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Volumn 73, Issue 18, 2007, Pages 5797-5808

Characterization of protein-protein interactions involved in iron reduction by Shewanella oneidensis MR-1

Author keywords

[No Author keywords available]

Indexed keywords

SHEWANELLA ONEIDENSIS; SODIUM DODECYL SULFATE; ULTRACENTRIFUGATION;

EID: 34648827433     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00146-07     Document Type: Article
Times cited : (139)

References (63)
  • 1
    • 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
  • 2
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli
    • Arslan, E., H. Schulz, R. Zufferey, P. Kunzler, and L. Thony-Meyer. 1998. Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 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    Kunzler, P.4    Thony-Meyer, L.5
  • 4
    • 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
  • 5
    • 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
  • 6
    • 4243995515 scopus 로고
    • About some critics of the BET theory
    • Brunauer, S. 1987. About some critics of the BET theory. Langmuir 3:3-4.
    • (1987) Langmuir , vol.3 , pp. 3-4
    • Brunauer, S.1
  • 7
    • 34547829281 scopus 로고    scopus 로고
    • The crystal structure of the pentahaem c-type cytochrome NrfB and characterisation of its solution-state interaction with the pentahaem nitrite reductase NrfA
    • Clarke, T., J. Cole, D. Richardson, and A. Hemmings. 2007. The crystal structure of the pentahaem c-type cytochrome NrfB and characterisation of its solution-state interaction with the pentahaem nitrite reductase NrfA. Biochem. J. 406:19-30.
    • (2007) Biochem. J , vol.406 , pp. 19-30
    • Clarke, T.1    Cole, J.2    Richardson, D.3    Hemmings, A.4
  • 8
    • 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., C. M. Moore, and C. A. Haller. 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
  • 10
    • 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
  • 11
    • 0242488719 scopus 로고    scopus 로고
    • Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration
    • Gordon, E. H. J., A. D. Pike, A. E. Hill, P. M. Cuthbertson, S. K. Chapman, and G. A. Reid. 2000. Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration. Biochem. J. 349:153-158.
    • (2000) Biochem. J , vol.349 , pp. 153-158
    • Gordon, E.H.J.1    Pike, A.D.2    Hill, A.E.3    Cuthbertson, P.M.4    Chapman, S.K.5    Reid, G.A.6
  • 13
    • 0346294231 scopus 로고    scopus 로고
    • Reduction of elemental selenium to selenide: Experiments with anoxic sediments and bacteria that respire Se-oxyanions
    • Herbel, M. J., J. S. Blum, R. S. Oremland, and S. E. Borglin. 2003. Reduction of elemental selenium to selenide: experiments with anoxic sediments and bacteria that respire Se-oxyanions. Geomicrobiol. J. 20:587-602.
    • (2003) Geomicrobiol. J , vol.20 , pp. 587-602
    • Herbel, M.J.1    Blum, J.S.2    Oremland, R.S.3    Borglin, S.E.4
  • 14
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs, P. I., P. S. Myers, and K. Postle. 1998. Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers. J. Bacteriol. 180:6031-6038.
    • (1998) J. Bacteriol , vol.180 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 15
    • 0028802638 scopus 로고
    • Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3
    • Horan, T., J. Wen, T. Arakawa, N. L. Liu, D. Brankow, S. Hu, B. Ratzkin, and J. S. Philo. 1995. Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. 270:24604- 24608.
    • (1995) J. Biol. Chem , vol.270 , pp. 24604-24608
    • Horan, T.1    Wen, J.2    Arakawa, T.3    Liu, N.L.4    Brankow, D.5    Hu, S.6    Ratzkin, B.7    Philo, J.S.8
  • 16
    • 0042029411 scopus 로고    scopus 로고
    • A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm
    • Kaderbhai, M. A., D. J. Hopper, K. M. Akhtar, S. K. Abbas, and N. N. Kaderbhai. 2003. A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm. Appl. Environ. Microbiol. 69:4727-4731.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 4727-4731
    • Kaderbhai, M.A.1    Hopper, D.J.2    Akhtar, K.M.3    Abbas, S.K.4    Kaderbhai, N.N.5
  • 17
    • 0001351753 scopus 로고
    • Chemical and biological reduction of Mn(III)-pyrophosphate complexes - potential importance of dissolved Mn(III) as an environmental oxidant
    • Kostka, J. E., G. W. Luther, and K. H. Nealson. 1995. Chemical and biological reduction of Mn(III)-pyrophosphate complexes - potential importance of dissolved Mn(III) as an environmental oxidant. Geochim. Cosmochim. Acta 59:885-894.
    • (1995) Geochim. Cosmochim. Acta , vol.59 , pp. 885-894
    • Kostka, J.E.1    Luther, G.W.2    Nealson, K.H.3
