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Volumn 72, Issue 4, 2006, Pages 2925-2935

Reduction of soluble and insoluble iron forms by membrane fractions of Shewanella oneidensis grown under aerobic and anaerobic conditions

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELL CULTURE; CHELATION; ELECTROPHORESIS; GROWTH KINETICS; PROTEINS;

EID: 33646082512     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.4.2925-2935.2006     Document Type: Article
Times cited : (59)

References (72)
  • 2
    • 0020696739 scopus 로고
    • Isolation and characterization of the outer and cytoplasmic membranes of Pseudomonas cepacia
    • Anwar, H., M. R. W. Brown, R. M. Cozens, and P. A. Lambert. 1983. Isolation and characterization of the outer and cytoplasmic membranes of Pseudomonas cepacia. J. Gen. Microbiol. 129:499-507.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 499-507
    • Anwar, H.1    Brown, M.R.W.2    Cozens, R.M.3    Lambert, P.A.4
  • 3
    • 0022518468 scopus 로고
    • Inhibitor studies of dissimilative Fe(III) reduction by Pseudomonas sp. strain 200 (Pseudomonas ferrireductans)
    • Arnold, R. G., T. J. Dichristina, and M. R. Hoffmann. 1986. Inhibitor studies of dissimilative Fe(III) reduction by Pseudomonas sp. strain 200 (Pseudomonas ferrireductans). Appl. Environ. Microbiol. 52:281-289.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 281-289
    • Arnold, R.G.1    Dichristina, T.J.2    Hoffmann, M.R.3
  • 4
    • 0024095388 scopus 로고
    • Reductive dissolution of Fe(III) oxides by Pseudomonas sp. 200
    • Arnold, R. G., T. J. Dichristina, and M. R. Hoffmann. 1986. Reductive dissolution of Fe(III) oxides by Pseudomonas sp. 200. Biotechnol. Bioeng. 32:1081-1096.
    • (1986) Biotechnol. Bioeng. , vol.32 , pp. 1081-1096
    • Arnold, R.G.1    Dichristina, T.J.2    Hoffmann, M.R.3
  • 5
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli
    • Arslan, E., H. Schulz, R. Zufferey, P. Kanzler, and L. Thony-Meyer. 1998. Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb(3) oxidase in Escherichia coli. Biochem. Biophys. Res. Commun. 251:744-747.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Kanzler, P.4    Thony-Meyer, L.5
  • 6
    • 0031754775 scopus 로고    scopus 로고
    • Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction
    • Beliaev, A. S., and D. A. Saffarini. 1998. Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction. J. Bacteriol. 180:6292-6297.
    • (1998) J. Bacteriol. , vol.180 , pp. 6292-6297
    • Beliaev, A.S.1    Saffarini, D.A.2
  • 7
    • 0035131413 scopus 로고    scopus 로고
    • MtrC, an outer membrane decahaem c-cytochrome required for metal reduction in Shewanella putrefaciens MR-1
    • Beliaev, A. S., D. A. Saffarini, J. L. McLaughlin, and D. Hunnicutt. 2001. MtrC, an outer membrane decahaem c-cytochrome required for metal reduction in Shewanella putrefaciens MR-1. Mol. Microbiol. 39:722-730.
    • (2001) Mol. Microbiol. , vol.39 , pp. 722-730
    • Beliaev, A.S.1    Saffarini, D.A.2    McLaughlin, J.L.3    Hunnicutt, D.4
  • 9
    • 0033880921 scopus 로고    scopus 로고
    • Fe(III) reduction activity and cytochrome content of Shewanella putrefaciens grown on ten compounds as sole terminal electron acceptor
    • Blakeney, M. D, T. Moulaei, and T. J. DiChristina. 2000. Fe(III) reduction activity and cytochrome content of Shewanella putrefaciens grown on ten compounds as sole terminal electron acceptor. Microbiol. Res. 155:87-94.
    • (2000) Microbiol. Res. , vol.155 , pp. 87-94
    • Blakeney, M.D.1    Moulaei, T.2    Dichristina, T.J.3
  • 10
    • 0037457677 scopus 로고    scopus 로고
    • The roles of natural organic matter in chemical and microbial reduction of ferric iron
    • Chen, J., B. H. Gu, R. A. Royer, and W. D. Burgos. 2003. The roles of natural organic matter in chemical and microbial reduction of ferric iron. Sci. Total Environ. 307:167-178.
