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Volumn 87, Issue 3, 2013, Pages 493-508

In vivo [Fe-S] cluster acquisition by IscR and NsrR, two stress regulators in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; ERPA PROTEIN; IRON SULFUR PROTEIN; ISCA PROTEIN; ISCR PROTEIN; ISCU PROTEIN; NSRR PROTEIN; SCAFFOLD PROTEIN; SUFA PROTEIN; SUFB PROTEIN; UNCLASSIFIED DRUG;

EID: 84873058881     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12135     Document Type: Article
Times cited : (50)

References (89)
  • 1
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar, J.N., Krebs, C., Frazzon, J., Huynh, B.H., Dean, D.R., and Johnson, M.K. (2000) IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 39: 7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 2
  • 3
    • 46649115965 scopus 로고    scopus 로고
    • NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions
    • Angelini, S., Gerez, C., Ollagnier-de Choudens, S., Sanakis, Y., Fontecave, M., Barras, F., and Py, B. (2008) NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions. J Biol Chem 283: 14084-14091.
    • (2008) J Biol Chem , vol.283 , pp. 14084-14091
    • Angelini, S.1    Gerez, C.2    Ollagnier-de Choudens, S.3    Sanakis, Y.4    Fontecave, M.5    Barras, F.6    Py, B.7
  • 5
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006-0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 2006-0008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 6
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk, J., and Lobreaux, S. (2005) Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci 10: 324-331.
    • (2005) Trends Plant Sci , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 7
    • 26444455549 scopus 로고    scopus 로고
    • How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins
    • Barras, F., Loiseau, L., and Py, B. (2005) How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins. Adv Microb Physiol 50: 41-101.
    • (2005) Adv Microb Physiol , vol.50 , pp. 41-101
    • Barras, F.1    Loiseau, L.2    Py, B.3
  • 8
    • 4744352703 scopus 로고    scopus 로고
    • Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor
    • Beaumont, H.J., Lens, S.I., Reijnders, W.N., Westerhoff, H.V., and van Spanning, R.J. (2004) Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor. Mol Microbiol 54: 148-158.
    • (2004) Mol Microbiol , vol.54 , pp. 148-158
    • Beaumont, H.J.1    Lens, S.I.2    Reijnders, W.N.3    van Westerhoff, H.V.4    Spanning, R.J.5
  • 9
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert, H. (1983) Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins. Anal Biochem 131: 373-378.
    • (1983) Anal Biochem , vol.131 , pp. 373-378
    • Beinert, H.1
  • 10
    • 31344459536 scopus 로고    scopus 로고
    • The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator
    • Bodenmiller, D.M., and Spiro, S. (2006) The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator. J Bacteriol 188: 874-881.
    • (2006) J Bacteriol , vol.188 , pp. 874-881
    • Bodenmiller, D.M.1    Spiro, S.2
  • 11
    • 58649101413 scopus 로고    scopus 로고
    • Bacterial ApbC protein has two biochemical activities that are required for in vivo function
    • Boyd, J.M., Sondelski, J.L., and Downs, D.M. (2009) Bacterial ApbC protein has two biochemical activities that are required for in vivo function. J Biol Chem 284: 110-118.
    • (2009) J Biol Chem , vol.284 , pp. 110-118
    • Boyd, J.M.1    Sondelski, J.L.2    Downs, D.M.3
  • 12
    • 0035154356 scopus 로고    scopus 로고
    • Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyldiphosphate from mevalonate: a novel system for the genetic analysis of the 2-C-methyl-d-erythritol 4-phosphate pathway for isoprenoid biosynthesis
    • Campos, N., Rodriguez-Concepcion, M., Sauret-Güeto, S., Gallego, F., Lois, L.M., and Boronat, A. (2001) Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyldiphosphate from mevalonate: a novel system for the genetic analysis of the 2-C-methyl-d-erythritol 4-phosphate pathway for isoprenoid biosynthesis. Biochem J 353: 59-67.
    • (2001) Biochem J , vol.353 , pp. 59-67
    • Campos, N.1    Rodriguez-Concepcion, M.2    Sauret-Güeto, S.3    Gallego, F.4    Lois, L.M.5    Boronat, A.6
  • 13
