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Volumn 5, Issue 7, 2016, Pages 679-688

CymA and Exogenous Flavins Improve Extracellular Electron Transfer and Couple It to Cell Growth in Mtr-Expressing Escherichia coli

Author keywords

bioelectrochemical systems; dissimilatory metal reducing bacteria; energy conservation; multiheme cytochrome c; synthetic biology

Indexed keywords

CYTOCHROME C; CYTOCHROME C CYMA; CYTOCHROME C MTR; FERRIC ION; FERROZINE; RIBOFLAVIN DERIVATIVE; UNCLASSIFIED DRUG; ABC TRANSPORTER; BACTERIAL PROTEIN; CYTOCHROME C(3); FERRIC CITRATE; FERRIC OXIDE; IRON; MTRA PROTEIN, BACTERIA; MTRC PROTEIN, SHEWANELLA; RECOMBINANT PROTEIN; RIBOFLAVIN;

EID: 84978698063     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.5b00279     Document Type: Article
Times cited : (87)

References (50)
  • 1
    • 0032468301 scopus 로고    scopus 로고
    • Biogenic iron mineralization accompanying the dissimilatory reduction of hydrous ferric oxide by a groundwater bacterium
    • Fredrickson, J. K., Zachara, J. M., Kennedy, D. W., Dong, H., Onstott, T. C., Hinman, N. W., and Li, S.-M. (1998) Biogenic iron mineralization accompanying the dissimilatory reduction of hydrous ferric oxide by a groundwater bacterium Geochim. Cosmochim. Acta 62, 3239-3257 10.1016/S0016-7037(98)00243-9
    • (1998) Geochim. Cosmochim. Acta , vol.62 , pp. 3239-3257
    • Fredrickson, J.K.1    Zachara, J.M.2    Kennedy, D.W.3    Dong, H.4    Onstott, T.C.5    Hinman, N.W.6    Li, S.-M.7
  • 2
    • 77949915708 scopus 로고    scopus 로고
    • Biological synthesis of metal nanoparticles by microbes
    • Narayanan, K. and Sakthivel, N. (2010) Biological synthesis of metal nanoparticles by microbes Adv. Colloid Interface Sci. 156, 1-13 10.1016/j.cis.2010.02.001
    • (2010) Adv. Colloid Interface Sci. , vol.156 , pp. 1-13
    • Narayanan, K.1    Sakthivel, N.2
  • 4
    • 77749261551 scopus 로고    scopus 로고
    • Metals, minerals and microbes: Geomicrobiology and bioremediation
    • Gadd, G. M. (2010) Metals, minerals and microbes: geomicrobiology and bioremediation Microbiology 156, 609-643 10.1099/mic.0.037143-0
    • (2010) Microbiology , vol.156 , pp. 609-643
    • Gadd, G.M.1
  • 7
    • 84923885794 scopus 로고    scopus 로고
    • The Mtr Pathway of Shewanella oneidensis MR-1 Couples Substrate Utilization to Current Production in Escherichia coli
    • TerAvest, M. A., Zajdel, T. J., and Ajo-Franklin, C. M. (2014) The Mtr Pathway of Shewanella oneidensis MR-1 Couples Substrate Utilization to Current Production in Escherichia coli ChemElectroChem 1, 1874-1879 10.1002/celc.201402194
    • (2014) ChemElectroChem , vol.1 , pp. 1874-1879
    • TerAvest, M.A.1    Zajdel, T.J.2    Ajo-Franklin, C.M.3
  • 8
    • 41749120309 scopus 로고    scopus 로고
    • Dissimilatory iron reduction in Escherichia coli: Identification of CymA of Shewanella oneidensis and NapC of E. Coli as ferric reductases
    • Gescher, J. S., Cordova, C. D., and Spormann, A. M. (2008) Dissimilatory iron reduction in Escherichia coli: identification of CymA of Shewanella oneidensis and NapC of E. coli as ferric reductases Mol. Microbiol. 68, 706-719 10.1111/j.1365-2958.2008.06183.x
    • (2008) Mol. Microbiol. , vol.68 , pp. 706-719
    • Gescher, J.S.1    Cordova, C.D.2    Spormann, A.M.3
  • 9
    • 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 10.1128/AEM.01834-09
    • (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
  • 10
    • 84925379369 scopus 로고    scopus 로고