    • (2003) Sci. Total Environ. , vol.307 , pp. 167-178
    • Chen, J.1    Gu, B.H.2    Royer, R.A.3    Burgos, W.D.4
  • 11
    • 0028938072 scopus 로고
    • The influence of chelating-agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens
    • Dobbin, P. S., A. K. Powell, A. G. McEwan, and D. J. Richardson. 1995. The influence of chelating-agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens. Biometals 8:163-173.
    • (1995) Biometals , vol.8 , pp. 163-173
    • Dobbin, P.S.1    Powell, A.K.2    McEwan, A.G.3    Richardson, D.J.4
  • 12
    • 0032468301 scopus 로고    scopus 로고
    • Biogenic iron mineralization accompanying the dissimilatory reduction of hydrous ferric oxide by a groundwater bacterium
    • Fredrickson, J. K., J. M. Zachara, D. W. Kennedy, H. L. Dong, T. C. Onstott, N. W. Hinman, and S. M. Li. 1998. Biogenic iron mineralization accompanying the dissimilatory reduction of hydrous ferric oxide by a groundwater bacterium. Geochim. Cosmochim. Acta 62:3239-3257.
    • (1998) Geochim. Cosmochim. Acta , vol.62 , pp. 3239-3257
    • Fredrickson, J.K.1    Zachara, J.M.2    Kennedy, D.W.3    Dong, H.L.4    Onstott, T.C.5    Hinman, N.W.6    Li, S.M.7
  • 14
    • 0038555376 scopus 로고    scopus 로고
    • Analysis of the Shewanella oneidensis proteome by two-dimensional gel electrophoresis under 3 nondenaturing conditions
    • Giometti, C. S., T. Khare, S. L. Tollaksen, A. Tsapin, W. H. Zhu, J. R. Yates, and K. H. Nealson. 2003. Analysis of the Shewanella oneidensis proteome by two-dimensional gel electrophoresis under 3 nondenaturing conditions. Proteomics 3:777-785.
    • (2003) Proteomics , vol.3 , pp. 777-785
    • Giometti, C.S.1    Khare, T.2    Tollaksen, S.L.3    Tsapin, A.4    Zhu, W.H.5    Yates, J.R.6    Nealson, K.H.7
  • 16
    • 0036469140 scopus 로고    scopus 로고
    • Effects of Fe(III) chemical speciation on dissimilatory Fe(III) reduction by Shewanella putrefaciens
    • Haas, J. R., and T. J. Dichristina. 2002. Effects of Fe(III) chemical speciation on dissimilatory Fe(III) reduction by Shewanella putrefaciens. Environ. Sci. Technol. 36:373-380.
    • (2002) Environ. Sci. Technol. , vol.36 , pp. 373-380
    • Haas, J.R.1    Dichristina, T.J.2
  • 17
    • 0041709347 scopus 로고    scopus 로고
    • Kinetics and mechanisms for reactions of Fe(II) with iron(III) oxides
    • Jeon, B. H., B. A. Dempsey, and W. D. Burgos. 2003. Kinetics and mechanisms for reactions of Fe(II) with iron(III) oxides. Environ. Sci. Technol. 37:3309-3315.
    • (2003) Environ. Sci. Technol. , vol.37 , pp. 3309-3315
    • Jeon, B.H.1    Dempsey, B.A.2    Burgos, W.D.3
  • 18
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jonnakka, M., S. Tornroth, B. Byrne, and S. Iwata. 2002. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jonnakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 19
    • 0020488878 scopus 로고
    • The oxidation-reduction kinetics of the reaction of cytochrome c, with non-physiological redox agents
    • Konig, B. W., E. C. I. Veennan, and B. F. Van Gelder. 1982. The oxidation-reduction kinetics of the reaction of cytochrome c, with non-physiological redox agents. Biochim. Biophys. Acta 681:54-61.
    • (1982) Biochim. Biophys. Acta , vol.681 , pp. 54-61
    • Konig, B.W.1    Veennan, E.C.I.2    Van Gelder, B.F.3
  • 20
    • 0028991585 scopus 로고
    • Dissolution and reduction of magnetite by bacteria
    • Kostka, J. E., and K. H. Nealson. 1995. Dissolution and reduction of magnetite by bacteria. Environ. Sci. Technol. 29:2535-2540.