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 33947269995 scopus 로고    scopus 로고
    • Time-resolved structural analysis of K- and Ba-exchange reactions with synthetic Na-birnessite using synchrotron X-ray diffraction
    • Lopano, C. L., P. J. Heaney, J. E. Post, J. Hanson, and S. Komarneni. 2007. Time-resolved structural analysis of K- and Ba-exchange reactions with synthetic Na-birnessite using synchrotron X-ray diffraction. Am. Miner. 92:380-387.
    • (2007) Am. Miner , vol.92 , pp. 380-387
    • Lopano, C.L.1    Heaney, P.J.2    Post, J.E.3    Hanson, J.4    Komarneni, S.5
  • 22
    • 0037516636 scopus 로고    scopus 로고
    • Dissimilatory metal reduction: From early life to bioremediation
    • 68
    • Lovley, D. R. 2002. Dissimilatory metal reduction: from early life to bioremediation. ASM News 68:231-237.
    • (2002) ASM News , pp. 231-237
    • Lovley, D.R.1
  • 23
    • 0024191542 scopus 로고
    • Novel mode of microbial energy metabolism: Organic carbon oxidation coupled to dissimilatory reduction of iron or manganese
    • Lovley, D. R., and E. J. P. Phillips. 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.P.2
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0034091960 scopus 로고    scopus 로고
    • Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., B. P. Carstens, W. E. Antholine, and J. M. Myers. 2000. Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR-1. J. Appl. Microbiol. 88:98-106.
    • (2000) J. Appl. Microbiol , vol.88 , pp. 98-106
    • Myers, C.R.1    Carstens, B.P.2    Antholine, W.E.3    Myers, J.M.4
  • 29
    • 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
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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. 68:5585-9554.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 5585-9554
    • Myers, C.R.1    Myers, J.M.2
  • 34
    • 0027438193 scopus 로고
    • Role of menaquinone in the reduction of fumarate, nitrate, iron(III) and manganese(IV) by Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1993. Role of menaquinone in the reduction of fumarate, nitrate, iron(III) and manganese(IV) by Shewanella putrefaciens MR-1. FEMS Microbiol. Lett. 114:215-222.
    • (1993) FEMS Microbiol. Lett , vol.114 , pp. 215-222
    • Myers, C.R.1    Myers, J.M.2
  • 35
    • 4644245648 scopus 로고    scopus 로고
    • Shewanella oneidensis MR-1 restores menaquinone synthesis to a menaquinone-negative mutant
    • Myers, C. R., and J. M. Myers. 2004. Shewanella oneidensis MR-1 restores menaquinone synthesis to a menaquinone-negative mutant. Appl. Environ. Microbiol. 70:5515-5525.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 5515-5525
    • Myers, C.R.1    Myers, J.M.2
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0036419051 scopus 로고    scopus 로고
    • Breathing metals as a way of life: Geobiology in action
    • Nealson, K. H., A. Belz, and B. McKee. 2002. Breathing metals as a way of life: geobiology in action. Antonie Leeuwenhoek 81:215-222.
    • (2002) Antonie Leeuwenhoek , vol.81 , pp. 215-222
    • Nealson, K.H.1    Belz, A.2    McKee, B.3
  • 40
    • 0030946056 scopus 로고    scopus 로고
    • Precipitation of arsenic trisulfide by Desulfotomaculum auripigmentum
    • Newman, D. K., T. J. Beveridge, and F. M. M. Morel. 1997. Precipitation of arsenic trisulfide by Desulfotomaculum auripigmentum. Appl. Environ. Microbiol. 63:2022-2028.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 2022-2028
    • Newman, D.K.1    Beveridge, T.J.2    Morel, F.M.M.3
  • 41
    • 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
  • 42
    • 37049142540 scopus 로고
    • Semiquinone free radicals and oxygen. Pulse radiolysis study of one electron transfer equilibra
    • Patel, K. B., and R. L. Willson. 1973. Semiquinone free radicals and oxygen. Pulse radiolysis study of one electron transfer equilibra. J. Chem. Soc. Faraday Trans. 69:814-825.
    • (1973) J. Chem. Soc. Faraday Trans , vol.69 , pp. 814-825
    • Patel, K.B.1    Willson, R.L.2
  • 43
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low-molecular-weight solutes
    • Philo, J. S. 1997. An improved function for fitting sedimentation velocity data for low-molecular-weight solutes. Biophys. J. 72:435-444.
    • (1997) Biophys. J , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 45
    • 0024237213 scopus 로고
    • Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium
    • Prossnitz, E., K. Nikaido, S. J. Ulbrich, and G. F. Ames. 1988. Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium. J. Biol. Chem. 263:17917-17920.
    • (1988) J. Biol. Chem , vol.263 , pp. 17917-17920
    • Prossnitz, E.1    Nikaido, K.2    Ulbrich, S.J.3    Ames, G.F.4
  • 46
    • 0037040603 scopus 로고    scopus 로고