    • Unbalanced fermentation of glycerol in Escherichia coli via heterologous production of an electron transport chain and electrode interaction in microbial electrochemical cells
    • Sturm-Richter, K., Golitsch, F., Sturm, G., Kipf, E., Dittrich, A., Beblawy, S., Kerzenmacher, S., and Gescher, J. (2015) Unbalanced fermentation of glycerol in Escherichia coli via heterologous production of an electron transport chain and electrode interaction in microbial electrochemical cells Bioresour. Technol. 186, 89-96 10.1016/j.biortech.2015.02.116
    • (2015) Bioresour. Technol. , vol.186 , pp. 89-96
    • Sturm-Richter, K.1    Golitsch, F.2    Sturm, G.3    Kipf, E.4    Dittrich, A.5    Beblawy, S.6    Kerzenmacher, S.7    Gescher, J.8
  • 11
    • 84943587491 scopus 로고    scopus 로고
    • Crossing Over: Nanostructures that Move Electrons and Ions across Cellular Membranes
    • Ajo-Franklin, C. M. and Noy, A. (2015) Crossing Over: Nanostructures that Move Electrons and Ions across Cellular Membranes Adv. Mater. 27, 5797-5804 10.1002/adma.201500344
    • (2015) Adv. Mater. , vol.27 , pp. 5797-5804
    • Ajo-Franklin, C.M.1    Noy, A.2
  • 15
    • 56449092797 scopus 로고    scopus 로고
    • The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems
    • Simon, J., van Spanning, R. J. M., and Richardson, D. J. (2008) The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems Biochim. Biophys. Acta, Bioenerg. 1777, 1480-1490 10.1016/j.bbabio.2008.09.008
    • (2008) Biochim. Biophys. Acta, Bioenerg. , vol.1777 , pp. 1480-1490
    • Simon, J.1    Van Spanning, R.J.M.2    Richardson, D.J.3
  • 16
    • 84859951809 scopus 로고    scopus 로고
    • Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA
    • McMillan, D. G. G., Marritt, S. J., Butt, J. N., and Jeuken, L. J. C. (2012) Menaquinone-7 is specific cofactor in tetraheme quinol dehydrogenase CymA J. Biol. Chem. 287, 14215-14225 10.1074/jbc.M112.348813
    • (2012) J. Biol. Chem. , vol.287 , pp. 14215-14225
    • McMillan, D.G.G.1    Marritt, S.J.2    Butt, J.N.3    Jeuken, L.J.C.4
  • 17
    • 84937144196 scopus 로고    scopus 로고
    • Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1
    • Alves, M. N., Neto, S. E., Alves, A. S., and Fonseca, B. M. (2015) Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1 Front. Microbiol. 6, 665 10.3389/fmicb.2015.00665
    • (2015) Front. Microbiol. , vol.6 , pp. 665
    • Alves, M.N.1    Neto, S.E.2    Alves, A.S.3    Fonseca, B.M.4
  • 18
    • 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 10.1042/BJ20121467
    • (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
  • 19
    • 84937733230 scopus 로고    scopus 로고
    • A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime
    • Sturm, G., Richter, K., Doetsch, A., Heide, H., Louro, R. O., and Gescher, J. (2015) A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime ISME J. 9, 1802-1815 10.1038/ismej.2014.264
    • (2015) ISME J. , vol.9 , pp. 1802-1815
    • Sturm, G.1    Richter, K.2    Doetsch, A.3    Heide, H.4    Louro, R.O.5    Gescher, J.6
  • 21
    • 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 10.1128/AEM.00544-09
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 5218-5226
    • Ross, D.E.1    Brantley, S.L.2    Tien, M.3
  • 22
    • 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 10.1007/s00253-011-3653-0
    • (2012) Appl. Microbiol. Biotechnol. , vol.93 , pp. 41-48
    • Brutinel, E.D.1    Gralnick, J.A.2
  • 24
    • 84936746465 scopus 로고    scopus 로고
    • Bound Flavin Model Suggests Similar Electron Transfer Mechanisms in Shewanella and Geobacter
