leang, C., Adams, L. A., Chin, K. J., Nevin, K. P., Methe, B. A., Webster, J. et al. (2005). Adaptation to disruption of the electron transfer pathway for Fe(III) reduction in Geobacter sulfurreducens. J Bacteriol 187: 5918-5926.
    • (2005) J Bacteriol , vol.187 , pp. 5918-5926
    • Leang, C.1    Adams, L.A.2    Chin, K.J.3    Nevin, K.P.4    Methe, B.A.5    Webster, J.6
  • 54
    • 0037379469 scopus 로고    scopus 로고
    • OmcB, a c-type polyheme cytochrome, involved in Fe(III) reduction in Geobacter sulfurreducens
    • Leang, C., Coppi, M. V., and Lovley, D. R. (2003). OmcB, a c-type polyheme cytochrome, involved in Fe(III) reduction in Geobacter sulfurreducens. J Bacteriol 185: 2096-2103.
    • (2003) J Bacteriol , vol.185 , pp. 2096-2103
    • Leang, C.1    Coppi, M.V.2    Lovley, D.R.3
  • 55
    • 77953645311 scopus 로고    scopus 로고
    • Alignment of the c-type cytochrome OmcS along pili of Geobacter sulfurreducens
    • Leang, C., Qian, X., Mester, T., and Lovley, D. R. (2010). Alignment of the c-type cytochrome OmcS along pili of Geobacter sulfurreducens. Appl Environ Microbiol 76: 4080-4084.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4080-4084
    • Leang, C.1    Qian, X.2    Mester, T.3    Lovley, D.R.4
  • 56
    • 84879086317 scopus 로고    scopus 로고
    • Shewanella oneidensis MR-1 bacterial nanowires exhibit p-type, tunable electronic behavior
    • Leung, K. M., Wanger, G., El-Naggar, M. Y., Gorby, Y., Southam, G., Lau, W. M. and Yang, J. (2013). Shewanella oneidensis MR-1 bacterial nanowires exhibit p-type, tunable electronic behavior. Nano Lett 13: 2407-2411.
    • (2013) Nano Lett , vol.13 , pp. 2407-2411
    • Leung, K.M.1    Wanger, G.2    El-Naggar, M.Y.3    Gorby, Y.4    Southam, G.5    Lau, W.M.6    Yang, J.7
  • 57
    • 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
    • Lies, D. P., Hernandez, M. E., Kappler, A., Mielke, R. E., Gralnick, J. A., and Newman, D. K. (2005). 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.
    • (2005) Appl Environ Microbiol , vol.71 , 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
  • 58
    • 84879372325 scopus 로고    scopus 로고
    • Fep-x) Ti(X)O4 nanoparticles as tunable probes of microbial metal oxidation
    • Liu, J., Pearce, C. I., Liu, C., Wang, Z., Shi, L., Arenholz, E., and Rosso, K. M. (2013). Fep-x) Ti(X)O4 nanoparticles as tunable probes of microbial metal oxidation. J Am Chem Soc 135: 8896-8907.
    • (2013) J am Chem Soc , vol.135 , pp. 8896-8907
    • Liu, J.1    Pearce, C.I.2    Liu, C.3    Wang, Z.4    Shi, L.5    Arenholz, E.6    Rosso, K.M.7
  • 59
    • 84863581057 scopus 로고    scopus 로고
    • Identification and characterization of MtoA: A decaheme c-type cytochrome of the neutrophilic Fe(II)-oxidizing bacterium Sideroxydans lithotrophicus ES-1
    • Liu, J., Wang, Z., Belchik, S. M., Edwards, M. J., Liu, C., Kennedy, D. W et al. (2012). Identification and characterization of MtoA: A decaheme c-type cytochrome of the neutrophilic Fe(II)-oxidizing bacterium Sideroxydans lithotrophicus ES-1. Front Microbiol 3: 37.
    • (2012) Front Microbiol , vol.3 , pp. 37
    • Liu, J.1    Wang, Z.2    Belchik, S.M.3    Edwards, M.J.4    Liu, C.5    Kennedy, D.W.6
  • 60
    • 84913534233 scopus 로고    scopus 로고
    • A trans-outer membrane porin-cytochrome protein complex for extracellular electron transfer by Geobacter sul-furreducens PCA
    • Liu, Y., Wang, Z., Liu, J., Levar, C., Edwards, M. J., Babauta, J. T. et al. (2014). A trans-outer membrane porin-cytochrome protein complex for extracellular electron transfer by Geobacter sul-furreducens PCA. Environ Microbiol Rep 6: 776-785.
    • (2014) Environ Microbiol Rep , vol.6 , pp. 776-785
    • Liu, Y.1    Wang, Z.2    Liu, J.3    Levar, C.4    Edwards, M.J.5    Babauta, J.T.6
  • 61
    • 0037266296 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of PpcA, a periplasmic c-type cytochrome in Geobacter sulfurreducens
    • Lloyd, J. R., Leang, C., Hodges Myerson, A. L., Coppi, M. V., Cuifo, S., Methe, B. et al. (2003). Biochemical and genetic characterization of PpcA, a periplasmic c-type cytochrome in Geobacter sulfurreducens. Biochem J 369: 153-161.