    • (1995) Environ. Sci. Technol. , vol.29 , pp. 2535-2540
    • Kostka, J.E.1    Nealson, K.H.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 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., M. E. Hernandez, A. Kappler, R. E. Mielke, J. A. Gralnick, and D. K. Newman. 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
  • 24
    • 0035298627 scopus 로고    scopus 로고
    • Microbial reduction of Fe(III) and sorption/precipitation of Fe(II) on Shewanella putrefaciens strain CN32
    • Liu, C., J. M. Zachara, Y. A. Gorby, J. E. Szecsody, and C. F. Brown. 2001. Microbial reduction of Fe(III) and sorption/precipitation of Fe(II) on Shewanella putrefaciens strain CN32. Environ. Sci. Technol. 35:1385-1393.
    • (2001) Environ. Sci. Technol. , vol.35 , pp. 1385-1393
    • Liu, C.1    Zachara, J.M.2    Gorby, Y.A.3    Szecsody, J.E.4    Brown, C.F.5
  • 25
    • 0037146816 scopus 로고    scopus 로고
    • Reduction kinetics of Fe(III), Co(III), U(VI), Cr(VI), and Tc(VII) in cultures of dissimilatory metal-reducing bacteria
    • Liu, C. X., Y. A. Gorby, J. M. Zachara, J. K. Fredrickson, and C. F. Brown. 2002. Reduction kinetics of Fe(III), Co(III), U(VI), Cr(VI), and Tc(VII) in cultures of dissimilatory metal-reducing bacteria. Biotechnol. Bioeng. 80:637-649.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 637-649
    • Liu, C.X.1    Gorby, Y.A.2    Zachara, J.M.3    Fredrickson, J.K.4    Brown, C.F.5
  • 28
    • 0000209741 scopus 로고
    • Organic-matter mineralization with reduction of ferric iron in anaerobic sediments
    • Lovley, D. R., and E. J. P. Phillips. 1986. Organic-matter mineralization with reduction of ferric iron in anaerobic sediments. Appl. Environ. Microbiol. 51:683-689.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 683-689
    • Lovley, D.R.1    Phillips, E.J.P.2
  • 30
    • 0023906969 scopus 로고
    • Structure and mass analysis of 14S dynein obtained from Tetrahymena cilia
    • Marchese-Ragona, S. P., J. S. Wall, and K. A. Johnson. 1988. Structure and mass analysis of 14S dynein obtained from Tetrahymena cilia. J. Cell Biol. 106:127-132.
    • (1988) J. Cell Biol. , vol.106 , pp. 127-132
    • Marchese-Ragona, S.P.1    Wall, J.S.2    Johnson, K.A.3
  • 31
    • 0017831492 scopus 로고
    • Detection of hemeprotiens in SDS-polyacrylamide gels
    • Moore, R. W., A. F. Welton, and S. D. Aust. 1978. Detection of hemeprotiens in SDS-polyacrylamide gels. Methods Enzymol. 52:324-331.
    • (1978) Methods Enzymol. , vol.52 , pp. 324-331
    • Moore, R.W.1    Welton, A.F.2    Aust, S.D.3
  • 32
    • 0029992689 scopus 로고    scopus 로고
    • Growth of the facultative anaerobe Shewanella putrefaciens by elemental sulfur reduction
    • Moser, D. P., and K. H. Nealson. 1996. Growth of the facultative anaerobe Shewanella putrefaciens by elemental sulfur reduction. Appl. Environ. Microbiol. 62:2100-2105.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2100-2105
    • Moser, D.P.1    Nealson, K.H.2
  • 33
    • 0042378909 scopus 로고    scopus 로고
    • Cell surface exposure of the outer membrane cytochromes of Shewanella oneidensis MR-1
    • Myers, C. R., and J. M. Myers. 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
  • 34
    • 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 putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1997. Cloning and sequence of cymA a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1. J. Bacteriol. 179:1143-1152.
    • (1997) J. Bacteriol. , vol.179 , pp. 1143-1152
    • Myers, C.R.1    Myers, J.M.2
  • 35
    • 0028359079 scopus 로고
    • Ferric iron reduction-linked growth yields of Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1994. Ferric iron reduction-linked growth yields of Shewanella putrefaciens MR-1. J. Appl. Bacteriol. 76:253-258.
    • (1994) J. Appl. Bacteriol. , vol.76 , pp. 253-258
    • Myers, C.R.1    Myers, J.M.2
  • 36
    • 0027526231 scopus 로고
    • Ferric reductase is associated with the membranes of anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1993. Ferric reductase is associated with the membranes of anaerobically grown Shewanella putrefaciens MR-1. FEMS Microb. Lett. 108:15-22.