    • Okamoto, A., Nakamura, R., and Nealson, K. H. (2014) Bound Flavin Model Suggests Similar Electron Transfer Mechanisms in Shewanella and Geobacter ChemElectroChem 1, 1808-1812 10.1002/celc.201402151
    • (2014) ChemElectroChem , vol.1 , pp. 1808-1812
    • Okamoto, A.1    Nakamura, R.2    Nealson, K.H.3
  • 25
    • 78049289028 scopus 로고    scopus 로고
    • Probing electron transfer mechanisms in Shewanella oneidensis MR-1 using a nanoelectrode platform and single-cell imaging
    • Jiang, X. C., Hu, J. S., Fitzgerald, L. A., Biffinger, J. C., Xie, P., Ringeisen, B. R., and Lieber, C. M. (2010) Probing electron transfer mechanisms in Shewanella oneidensis MR-1 using a nanoelectrode platform and single-cell imaging Proc. Natl. Acad. Sci. U. S. A. 107, 16806-16810 10.1073/pnas.1011699107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16806-16810
    • Jiang, X.C.1    Hu, J.S.2    Fitzgerald, L.A.3    Biffinger, J.C.4    Xie, P.5    Ringeisen, B.R.6    Lieber, C.M.7
  • 27
    • 84874582197 scopus 로고    scopus 로고
    • Flavin electron shuttles dominate extracellular electron transfer by Shewanella oneidensis
    • Kotloski, N. J. and Gralnick, J. A. (2013) Flavin electron shuttles dominate extracellular electron transfer by Shewanella oneidensis mBio 4, e00553-12 10.1128/mBio.00553-12
    • (2013) MBio , vol.4 , pp. e00553-e00612
    • Kotloski, N.J.1    Gralnick, J.A.2
  • 28
    • 84871436225 scopus 로고    scopus 로고
    • Engineering an anaerobic metabolic regime in Pseudomonas putida KT2440 for the anoxic biodegradation of 1, 3-dichloroprop-1-ene
    • Nikel, P. I. and de Lorenzo, V. (2013) Engineering an anaerobic metabolic regime in Pseudomonas putida KT2440 for the anoxic biodegradation of 1, 3-dichloroprop-1-ene Metab. Eng. 15, 98-112 10.1016/j.ymben.2012.09.006
    • (2013) Metab. Eng. , vol.15 , pp. 98-112
    • Nikel, P.I.1    De Lorenzo, V.2
  • 29
    • 84930934882 scopus 로고    scopus 로고
    • Engineering mediator-based electroactivity in the obligate aerobic bacterium Pseudomonas putida KT2440
    • Schmitz, S., Nies, S., Wierckx, N., Blank, L. M., and Rosenbaum, M. A. (2015) Engineering mediator-based electroactivity in the obligate aerobic bacterium Pseudomonas putida KT2440 Front. Microbiol. 6, 284 10.3389/fmicb.2015.00284
    • (2015) Front. Microbiol. , vol.6 , pp. 284
    • Schmitz, S.1    Nies, S.2    Wierckx, N.3    Blank, L.M.4    Rosenbaum, M.A.5
  • 30
    • 84872183816 scopus 로고    scopus 로고
    • Construction and characterization of nitrate and nitrite respiring Pseudomonas putida KT2440 strains for anoxic biotechnical applications
    • Steen, A., Ütkür, F. O., Borrero-de Acuña, J. M., Bunk, B., Roselius, L., Bühler, B., Jahn, D., and Schobert, M. (2013) Construction and characterization of nitrate and nitrite respiring Pseudomonas putida KT2440 strains for anoxic biotechnical applications J. Biotechnol. 163, 155-165 10.1016/j.jbiotec.2012.09.015
    • (2013) J. Biotechnol. , vol.163 , pp. 155-165
    • Steen, A.1    Ütkür, F.O.2    Borrero-De Acuña, J.M.3    Bunk, B.4    Roselius, L.5    Bühler, B.6    Jahn, D.7    Schobert, M.8
  • 31
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis, H. M., Mirsky, E. A., and Voigt, C. A. (2009) Automated design of synthetic ribosome binding sites to control protein expression Nat. Biotechnol. 27, 946-950 10.1038/nbt.1568
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 32
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-Type Cytochrome Subunits of the cbb 3 Oxidase in Escherichia coli