    • (2003) Biochem J , vol.369 , pp. 153-161
    • Lloyd, J.R.1    Leang, C.2    Hodges Myerson, A.L.3    Coppi, M.V.4    Cuifo, S.5    Methe, B.6
  • 62
    • 84870198378 scopus 로고    scopus 로고
    • The quest to achieve the detailed structural and functional characterization of CymA
    • Louro, R. O., and Paquete, C. M. (2012). The quest to achieve the detailed structural and functional characterization of CymA. Biochem Soc Trans 40: 1291-1294.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1291-1294
    • Louro, R.O.1    Paquete, C.M.2
  • 64
    • 7044222207 scopus 로고    scopus 로고
    • Dissimilatory Fe(III) and Mn(IV) reduction
    • Lovley, D. R., Holmes, D. E., and Nevin, K. P. (2004). Dissimilatory Fe(III) and Mn(IV) reduction. Adv Microb Physiol 49: 219-286.
    • (2004) Adv Microb Physiol , vol.49 , pp. 219-286
    • Lovley, D.R.1    Holmes, D.E.2    Nevin, K.P.3
  • 65
    • 0024191542 scopus 로고
    • Novel mode of microbial energy metabolism: Organic carbon oxidation coupled to dissimilatory reduction of iron or manganese
    • Lovley, D. R., and Phillips, E. J. (1988). Novel mode of microbial energy metabolism: Organic carbon oxidation coupled to dissimilatory reduction of iron or manganese. Appl Environ Microbiol 54: 1472-1480.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1472-1480
    • Lovley, D.R.1    Phillips, E.J.2
  • 68
    • 43749121443 scopus 로고    scopus 로고
    • In vitro evolution of a peptide with a hematite binding motif that may constitute a natural metal-oxide binding archetype
    • Lower, B. H., Lins, R. D., Oestreicher, Z., Straatsma, T. P., Hochella, M. F., Jr., Shi, L., and Lower, S. K. (2008). In vitro evolution of a peptide with a hematite binding motif that may constitute a natural metal-oxide binding archetype. Environ Sci Technol 42: 3821-3827.
    • (2008) Environ Sci Technol , vol.42 , pp. 3821-3827
    • Lower, B.H.1    Lins, R.D.2    Oestreicher, Z.3    Straatsma, T.P.4    Hochella, M.F.5    Shi, L.6    Lower, S.K.7
  • 69
    • 34347370683 scopus 로고    scopus 로고
    • Specific bonds between an iron oxide surface and outer membrane cytochromes MtrC and OmcA from Shewanella oneidensis MR-1
    • Lower, B. H., Shi, L., Yongsunthon, R., Droubay, T. C., McCready, D. E., and Lower, S. K. (2007). Specific bonds between an iron oxide surface and outer membrane cytochromes MtrC and OmcA from Shewanella oneidensis MR-1. J Bacteriol 189: 4944-4952.
    • (2007) J Bacteriol , vol.189 , pp. 4944-4952
    • Lower, B.H.1    Shi, L.2    Yongsunthon, R.3    Droubay, T.C.4    McCready, D.E.5    Lower, S.K.6
  • 71
    • 33144470047 scopus 로고    scopus 로고
    • Characterization of metabolism in the Fe(III)-reducing organism Geobacter sulfurreducens by constraint-based modeling
    • Mahadevan, R., Bond, D. R., Butler, J. E., Esteve-Nunez, A., Coppi, M. V., Palsson, B. O. et al. (2006). Characterization of metabolism in the Fe(III)-reducing organism Geobacter sulfurreducens by constraint-based modeling. Appl Environ Microbiol 72: 1558-1568.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1558-1568
    • Mahadevan, R.1    Bond, D.R.2    Butler, J.E.3    Esteve-Nunez, A.4    Coppi, M.V.5    Palsson, B.O.6
  • 73
    • 84880671902 scopus 로고    scopus 로고
    • Extracellular electron transfer to Fe(III) oxides by the hyperthermophilic archaeon Geoglobus ahangari via a direct contact mechanism
    • Manzella, M. P., Reguera, G., and Kashefi, K. (2013). Extracellular electron transfer to Fe(III) oxides by the hyperthermophilic archaeon Geoglobus ahangari via a direct contact mechanism. Appl Environ Microbiol 79: 4694-4700.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 4694-4700
    • Manzella, M.P.1    Reguera, G.2    Kashefi, K.3
  • 74
    • 84862202398 scopus 로고    scopus 로고
    • A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella
    • (a)
    • Marritt, S. J., Lowe, T. G., Bye, J., McMillan, D. G., Shi, L., Fredrickson, J. et al. (2012a). A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella. Biochem J444: 465-474.
    • (2012) Biochem , vol.J444 , pp. 465-474
    • Marritt, S.J.1    Lowe, T.G.2    Bye, J.3    McMillan, D.G.4    Shi, L.5    Fredrickson, J.6
  • 76
    • 85044708028 scopus 로고    scopus 로고
    • Wang, Z. et al. (2006). c-Type cytochrome-dependent formation of U(IV) nanoparticles by Shewanella oneidensis
    • Marshall, M. J., Beliaev, A. S., Dohnalkova, A. C., Kennedy, D. W., Shi, L., Wang, Z. et al. (2006). c-Type cytochrome-dependent formation of U(IV) nanoparticles by Shewanella oneidensis. PLoS Biol 4: e268.