    • (1993) FEMS Microb. Lett. , vol.108 , pp. 15-22
    • Myers, C.R.1    Myers, J.M.2
  • 37
    • 0026440525 scopus 로고
    • Fumarate reductase is a soluble enzyme in anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1992. Fumarate reductase is a soluble enzyme in anaerobically grown Shewanella putrefaciens MR-1. FEMS Microb. Lett. 98:13-19.
    • (1992) FEMS Microb. Lett. , vol.98 , pp. 13-19
    • Myers, C.R.1    Myers, J.M.2
  • 38
    • 0026740398 scopus 로고
    • Localization of cytochromes to the outer-membrane of anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1992. Localization of cytochromes to the outer-membrane of anaerobically grown Shewanella putrefaciens MR-1. J. Bacteriol. 174:3429-3438.
    • (1992) J. Bacteriol. , vol.174 , pp. 3429-3438
    • Myers, C.R.1    Myers, J.M.2
  • 39
    • 0036841160 scopus 로고    scopus 로고
    • MtrB is required for proper incorporation of the cytochromes OmcA and OmcB into the outer membrane of Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 2002. MtrB is required for proper incorporation of the cytochromes OmcA and OmcB into the outer membrane of Shewanella putrefaciens MR-1. Appl. Environ. Microbiol. 68:5585-5594.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5585-5594
    • Myers, C.R.1    Myers, J.M.2
  • 40
    • 0030903069 scopus 로고    scopus 로고
    • Outer membrane cytochromes of Shewanella putrefaciens MR-1: Spectral analysis, and purification of the 83-kDa c-type cytochrome
    • Myers, C. R., and J. M. Myers. 1997. 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.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 307-318
    • Myers, C.R.1    Myers, J.M.2
  • 41
    • 0024219883 scopus 로고
    • Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor
    • Myers, C. R., and K. H. Nealson. 1988. Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor. Science 240:1319-1321.
    • (1988) Science , vol.240 , pp. 1319-1321
    • Myers, C.R.1    Nealson, K.H.2
  • 42
    • 0024231430 scopus 로고
    • Microbial reduction of manganese oxides: Interactions with iron and sulfur
    • Myers, C. R., and K. H. Nealson. 1988. Microbial reduction of manganese oxides: interactions with iron and sulfur. Geochim. Cosmochim. Acta 52:2727-2732.
    • (1988) Geochim. Cosmochim. Acta , vol.52 , pp. 2727-2732
    • Myers, C.R.1    Nealson, K.H.2
  • 43
    • 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 K. H. Nealson. 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
  • 44
    • 0035166832 scopus 로고    scopus 로고
    • Role for outer membrane cytochromes OmcA and OmcB of Shewanella putrefaciens MR-1 in reduction of manganese dioxide
    • Myers, J. M., and C. R. Myers. 2001. Role for outer membrane cytochromes OmcA and OmcB of Shewanella putrefaciens MR-1 in reduction of manganese dioxide. Appl. Environ. Microbiol. 67:260-269.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 260-269
    • Myers, J.M.1    Myers, C.R.2
  • 45
    • 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 C. R. Myers. 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. 182:67-75.
    • (2000) J. Bacteriol. , vol.182 , pp. 67-75
    • Myers, J.M.1    Myers, C.R.2
  • 46
    • 0036244691 scopus 로고    scopus 로고
    • Mechanisms for accessing insoluble Fe(III) oxide during dissimilatory Fe(III) reduction by Geothrix fermentans
    • Nevin, K. P., and D. R. Lovley. 2002. Mechanisms for accessing insoluble Fe(III) oxide during dissimilatory Fe(III) reduction by Geothrix fermentans. Appl. Environ. Microbiol. 68:2294-2299.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2294-2299
    • Nevin, K.P.1    Lovley, D.R.2
  • 47
    • 0036252368 scopus 로고    scopus 로고
    • Mechanisms for Fe(III) oxide reduction in sedimentary environments
    • Nevin, K. P., and D. R. Lovley. 2002. Mechanisms for Fe(III) oxide reduction in sedimentary environments. Geomicrobiol. J. 19:141-159.
    • (2002) Geomicrobiol. J. , vol.19 , pp. 141-159
    • Nevin, K.P.1    Lovley, D.R.2
  • 48
    • 0034604081 scopus 로고    scopus 로고
    • A role for excreted quinones in extracellular electron transfer
    • Newman, D. K., and R. Kolter. 2000. A role for excreted quinones in extracellular electron transfer. Nature 405:94-97.