    • Arslan, E., Schulz, H., Zufferey, R., Künzler, P., and Thöny-Meyer, L. (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 10.1006/bbrc.1998.9549
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Künzler, P.4    Thöny-Meyer, L.5
  • 33
    • 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 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 putrefaciens MR-1 J. Bacteriol. 179, 1143-1152
    • (1997) J. Bacteriol. , vol.179 , pp. 1143-1152
    • Myers, C.R.1    Myers, J.M.2
  • 34
    • 0036271921 scopus 로고    scopus 로고
    • Genetic complementation of an outer membrane cytochrome omcB mutant of Shewanella putrefaciens MR-1 requires omcB plus downstream DNA
    • Myers, J. M. and Myers, C. R. (2002) Genetic complementation of an outer membrane cytochrome omcB mutant of Shewanella putrefaciens MR-1 requires omcB plus downstream DNA Appl. Environ. Microbiol. 68, 2781-2793 10.1128/AEM.68.6.2781-2793.2002
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2781-2793
    • Myers, J.M.1    Myers, C.R.2
  • 36
    • 84903699495 scopus 로고    scopus 로고
    • Uncovering alternate charge transfer mechanisms in Escherichia coli chemically functionalized with conjugated oligoelectrolytes
    • Wang, V. B., Yantara, N., Koh, T. M., Kjelleberg, S., Zhang, Q., Bazan, G. C., Loo, S. C. J., and Mathews, N. (2014) Uncovering alternate charge transfer mechanisms in Escherichia coli chemically functionalized with conjugated oligoelectrolytes Chem. Commun. (Cambridge, U. K.) 50, 8223-8226 10.1039/c4cc02784a
    • (2014) Chem. Commun. (Cambridge, U. K.) , vol.50 , pp. 8223-8226
    • Wang, V.B.1    Yantara, N.2    Koh, T.M.3    Kjelleberg, S.4    Zhang, Q.5    Bazan, G.C.6    Loo, S.C.J.7    Mathews, N.8
  • 37
    • 79956134721 scopus 로고    scopus 로고
    • Cyclic voltammetric analysis of the electron transfer of Shewanella oneidensis MR-1 and nanofilament and cytochrome knock-out mutants
    • Carmona-Martinez, A. A., Harnisch, F., Fitzgerald, L. A., Biffinger, J. C., Ringeisen, B. R., and Schröder, U. (2011) Cyclic voltammetric analysis of the electron transfer of Shewanella oneidensis MR-1 and nanofilament and cytochrome knock-out mutants Bioelectrochemistry 81, 74-80 10.1016/j.bioelechem.2011.02.006
    • (2011) Bioelectrochemistry , vol.81 , pp. 74-80
    • Carmona-Martinez, A.A.1    Harnisch, F.2    Fitzgerald, L.A.3    Biffinger, J.C.4    Ringeisen, B.R.5    Schröder, U.6
  • 38
    • 0141994975 scopus 로고    scopus 로고
    • Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias, V. R. F., Al-Amoudi, A., Dubochet, J., and Beveridge, T. J. (2003) Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa J. Bacteriol. 185, 6112-6118 10.1128/JB.185.20.6112-6118.2003
    • (2003) J. Bacteriol. , vol.185 , pp. 6112-6118
    • Matias, V.R.F.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 39
    • 33646594697 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in three cell environments in Escherichia coli
    • Mullineaux, C. W., Nenninger, A., and Ray, N. (2006) Diffusion of green fluorescent protein in three cell environments in Escherichia coli J. Bacteriol. 188, 3442-3448 10.1128/JB.188.10.3442-3448.2006
    • (2006) J. Bacteriol. , vol.188 , pp. 3442-3448
    • Mullineaux, C.W.1    Nenninger, A.2    Ray, N.3
  • 40
    • 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 10.1039/c0mt00097c
    • (2011) Metallomics , vol.3 , pp. 344-348
    • Firer-Sherwood, M.A.1    Bewley, K.D.2    Mock, J.-Y.3    Elliott, S.J.4
  • 41
    • 0019132335 scopus 로고
    • Are growth rates of Escherichia coli in batch cultures limited by respiration?