    • Plos Biol , vol.4 , pp. e268
    • Marshall, M.J.1    Beliaev, A.S.2    Dohnalkova, A.C.3    Kennedy, D.W.4    Shi, L.5
  • 78
    • 84859951809 scopus 로고    scopus 로고
    • Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA
    • McMillan, D. G., Marritt, S. J., Butt, J. N., and Jeuken, L. J. (2012). Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA. J Biol Chem 2S7: 14215-14225.
    • (2012) J Biol Chem 2S7 , pp. 14215-14225
    • McMillan, D.G.1    Marritt, S.J.2    Butt, J.N.3    Jeuken, L.J.4
  • 79
    • 84880380265 scopus 로고    scopus 로고
    • Protein-protein interaction regulates the direction of catalysis and electron transfer in a redox enzyme complex
    • McMillan, D. G., Marritt, S. J., Firer-Sherwood, M. A., Shi, L., Richardson, D. J., Evans, S. D. et al. (2013). Protein-protein interaction regulates the direction of catalysis and electron transfer in a redox enzyme complex. J Am Chem Soc 135: 10550-10556.
    • (2013) J am Chem Soc , vol.135 , pp. 10550-10556
    • McMillan, D.G.1    Marritt, S.J.2    Firer-Sherwood, M.A.3    Shi, L.4    Richardson, D.J.5    Evans, S.D.6
  • 80
    • 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, S. E., Glaven, R., Lovley, D. R., and Mester, T. (2006). A putative multicopper protein secreted by an atypical type II secretion system involved in the reduction of insoluble electron acceptors in Geobacter sulfurreducens. Microbiology 152: 2257-2264.
    • (2006) Microbiology , vol.152 , pp. 2257-2264
    • Mehta, T.1    Childers, S.E.2    Glaven, R.3    Lovley, D.R.4    Mester, T.5
  • 81
    • 29144451480 scopus 로고    scopus 로고
    • Outer membrane c-type cytochromes required for Fe(III) and Mn(IV) oxide reduction in Geobacter sulfurreducens
    • Mehta, T., Coppi, M. V., Childers, S. E., and Lovley, D. R. (2005). Outer membrane c-type cytochromes required for Fe(III) and Mn(IV) oxide reduction in Geobacter sulfurreducens. Appl Environ Microbiol 71: 8634-8641.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8634-8641
    • Mehta, T.1    Coppi, M.V.2    Childers, S.E.3    Lovley, D.R.4
  • 82
    • 68149099862 scopus 로고    scopus 로고
    • Electrochemical interaction of Shewanella oneidensis MR-1 and its outer membrane cytochromes OmcA and MtrC with hematite electrodes
    • Meitl, L. A., Eggleston, C. M., Colberg, P. J. S., Khare, N., Reardon, C. L., and Shi, L. (2009). Electrochemical interaction of Shewanella oneidensis MR-1 and its outer membrane cytochromes OmcA and MtrC with hematite electrodes. Geochim Cosmochim Acta 2QQ9: 5292-5307.
    • (2009) Geochim Cosmochim Acta 2QQ9 , pp. 5292-5307
    • Meitl, L.A.1    Eggleston, C.M.2    Colberg, P.J.S.3    Khare, N.4    Reardon, C.L.5    Shi, L.6
  • 83
    • 84862227302 scopus 로고    scopus 로고
    • Role of outer membrane c-type cytochromes MtrC and OmcA in Shewanella oneidensis MR-1 cell production, accumulation, and detachment during respiration on hematite
    • Mitchell, A. C., Peterson, L., Reardon, C. L., Reed, S. B., Culley, D. E., Romine, M. R., and Geesey, G. G. (2012). Role of outer membrane c-type cytochromes MtrC and OmcA in Shewanella oneidensis MR-1 cell production, accumulation, and detachment during respiration on hematite. Geobiology 1Q: 355-370.
    • (2012) Geobiology , vol.1Q , pp. 355-370
    • Mitchell, A.C.1    Peterson, L.2    Reardon, C.L.3    Reed, S.B.4    Culley, D.E.5    Romine, M.R.6    Geesey, G.G.7
  • 84
    • 77954380092 scopus 로고    scopus 로고
    • Thermodynamic characterization of a triheme cytochrome family from Geobacter sulfurreducens reveals mechanistic and functional diversity
    • Morgado, L., Bruix, M., Pessanha, M., Londer, Y. Y., and Salgueiro, C. A. (2010). Thermodynamic characterization of a triheme cytochrome family from Geobacter sulfurreducens reveals mechanistic and functional diversity. Biophys J99: 293-301.
    • (2010) Biophys , vol.J99 , pp. 293-301
    • Morgado, L.1    Bruix, M.2    Pessanha, M.3    Londer, Y.Y.4    Salgueiro, C.A.5
  • 86
    • 33947183722 scopus 로고    scopus 로고
    • The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species
    • Murphy, J. N., and Saltikov, C. W. (2007). The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species. J Bacteriol 1S9: 2283-2290.
    • (2007) J Bacteriol 1S9 , pp. 2283-2290
    • Murphy, J.N.1    Saltikov, C.W.2
  • 87
    • 0031054309 scopus 로고    scopus 로고
    • Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefa-ciens MR-1
    • Myers, C. R., and Myers, J. M. (1997). Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefa-ciens MR-1. J Bacteriol 179: 1143-1152.