    • (2000) Nature , vol.405 , pp. 94-97
    • Newman, D.K.1    Kolter, R.2
  • 49
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium: Isolation and characterization of cytoplasmic and outer membrane
    • Osborn, M. J., J. E. Gander, E. Parisi, and J. Carson. 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium: isolation and characterization of cytoplasmic and outer membrane. J. Biol. Chem. 247:3962-3972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 50
    • 0026752211 scopus 로고
    • Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: A tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria
    • Pealing, S. L, A. C. Black, F. D. C. Manson, F. B. Ward, S. K. Chapman, and G. A. Reid. 1992. Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria. Biochemistry 31:12132-12140.
    • (1992) Biochemistry , vol.31 , pp. 12132-12140
    • Pealing, S.L.1    Black, A.C.2    Manson, F.D.C.3    Ward, F.B.4    Chapman, S.K.5    Reid, G.A.6
  • 52
    • 0034015380 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 146:551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 53
    • 0032995763 scopus 로고    scopus 로고
    • Ferrous iron removal promotes microbial reduction of crystalline iron(III) oxides
    • Roden, E. E., and M. M. Urrutia. 1999. Ferrous iron removal promotes microbial reduction of crystalline iron(III) oxides. Environ. Sci. Technol. 33:1847-1853.
    • (1999) Environ. Sci. Technol. , vol.33 , pp. 1847-1853
    • Roden, E.E.1    Urrutia, M.M.2
  • 54
    • 0029935919 scopus 로고    scopus 로고
    • Microbial reduction of crystalline iron(III) oxides: Influence of oxide surface area and potential for cell growth
    • Roden, E. E., and J. M. Zachara. 1996. Microbial reduction of crystalline iron(III) oxides: influence of oxide surface area and potential for cell growth. Environ. Sci. Technol. 30:1618-1628.
    • (1996) Environ. Sci. Technol. , vol.30 , pp. 1618-1628
    • Roden, E.E.1    Zachara, J.M.2
  • 56
    • 0348046329 scopus 로고    scopus 로고
    • Inhibition of biological reductive dissolution of hematite by ferrous iron
    • Royer, R. A., B. A. Dempsey, B. H. Jeon, and W. D. Burgos. 2004. Inhibition of biological reductive dissolution of hematite by ferrous iron. Environ. Sci. Technol. 38:187-193.
    • (2004) Environ. Sci. Technol. , vol.38 , pp. 187-193
    • Royer, R.A.1    Dempsey, B.A.2    Jeon, B.H.3    Burgos, W.D.4
  • 57
    • 29444431620 scopus 로고    scopus 로고
    • In vitro enzymatic reduction kinetics of mineral oxides by membrane fractions from Shewanella oneidensis MR-1
    • Ruebush, S. S., G. A. Icopini, S. L. Brantley, and M. Tien. 2005. In vitro enzymatic reduction kinetics of mineral oxides by membrane fractions from Shewanella oneidensis MR-1. Geochim. Cosmochim. Acta 70:56-70.
    • (2005) Geochim. Cosmochim. Acta , vol.70 , pp. 56-70
    • Ruebush, S.S.1    Icopini, G.A.2    Brantley, S.L.3    Tien, M.4
  • 59
    • 0036670757 scopus 로고    scopus 로고
    • The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella
    • Schwalb, C., S. K. Chapman, and G. A. Reid. 2002. The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella. Biochem. Soc. Trans. 30:658-662.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 658-662
    • Schwalb, C.1    Chapman, S.K.2    Reid, G.A.3
  • 60
    • 0042572520 scopus 로고    scopus 로고
    • The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis
    • Schwalb, C., S. K. Chapman, and G. A. Reid. 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
  • 61
    • 0028364163 scopus 로고
    • A biochemical study of the intermediary carbon metabolism of Shewanella putrefaciens
    • Scott, J. H., and K. H. Nealson. 1994. A biochemical study of the intermediary carbon metabolism of Shewanella putrefaciens. J. Bacteriol. 176:3408-3411.
    • (1994) J. Bacteriol. , vol.176 , pp. 3408-3411
    • Scott, J.H.1    Nealson, K.H.2
  • 62
    • 0036186071 scopus 로고    scopus 로고
    • Protective role of tolC in efflux of the electron shuttle anthraquinone-2,6-disulfonate
    • Shyu, J. B. H., D. P. Lies, and D. K. Newman. 2002. Protective role of tolC in efflux of the electron shuttle anthraquinone-2,6-disulfonate. J. Bacteriol. 184:1806-1810.