    • PMF through the redox loop
    • Richardson, D., and G. Sawers. 2002. PMF through the redox loop. Science 295:1842-1843.
    • (2002) Science , vol.295 , pp. 1842-1843
    • Richardson, D.1    Sawers, G.2
  • 47
    • 33646082512 scopus 로고    scopus 로고
    • Reduction of soluble and insoluble iron forms by membrane fractions of Shewanella oneidensis grown under aerobic and anaerobic conditions
    • Ruebush, S. S., S. L. Brantley, and M. Tien. 2006. Reduction of soluble and insoluble iron forms by membrane fractions of Shewanella oneidensis grown under aerobic and anaerobic conditions. Appl. Environ. Microbiol. 72:2925-2935.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 2925-2935
    • Ruebush, S.S.1    Brantley, S.L.2    Tien, M.3
  • 48
    • 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. 2006. In vitro enzymatic reduction kinetics of mineral oxides by membrane fractions from Shewanella oneidensis MR-1. Geochim. Cosmochim. Acta 70:56-70.
    • (2006) Geochim. Cosmochim. Acta , vol.70 , pp. 56-70
    • Ruebush, S.S.1    Icopini, G.A.2    Brantley, S.L.3    Tien, M.4
  • 49
    • 84981766557 scopus 로고
    • Komplexone XVIII. Die Eisen(II)-und Eisen(III)-komplexe der Athylendiamin-tetraessig-saure und ihr Redoxgleichgewicht
    • Schwarzenbach, G., and J. Heller. 1951. Komplexone XVIII. Die Eisen(II)-und Eisen(III)-komplexe der Athylendiamin-tetraessig-saure und ihr Redoxgleichgewicht. Helv. Chim. Acta 34:576-591.
    • (1951) Helv. Chim. Acta , vol.34 , pp. 576-591
    • Schwarzenbach, G.1    Heller, J.2
  • 50
    • 0001784152 scopus 로고
    • Iron oxides in the laboratory: Preparation and characterization
    • R. M. Cornell and U. Schwertmann ed, John Wiley & Sons, New York, NY
    • Schwertmann, U., and R. M. Cornell. 1991. Iron oxides in the laboratory: preparation and characterization, p. 137. In R. M. Cornell and U. Schwertmann (ed.), The iron oxides: structure, properties, reactions, occurrences and uses. John Wiley & Sons, New York, NY.
    • (1991) The iron oxides: Structure, properties, reactions, occurrences and uses , pp. 137
    • Schwertmann, U.1    Cornell, R.M.2
  • 51
    • 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
  • 53
    • 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
  • 54
    • 0034924218 scopus 로고    scopus 로고
    • Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family
    • Steinle, A., P. Li, D. L. Morris, V. Groh, L. L. Lanier, R. K. Strong, and T. Spies. 2001. Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family. Immunogenetics 53:279-287.
    • (2001) Immunogenetics , vol.53 , pp. 279-287
    • Steinle, A.1    Li, P.2    Morris, D.L.3    Groh, V.4    Lanier, L.L.5    Strong, R.K.6    Spies, T.7
  • 55
    • 0003182409 scopus 로고
    • Kinetics and reaction stoichiometry in the reductive dissolution of manganese(IV) dioxide and Co(III) oxide by hydroquinone
    • Stone, A. T., and H. J. Ulrich. 1989. Kinetics and reaction stoichiometry in the reductive dissolution of manganese(IV) dioxide and Co(III) oxide by hydroquinone. J. Colloid Interface Sci. 132:509-522.
    • (1989) J. Colloid Interface Sci , vol.132 , pp. 509-522
    • Stone, A.T.1    Ulrich, H.J.2
  • 56
    • 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
  • 58
    • 0034371010 scopus 로고    scopus 로고
    • Bacterial manganese and iron reduction in aquatic sediments
    • Thamdrup, B. 2000. Bacterial manganese and iron reduction in aquatic sediments. Adv. Microb. Ecol. 16:1-84.
    • (2000) Adv. Microb. Ecol , vol.16 , pp. 1-84
    • Thamdrup, B.1
  • 60
    • 0031851364 scopus 로고    scopus 로고
    • Shewanella amazonensis sp. nov., a novel metal-reducing facultative anaerobe from Amazonian shelf muds
    • Venkateswaran, K., M. E. Dollhopf, R. Aller, E. Stackebrandt, and K. H. Nealson. 1998. Shewanella amazonensis sp. nov., a novel metal-reducing facultative anaerobe from Amazonian shelf muds. Int. J. Syst. Bacteriol. 48:965-972.
    • (1998) Int. J. Syst. Bacteriol , vol.48 , pp. 965-972
    • Venkateswaran, K.1    Dollhopf, M.E.2    Aller, R.3    Stackebrandt, E.4    Nealson, K.H.5
  • 61
    • 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 Microbiol. Lett. 184:143-148.
    • (2000) FEMS Microbiol. Lett , vol.184 , pp. 143-148
    • Wade, R.1    DiChristina, T.J.2
  • 63
    • 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., L. Shi, B. Chen, M. U. Mayer, B. H. Lower, Y. Lender, S. Bose, M. F. Hochella, J. K. Fredrickson, and T. C. Squier. 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    Lender, Y.6    Bose, S.7    Hochella, M.F.8    Fredrickson, J.K.9    Squier, T.C.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.