    • (1997) J Bacteriol , vol.179 , pp. 1143-1152
    • Myers, C.R.1    Myers, J.M.2
  • 88
    • 0042378909 scopus 로고    scopus 로고
    • Cell surface exposure of the outer membrane cytochromes of Shewanella oneidensis MR-1
    • Myers, C. R., and Myers, J. M. (2003). Cell surface exposure of the outer membrane cytochromes of Shewanella oneidensis MR-1. Lett Appl Microbiol 37: 254-258.
    • (2003) Lett Appl Microbiol , vol.37 , pp. 254-258
    • Myers, C.R.1    Myers, J.M.2
  • 89
    • 0024219883 scopus 로고
    • Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor
    • Myers, C. R., and Nealson, K. H. (1988). Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor. Science 24Q: 1319-1321.
    • (1988) Science , vol.24Q , pp. 1319-1321
    • Myers, C.R.1    Nealson, K.H.2
  • 90
    • 0025018122 scopus 로고
    • Respiration-linked proton translocation coupled to anaerobic reduction of manganese(IV) and iron(III) in Shewanella putrefaciens MR-1
    • Myers, C. R., and Nealson, K. H. (1990). Respiration-linked proton translocation coupled to anaerobic reduction of manganese(IV) and iron(III) in Shewanella putrefaciens MR-1. J Bacteriol 172: 6232-6238.
    • (1990) J Bacteriol , vol.172 , pp. 6232-6238
    • Myers, C.R.1    Nealson, K.H.2
  • 91
    • 0033989646 scopus 로고    scopus 로고
    • Role of the tetraheme cytochrome CymA in anaerobic electron transport in cells of Shewanella putrefaciens MR-1 with normal levels of menaquinone
    • Myers, J. M., and Myers, C. R. (2000). Role of the tetraheme cytochrome CymA in anaerobic electron transport in cells of Shewanella putrefaciens MR-1 with normal levels of menaquinone. J Bacteriol 1S2: 67-75.
    • (2000) J Bacteriol 1S2 , pp. 67-75
    • Myers, J.M.1    Myers, C.R.2
  • 92
    • 0036419051 scopus 로고    scopus 로고
    • Breathing metals as a way of life: Geobiology in action
    • Nealson, K. H., Belz, A., and McKee, B. (2002). Breathing metals as a way of life: Geobiology in action. Antonie Van Leeuwenhoek 81: 215-222.
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 215-222
    • Nealson, K.H.1    Belz, A.2    McKee, B.3
  • 93
    • 0028132223 scopus 로고
    • Iron and manganese in anaerobic respiration: Environmental significance, physiology, and regulation
    • Nealson, K. H., and Saffarini, D. (1994). Iron and manganese in anaerobic respiration: Environmental significance, physiology, and regulation. Annu Rev Microbiol 48: 311-343.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 311-343
    • Nealson, K.H.1    Saffarini, D.2
  • 94
    • 66249098568 scopus 로고    scopus 로고
    • Anode biofilm transcriptomics reveals outer surface components essential for high density current production in Geobacter sulfurreducens fuel cells
    • Nevin, K. P., Kim, B. C., Glaven, R. H., Johnson, J. P., Woodard, T. L., Methe, B. A. et al. (2009). Anode biofilm transcriptomics reveals outer surface components essential for high density current production in Geobacter sulfurreducens fuel cells. PLoS One 4: e5628.
    • (2009) Plos One , vol.e5628 , pp. 4
    • Nevin, K.P.1    Kim, B.C.2    Glaven, R.H.3    Johnson, J.P.4    Woodard, T.L.5    Methe, B.A.6
  • 95
    • 84877334667 scopus 로고    scopus 로고
    • Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones
    • Okamoto, A., Hashimoto, K., Nealson, K. H., and Nakamura, R. (2013). Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones. Proc Natl Acad Sci U S A llO: 7856-7861.
    • (2013) Proc Natl Acad Sci U S a Llo , pp. 7856-7861
    • Okamoto, A.1    Hashimoto, K.2    Nealson, K.H.3    Nakamura, R.4
  • 96
    • 84904322163 scopus 로고    scopus 로고
    • Cell-secreted flavins bound to membrane cytochromes dictate electron transfer reactions to surfaces with diverse charge and pH
    • Okamoto, A., Kalathil, S., Deng, X., Hashimoto, K., Nakamura, R., and Nealson, K. H. (2014). Cell-secreted flavins bound to membrane cytochromes dictate electron transfer reactions to surfaces with diverse charge and pH. Sci Rep 4: 5628.
    • (2014) Sci Rep , vol.4 , pp. 5628
    • Okamoto, A.1    Kalathil, S.2    Deng, X.3    Hashimoto, K.4    Nakamura, R.5    Nealson, K.H.6
  • 97
    • 2442638056 scopus 로고    scopus 로고
    • Vanadium respiration by Geobacter metallireducens: Novel strategy for in situ removal of vanadium from groundwater
    • Ortiz-Bernad, I., Anderson, R. T., Vrionis, H. A., and Lovley, D. R. (2004). Vanadium respiration by Geobacter metallireducens: Novel strategy for in situ removal of vanadium from groundwater. Appl Environ Microbiol 7O: 3091-3095.
    • (2004) Appl Environ Microbiol , vol.7O , pp. 3091-3095
    • Ortiz-Bernad, I.1    Anderson, R.T.2    Vrionis, H.A.3    Lovley, D.R.4
  • 99
    • 33751207759 scopus 로고    scopus 로고
    • Thermodynamic characterization of triheme cytochrome PpcA from Geobacter sulfurreducens: Evidence for a role played in e-/H+ energy transduction
    • Pessanha, M., Morgado, L., Louro, R. O., Londer, Y. Y., Pokkuluri, P. R., Schiffer, M., and Salgueiro, C. A. (2006). Thermodynamic characterization of triheme cytochrome PpcA from Geobacter sulfurreducens: Evidence for a role played in e-/H+ energy transduction. Biochemistry 4S: 13910-13917.