    • Andersen, K. B. and Meyenburg, K. (1980) Are growth rates of Escherichia coli in batch cultures limited by respiration? J. Bacteriol. 144, 114-123
    • (1980) J. Bacteriol. , vol.144 , pp. 114-123
    • Andersen, K.B.1    Meyenburg, K.2
  • 42
    • 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. A., Kennedy, D. W., McCready, D. E., Madden, 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 10.1016/j.gca.2008.11.031
    • (2009) Geochim. Cosmochim. Acta , vol.73 , pp. 962-976
    • Bose, S.1    Hochella, M.F.2    Gorby, Y.A.3    Kennedy, D.W.4    McCready, D.E.5    Madden, A.S.6    Lower, B.H.7
  • 43
    • 84959568240 scopus 로고    scopus 로고
    • Transforming exoelectrogens for biotechnology using synthetic biology
    • TerAvest, M. A. and Ajo-Franklin, C. M. (2016) Transforming exoelectrogens for biotechnology using synthetic biology Biotechnol. Bioeng. 113, 687 10.1002/bit.25723
    • (2016) Biotechnol. Bioeng. , vol.113 , pp. 687
    • TerAvest, M.A.1    Ajo-Franklin, C.M.2
  • 46
    • 0035656383 scopus 로고    scopus 로고
    • Sorption of Fe (hydr) oxides to the surface of Shewanella putrefaciens: Cell-bound fine-grained minerals are not always formed de novo
    • Glasauer, S., Langley, S., and Beveridge, T. J. (2001) Sorption of Fe (hydr) oxides to the surface of Shewanella putrefaciens: cell-bound fine-grained minerals are not always formed de novo Appl. Environ. Microbiol. 67, 5544-5550 10.1128/AEM.67.12.5544-5550.2001
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5544-5550
    • Glasauer, S.1    Langley, S.2    Beveridge, T.J.3
  • 47
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: Roles of flagella, motility, chemotaxis and type i pili
    • Pratt, L. A. and Kolter, R. (1998) Genetic analysis of Escherichia coli biofilm formation: roles of flagella, motility, chemotaxis and type I pili Mol. Microbiol. 30, 285-293 10.1046/j.1365-2958.1998.01061.x
    • (1998) Mol. Microbiol. , vol.30 , pp. 285-293
    • Pratt, L.A.1    Kolter, R.2
  • 48
    • 33750622462 scopus 로고    scopus 로고
    • Biological control of the size and reactivity of catalytic Pd (0) produced by Shewanella oneidensis
    • De Windt, W., Boon, N., and Van den Bulcke, J. (2006) Biological control of the size and reactivity of catalytic Pd (0) produced by Shewanella oneidensis Antonie van Leeuwenhoek 90, 377-389 10.1007/s10482-006-9088-4
    • (2006) Antonie van Leeuwenhoek , vol.90 , pp. 377-389
    • De Windt, W.1    Boon, N.2    Van Den Bulcke, J.3
  • 49
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis Nat. Methods 9, 671-675 10.1038/nmeth.2089
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 50
    • 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 10.1021/ac60289a016
    • (1970) Anal. Chem. , vol.42 , pp. 779-781
    • Stookey, L.L.1


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