    • (2002) J. Bacteriol. , vol.184 , pp. 1806-1810
    • Shyu, J.B.H.1    Lies, D.P.2    Newman, D.K.3
  • 63
    • 0024388691 scopus 로고
    • The inducible trimethylamine N-oxide reductase of Escherichia coli K-12: Its localization and inducers
    • Silvestro, A., J. Pommier, M. C. Pascal, and G. Giordano. 1989. The inducible trimethylamine N-oxide reductase of Escherichia coli K-12: its localization and inducers. Biochim. Biophys. Acta 999:208-216.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 208-216
    • Silvestro, A.1    Pommier, J.2    Pascal, M.C.3    Giordano, G.4
  • 65
    • 33847670407 scopus 로고
    • Ferrozine: A new spectrophotometric reagent for iron
    • Stookey, L. L. 1970. Ferrozine: a new spectrophotometric reagent for iron. Anal. Chem. 42:779-781.
    • (1970) Anal. Chem. , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 66
    • 0036156696 scopus 로고    scopus 로고
    • Transcriptional and proteomic analysis of a ferric uptake regulator (fur) mutant of Shewanella oneidensis: Possible involvement of fur in energy metabolism, transcriptional regulation, and oxidative stress
    • Thompson, D. K., A. S. Beliaev, C. S. Giometti, S. L. Tollaksen, T. Khare, D. P. Lies, K. H. Nealson, J. Lim, J. Yates, C. C. Brandt, J. M. Tiedje, and J. Z. Zhou. 2002. Transcriptional and proteomic analysis of a ferric uptake regulator (fur) mutant of Shewanella oneidensis: possible involvement of fur in energy metabolism, transcriptional regulation, and oxidative stress. Appl. Environ. Microbiol. 68:881-892.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 881-892
    • Thompson, D.K.1    Beliaev, A.S.2    Giometti, C.S.3    Tollaksen, S.L.4    Khare, T.5    Lies, D.P.6    Nealson, K.H.7    Lim, J.8    Yates, J.9    Brandt, C.C.10    Tiedje, J.M.11    Zhou, J.Z.12
  • 67
    • 0020484026 scopus 로고
    • The multiple effects of ethylenediaminetetraacetate in several model lipid peroxidation systems
    • Tien, M., L. A. Morehouse, J. R. Bucher, and S. D. Aust. 1982. The multiple effects of ethylenediaminetetraacetate in several model lipid peroxidation systems. Arch. Biochem. Biophys. 218:450-458.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 450-458
    • Tien, M.1    Morehouse, L.A.2    Bucher, J.R.3    Aust, S.D.4
  • 68
    • 0032462955 scopus 로고    scopus 로고
    • Microbial and surface chemistry controls on reduction of synthetic Fe(III) oxide minerals by the dissimilatory iron-reducing bacterium Shewanella alga
    • Urrutia, M. M., E. E. Roden, J. K. Fredrickson, and J. M. Zachara. 1998. Microbial and surface chemistry controls on reduction of synthetic Fe(III) oxide minerals by the dissimilatory iron-reducing bacterium Shewanella alga. Geomicrobiol. J. 15:269-291.
    • (1998) Geomicrobiol. J. , vol.15 , pp. 269-291
    • Urrutia, M.M.1    Roden, E.E.2    Fredrickson, J.K.3    Zachara, J.M.4
  • 69
    • 0032698221 scopus 로고    scopus 로고
    • Influence of aqueous and solid-phase Fe(II) complexants on microbial reduction of crystalline iron(III) oxides
    • Urrutia, M. M., E. E. Roden, and J. M. Zachara. 1999. Influence of aqueous and solid-phase Fe(II) complexants on microbial reduction of crystalline iron(III) oxides. Environ. Sci. Technol. 33:4022-4028.
    • (1999) Environ. Sci. Technol. , vol.33 , pp. 4022-4028
    • Urrutia, M.M.1    Roden, E.E.2    Zachara, J.M.3
  • 71
    • 0343485086 scopus 로고    scopus 로고
    • Isolation of U(VI) reduction-deficient mutants of Shewanella putrefaciens
    • Wade, R., and T. J. DiChristina. 2000. Isolation of U(VI) reduction-deficient mutants of Shewanella putrefaciens. FEMS Microb. Lett. 184:143-148.
    • (2000) FEMS Microb. Lett. , vol.184 , pp. 143-148
    • Wade, R.1    Dichristina, T.J.2


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