    • (2006) Biochemistry , vol.4S , pp. 13910-13917
    • Pessanha, M.1    Morgado, L.2    Louro, R.O.3    Londer, Y.Y.4    Pokkuluri, P.R.5    Schiffer, M.6    Salgueiro, C.A.7
  • 101
    • 84907227973 scopus 로고    scopus 로고
    • Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components
    • Pirbadian, S., Barchinger, S. E., Leung, K. M., Byun, H. S., Jangir, Y., Bouhenni, R. A. et al. (2014). Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components. Proc Natl Acad Sci U S A lll: 12883-12888.
    • (2014) Proc Natl Acad Sci U S a Lll , pp. 12883-12888
    • Pirbadian, S.1    Barchinger, S.E.2    Leung, K.M.3    Byun, H.S.4    Jangir, Y.5    Bouhenni, R.A.6
  • 102
    • 84866537380 scopus 로고    scopus 로고
    • Multistep hopping and extracellular charge transfer in microbial redox chains
    • Pirbadian, S., and El-Naggar, M. Y. (2012). Multistep hopping and extracellular charge transfer in microbial redox chains. Phys Chem Chem Phys l4: 13802-13808.
    • (2012) Phys Chem Chem Phys , vol.l4 , pp. 13802-13808
    • Pirbadian, S.1    El-Naggar, M.Y.2
  • 103
    • 0041344634 scopus 로고    scopus 로고
    • Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: Expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates
    • Pitts, K. E., Dobbin, P. S., Reyes-Ramirez, F., Thomson, A. J., Richardson, D. J., and Seward, H. E. (2003). Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: Expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates. J Biol Chem 278: 27758-27765.
    • (2003) J Biol Chem , vol.278 , pp. 27758-27765
    • Pitts, K.E.1    Dobbin, P.S.2    Reyes-Ramirez, F.3    Thomson, A.J.4    Richardson, D.J.5    Seward, H.E.6
  • 104
    • 0942290633 scopus 로고    scopus 로고
    • Family of cytochrome c7-type proteins from Geobacter sulfurreducens: Structure of one cytochrome c7 at 1.45 A resolution
    • Pokkuluri, P. R., Londer, Y. Y., Duke, N. E., Long, W. C., and Schiffer, M. (2004). Family of cytochrome c7-type proteins from Geobacter sulfurreducens: Structure of one cytochrome c7 at 1.45 A resolution. Biochemistry 43: 849-859.
    • (2004) Biochemistry , vol.43 , pp. 849-859
    • Pokkuluri, P.R.1    Londer, Y.Y.2    Duke, N.E.3    Long, W.C.4    Schiffer, M.5
  • 105
    • 79751531838 scopus 로고    scopus 로고
    • Biochemical characterization of purified OmcS, a c-type cytochrome required for insoluble Fe(III) reduction in Geobacter sulfurreducens
    • Qian, X., Mester, T., Morgado, L., Arakawa, T., Sharma, M. L., Inoue, K. et al. (2011). Biochemical characterization of purified OmcS, a c-type cytochrome required for insoluble Fe(III) reduction in Geobacter sulfurreducens. Biochim Biophys Acta l8O7: 404-412.
    • (2011) Biochim Biophys Acta L8o7 , pp. 404-412
    • Qian, X.1    Mester, T.2    Morgado, L.3    Arakawa, T.4    Sharma, M.L.5    Inoue, K.6
  • 106
    • 35748955474 scopus 로고    scopus 로고
    • Evidence that OmcB and OmpB of Geobacter sulfurreducens are outer membrane surface proteins
    • Qian, X., Reguera, G., Mester, T., and Lovley, D. R. (2007). Evidence that OmcB and OmpB of Geobacter sulfurreducens are outer membrane surface proteins. FEMS Microbiol Lett 277: 21-27.
    • (2007) FEMS Microbiol Lett , vol.277 , pp. 21-27
    • Qian, X.1    Reguera, G.2    Mester, T.3    Lovley, D.R.4
  • 107
    • 73349135628 scopus 로고    scopus 로고
    • Role of outer-membrane cytochromes MtrC and OmcA in the biomineralization of ferrihydrite by Shewanella oneidensis MR-1
    • Reardon, C. L., Dohnalkova, A. C., Nachimuthu, P., Kennedy, D. W., Saffarini, D. A., Arey, B. W. et al. (2010). Role of outer-membrane cytochromes MtrC and OmcA in the biomineralization of ferrihydrite by Shewanella oneidensis MR-1. Geobiology 8: 56-68.
    • (2010) Geobiology , vol.8 , pp. 56-68
    • Reardon, C.L.1    Dohnalkova, A.C.2    Nachimuthu, P.3    Kennedy, D.W.4    Saffarini, D.A.5    Arey, B.W.6
  • 108
    • 84885601452 scopus 로고    scopus 로고
    • Structure of the type IV a major pilin from the electrically conductive bacterial nanowires of Geobacter sulfurreducens
    • Reardon, P. N., and Mueller, K. T. (2013). Structure of the type IV a major pilin from the electrically conductive bacterial nanowires of Geobacter sulfurreducens. J Biol Chem 288: 29260-29266.
    • (2013) J Biol Chem , vol.288 , pp. 29260-29266
    • Reardon, P.N.1    Mueller, K.T.2
  • 111
    • 0034153610 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. (2000). Bacterial respiration: A flexible process for a changing environment. Microbiology l46 (Pt 3): 551-571.
    • (2000) Microbiology , vol.l46 , pp. 551-571
    • Richardson, D.J.1
  • 112
    • 84877352937 scopus 로고    scopus 로고
    • Controlling electron transfer at the microbe-mineral interface
    • Richardson, D. J., Butt, J. N., and Clarke, T. A. (2013). Controlling electron transfer at the microbe-mineral interface. Proc Natl Acad Sci U S A 110: 7537-7538.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7537-7538
    • Richardson, D.J.1    Butt, J.N.2    Clarke, T.A.3
  • 114
    • 84857082945 scopus 로고    scopus 로고
    • Dissimilatory reduction of extracellular electron acceptors in anaerobic respiration
    • Richter, K., Schicklberger, M., and Gescher, J. (2012). Dissimilatory reduction of extracellular electron acceptors in anaerobic respiration. Appl Environ Microbiol 78: 913-921.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 913-921
    • Richter, K.1    Schicklberger, M.2    Gescher, J.3
  • 116
    • 68549125315 scopus 로고    scopus 로고
    • Kinetic characterization of OmcA and MtrC, terminal reductases involved in respiratory electron transfer for dissimilatory iron reduction in Shewanella oneidensis MR-1
    • Ross, D. E., Brantley, S. L., and Tien, M. (2009). Kinetic characterization of OmcA and MtrC, terminal reductases involved in respiratory electron transfer for dissimilatory iron reduction in Shewanella oneidensis MR-1. Appl Environ Microbiol 75: 5218-5226.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5218-5226
    • Ross, D.E.1    Brantley, S.L.2    Tien, M.3
  • 117
    • 79551652545 scopus 로고    scopus 로고
    • Towards electrosynthesis in Shewanella: Energetics of reversing the mtr pathway for reductive metabolism
    • Ross, D. E., Flynn, J. M., Baron, D. B., Gralnick, J. A., and Bond, D. R. (2011). Towards electrosynthesis in Shewanella: Energetics of reversing the mtr pathway for reductive metabolism. PLoS One 6: e16649.
    • (2011) Plos One , vol.e16649 , pp. 6
    • Ross, D.E.1    Flynn, J.M.2    Baron, D.B.3    Gralnick, J.A.4    Bond, D.R.5
  • 120
    • 73249114332 scopus 로고    scopus 로고
    • Periplasmic electron transfer via the c-type cytochromes MtrA and FccA of Shewanella oneidensis MR-1
    • Schuetz, B., Schicklberger, M., Kuermann, J., Spormann, A. M., and Gescher, J. (2009). Periplasmic electron transfer via the c-type cytochromes MtrA and FccA of Shewanella oneidensis MR-1. Appl Environ Microbiol 75: 7789-7796.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 7789-7796
    • Schuetz, B.1    Schicklberger, M.2    Kuermann, J.3    Spormann, A.M.4    Gescher, J.5
  • 121
    • 0042572520 scopus 로고    scopus 로고
    • The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis
    • Schwalb, C., Chapman, S. K., and Reid, G. A. (2003). The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis. Biochemistry 42: 9491-9497.
    • (2003) Biochemistry , vol.42 , pp. 9491-9497
    • Schwalb, C.1    Chapman, S.K.2    Reid, G.A.3
  • 122
    • 79961093488 scopus 로고    scopus 로고
    • Identification and characterization of UndAHRCR-6, an outer membrane endecaheme c-type cytochrome of Shewanella sp. strain HRCR-6
    • Shi, L., Belchik, S. M., Wang, Z., Kennedy, D. W., Dohnalkova, A. C., Marshall, M. J. et al. (2011). Identification and characterization of UndAHRCR-6, an outer membrane endecaheme c-type cytochrome of Shewanella sp. strain HRCR-6. Appl Environ Microbiol 77: 5521-5523.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 5521-5523
    • Shi, L.1    Belchik, S.M.2    Wang, Z.3    Kennedy, D.W.4    Dohnalkova, A.C.5    Marshall, M.J.6
  • 123
    • 33745449038 scopus 로고    scopus 로고
    • Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1
    • Shi, L., Chen, B., Wang, Z., Elias, D. A., Mayer, M. U., Gorby, Y. A. et al. (2006). Isolation of a high-affinity functional protein complex between OmcA and MtrC: two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1. J Bacteriol 188: 4705-4714.
    • (2006) J Bacteriol , vol.188 , pp. 4705-4714
    • Shi, L.1    Chen, B.2    Wang, Z.3    Elias, D.A.4    Mayer, M.U.5    Gorby, Y.A.6
  • 124
    • 47549086918 scopus 로고    scopus 로고
    • Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochromes MtrC and OmcA
    • Shi, L., Deng, S., Marshall, M. J., Wang, Z., Kennedy, D. W., Dohnalkova, A. C. et al. (2008). Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochromes MtrC and OmcA. J Bacteriol 190: 5512-5516.
    • (2008) J Bacteriol , vol.190 , pp. 5512-5516
    • Shi, L.1    Deng, S.2    Marshall, M.J.3    Wang, Z.4    Kennedy, D.W.5    Dohnalkova, A.C.6
  • 128
    • 84870178309 scopus 로고    scopus 로고
    • Mtr extracellular electron-transfer pathways in Fe(III)-reducing or Fe(II)-oxidizing bacteria: A genomic perspective
    • (b)
    • Shi, L., Rosso, K. M., Zachara, J. M., and Fredrickson, J. K. (2012b). Mtr extracellular electron-transfer pathways in Fe(III)-reducing or Fe(II)-oxidizing bacteria: A genomic perspective. Biochem Soc Trans 40: 1261-1267.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1261-1267
    • Shi, L.1    Rosso, K.M.2    Zachara, J.M.3    Fredrickson, J.K.4
  • 129
    • 34250639301 scopus 로고    scopus 로고
    • Respiration of metal (hydr)oxides by Shewanella and Geobacter: A key role for multihaem c-type cytochromes
    • Shi, L., Squier, T. C., Zachara, J. M., and Fredrickson, J. K. (2007). Respiration of metal (hydr)oxides by Shewanella and Geobacter: A key role for multihaem c-type cytochromes. Mol Microbiol 65: 12-20.
    • (2007) Mol Microbiol , vol.65 , pp. 12-20
    • Shi, L.1    Squier, T.C.2    Zachara, J.M.3    Fredrickson, J.K.4
  • 130
    • 84883505570 scopus 로고    scopus 로고
    • Reductive dissolution of goethite and hematite by reduced flavins. Geochim. Cosmochim
    • Shi, Z., Zachara, J., Wang, Z., Shi, L., and Fredrickson, J. (2013). Reductive dissolution of goethite and hematite by reduced flavins. Geochim. Cosmochim. Acta 121: 139-154.
    • (2013) Acta , vol.121 , pp. 139-154
    • Shi, Z.1    Zachara, J.2    Wang, Z.3    Shi, L.4    Fredrickson, J.5
  • 131
    • 84868569888 scopus 로고    scopus 로고
    • Redox reactions of reduced flavin mononucleotide (FMN), riboflavin (RBF), and anthra-quinone-2,6-disulfonate (AQDS) with ferrihydrite and lepido crocite
    • (c)
    • Shi, Z., Zachara, J. M., Shi, L., Wang, Z., Moore, D. A., Kennedy, D. W., and Fredrickson, J. K. (2012c). Redox reactions of reduced flavin mononucleotide (FMN), riboflavin (RBF), and anthra-quinone-2,6-disulfonate (AQDS) with ferrihydrite and lepido crocite. Environ Sci Technol 46: 11644-11652.
    • (2012) Environ Sci Technol , vol.46 , pp. 11644-11652
    • Shi, Z.1    Zachara, J.M.2    Shi, L.3    Wang, Z.4    Moore, D.A.5    Kennedy, D.W.6    Fredrickson, J.K.7
  • 132
    • 78650774942 scopus 로고    scopus 로고
    • The octahaem SirA catalyses dissimila-tory sulfite reduction in Shewanella oneidensis MR-1
    • Shirodkar, S., Reed, S., Romine, M., and Saffarini, D. (2011). The octahaem SirA catalyses dissimila-tory sulfite reduction in Shewanella oneidensis MR-1. Environ Microbiol 13: 108-115.
    • (2011) Environ Microbiol , vol.13 , pp. 108-115
    • Shirodkar, S.1    Reed, S.2    Romine, M.3    Saffarini, D.4
  • 133
  • 134
    • 84893660109 scopus 로고    scopus 로고
    • Dissimilatory nitrate reduction by Aspergillus terreus isolated from the seasonal oxygen minimum zone in the Arabian Sea
    • Stief, P., Fuchs-Ocklenburg, S., Kamp, A., Manohar, C. S., Houbraken, J., Boekhout, T. et al. (2014). Dissimilatory nitrate reduction by Aspergillus terreus isolated from the seasonal oxygen minimum zone in the Arabian Sea. BMC Microbiol 14: 35.
    • (2014) BMC Microbiol , vol.14 , pp. 35
    • Stief, P.1    Fuchs-Ocklenburg, S.2    Kamp, A.3    Manohar, C.S.4    Houbraken, J.5    Boekhout, T.6
  • 135
    • 0032844160 scopus 로고    scopus 로고
    • Bacterial respiration of arsenic and selenium
    • Stolz, J. F., and Oremland, R. S. (1999). Bacterial respiration of arsenic and selenium. FEMS Microbiol Rev 23: 615-627.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 615-627
    • Stolz, J.F.1    Oremland, R.S.2
  • 137
    • 33847345976 scopus 로고    scopus 로고
    • Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes
    • Tang, X., Yi, W., Munske, G. R., Adhikari, D. P., Zakharova, N. L., and Bruce, J. E. (2007). Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes. J Proteome Res 6: 724-734.
    • (2007) J Proteome Res , vol.6 , pp. 724-734
    • Tang, X.1    Yi, W.2    Munske, G.R.3    Adhikari, D.P.4    Zakharova, N.L.5    Bruce, J.E.6
  • 140
    • 38949214833 scopus 로고    scopus 로고
    • Secretion of flavins by Shewanella species and their role in extracellular electron transfer
    • von Canstein, H., Ogawa, J., Shimizu, S., and Lloyd, J. R. (2008). Secretion of flavins by Shewanella species and their role in extracellular electron transfer. Appl Environ Microbiol 74: 615-623.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 615-623
    • von Canstein, H.1    Ogawa, J.2    Shimizu, S.3    Lloyd, J.R.4
  • 141
    • 84861217829 scopus 로고    scopus 로고
    • Genomic determinants of organohalide-respiration in Geobacter lovleyi, an unusual member of the Geobacteraceae
    • Wagner, D. D., Hug, L. A., Hatt, J. K., Spitzmiller, M. R., Padilla-Crespo, E., Ritalahti, K. M. et al. (2012). Genomic determinants of organohalide-respiration in Geobacter lovleyi, an unusual member of the Geobacteraceae. BMC Genomics 13: 200.
    • (2012) BMC Genomics , vol.13 , pp. 200
    • Wagner, D.D.1    Hug, L.A.2    Hatt, J.K.3    Spitzmiller, M.R.4    Padilla-Crespo, E.5    Ritalahti, K.M.6
  • 142
    • 84872721843 scopus 로고    scopus 로고
    • Single-cell imaging and spectroscopic analyses of Cr(VI) reduction on the surface of bacterial cells
    • Wang, Y., Sevinc, P. C., Belchik, S. M., Fredrickson, J., Shi, L., and Lu, H. P. (2013). Single-cell imaging and spectroscopic analyses of Cr(VI) reduction on the surface of bacterial cells. Langmuir 29: 950-956.
    • (2013) Langmuir , vol.29 , pp. 950-956
    • Wang, Y.1    Sevinc, P.C.2    Belchik, S.M.3    Fredrickson, J.4    Shi, L.5    Lu, H.P.6
  • 143
    • 84891829590 scopus 로고    scopus 로고
    • Identification of a molecular signature unique to metal-reducing Gammaproteobacteria
    • Wee, S. K., Burns, J. L., and DiChristina, T. J. (2014). Identification of a molecular signature unique to metal-reducing Gammaproteobacteria. FEMS Microbiol Lett 350: 90-99.
    • (2014) FEMS Microbiol Lett , vol.350 , pp. 90-99
    • Wee, S.K.1    Burns, J.L.2    Dichristina, T.J.3
  • 144
    • 84870153426 scopus 로고    scopus 로고
    • Development of a proteoliposome model to probe transmembrane electron-transfer reactions
    • White, G. F., Shi, Z., Shi, L., Dohnalkova, A. C., Fredrickson, J. K., Zachara, J. M. et al. (2012). Development of a proteoliposome model to probe transmembrane electron-transfer reactions. Biochem Soc Trans 40: 1257-1260.
    • (2012) Biochem Soc Trans , vol.40 , pp. 1257-1260
    • White, G.F.1    Shi, Z.2    Shi, L.3    Dohnalkova, A.C.4    Fredrickson, J.K.5    Zachara, J.M.6
  • 145
    • 84876250469 scopus 로고    scopus 로고
    • Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals
    • White, G. F., Shi, Z., Shi, L., Wang, Z., Dohnalkova, A. C., Marshall, M. J. et al. (2013). Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals. Proc Natl Acad Sci U S A 110: 6346-6351.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 6346-6351
    • White, G.F.1    Shi, Z.2    Shi, L.3    Wang, Z.4    Dohnalkova, A.C.5    Marshall, M.J.6
  • 146
    • 83155163702 scopus 로고    scopus 로고
    • Evidence for direct electron transfer by a gram-positive bacterium isolated from a microbial fuel cell
    • Wrighton, K. C., Thrash, J. C., Melnyk, R. A., Bigi, J. P., Byrne-Bailey, K. G., Remis, J. P. et al. (2011). Evidence for direct electron transfer by a gram-positive bacterium isolated from a microbial fuel cell. Appl Environ Microbiol 77: 7633-7639.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 7633-7639
    • Wrighton, K.C.1    Thrash, J.C.2    Melnyk, R.A.3    Bigi, J.P.4    Byrne-Bailey, K.G.5    Remis, J.P.6
  • 147
    • 33750430639 scopus 로고    scopus 로고
    • High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA
    • Xiong, Y., Shi, L., Chen, B., Mayer, M. U., Lower, B. H., Londer, Y. et al. (2006). High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA. J Am Chem Soc 128: 13978-13979.
    • (2006) J am Chem Soc , vol.128 , pp. 13978-13979
    • Xiong, Y.1    Shi, L.2    Chen, B.3    Mayer, M.U.4    Lower, B.H.5    Londer, Y.6
  • 148
    • 63049119068 scopus 로고    scopus 로고
    • Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry
    • Zhang, H., Tang, X., Munske, G. R., Tolic, N., Anderson, G. A., and Bruce, J. E. (2009). Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol Cell Proteomic 8: 409-420.
    • (2009) Mol Cell Proteomic , vol.8 , pp. 409-420
    • Zhang, H.1    Tang, X.2    Munske, G.R.3    Tolic, N.4    Anderson, G.A.5    Bruce, J.E.6
  • 149
    • 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
    • Zhang, H., Tang, X., Munske, G. R., Zakharova, N., Yang, L., Zheng, C. et al. (2008). 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.
    • (2008) J Proteome Res , vol.7 , pp. 1712-1720
    • Zhang, H.1    Tang, X.2    Munske, G.R.3    Zakharova, N.4    Yang, L.5    Zheng, C.6


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