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P.P., and Wackernagel, W. (1995) Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158: 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 14
    • 0036646484 scopus 로고    scopus 로고
    • NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp
    • Cruz-Ramos, H., Crack, J., Wu, G., Hughes, M.N., Scott, C., Thomson, A.J., etal. (2002) NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J 21: 3235-3244.
    • (2002) EMBO J , vol.21 , pp. 3235-3244
    • Cruz-Ramos, H.1    Crack, J.2    Wu, G.3    Hughes, M.N.4    Scott, C.5    Thomson, A.J.6
  • 15
    • 0037168511 scopus 로고    scopus 로고
    • Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron
    • D'Autreaux, B., Touati, D., Bersch, B., Latour, J.M., and Michaud-Soret, I. (2002) Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proc Natl Acad Sci USA 99: 16619-16624.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16619-16624
    • D'Autreaux, B.1    Touati, D.2    Bersch, B.3    Latour, J.M.4    Michaud-Soret, I.5
  • 16
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 17
    • 67349095027 scopus 로고    scopus 로고
    • Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA
    • Desnoyers, G., Morissette, A., Prevost, K., and Masse, E. (2009) Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA. EMBO J 28: 1551-1561.
    • (2009) EMBO J , vol.28 , pp. 1551-1561
    • Desnoyers, G.1    Morissette, A.2    Prevost, K.3    Masse, E.4
  • 18
    • 2142654882 scopus 로고    scopus 로고
    • Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
    • Ding, H., and Clark, R.J. (2004) Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem J 379: 433-440.
    • (2004) Biochem J , vol.379 , pp. 433-440
    • Ding, H.1    Clark, R.J.2
  • 19
    • 34250316617 scopus 로고    scopus 로고
    • The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase
    • Filenko, N., Spiro, S., Browning, D.F., Squire, D., Overton, T.W., Cole, J., and Constantinidou, C. (2007) The NsrR regulon of Escherichia coli K-12 includes genes encoding the hybrid cluster protein and the periplasmic, respiratory nitrite reductase. J Bacteriol 189: 4410-4417.
    • (2007) J Bacteriol , vol.189 , pp. 4410-4417
    • Filenko, N.1    Spiro, S.2    Browning, D.F.3    Squire, D.4    Overton, T.W.5    Cole, J.6    Constantinidou, C.7
  • 20
    • 0014037630 scopus 로고
    • A method for the rapid detection of acute iron toxicity
    • Fischer, D.S. (1967) A method for the rapid detection of acute iron toxicity. Clin Chem 13: 6-11.
    • (1967) Clin Chem , vol.13 , pp. 6-11
    • Fischer, D.S.1
  • 21
    • 15444363634 scopus 로고    scopus 로고
    • Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis
    • Flatley, J., Barrett, J., Pullan, S.T., Hughes, M.N., Green, J., and Poole, R.K. (2005) Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis. J Biol Chem 280: 10065-10072.
    • (2005) J Biol Chem , vol.280 , pp. 10065-10072
    • Flatley, J.1    Barrett, J.2    Pullan, S.T.3    Hughes, M.N.4    Green, J.5    Poole, R.K.6
  • 22
    • 79953298366 scopus 로고    scopus 로고
    • Iron-containing transcription factors and their roles as sensors
    • Fleischhacker, A.S., and Kiley, P.J. (2011) Iron-containing transcription factors and their roles as sensors. Curr Opin Chem Biol 15: 335-341.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 335-341
    • Fleischhacker, A.S.1    Kiley, P.J.2
  • 23
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint, D.H. (1996) Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J Biol Chem 271: 16068-16074.
    • (1996) J Biol Chem , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 24
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: ever-expanding roles
    • Fontecave, M. (2006) Iron-sulfur clusters: ever-expanding roles. Nat Chem Biol 2: 171-174.
    • (2006) Nat Chem Biol , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 25
    • 44549087696 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer
    • Fontecave, M., and Ollagnier-de-Choudens, S. (2008) Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer. Arch Biochem Biophys 474: 226-237.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 226-237
    • Fontecave, M.1    Ollagnier-de-Choudens, S.2
  • 26
    • 33646427470 scopus 로고    scopus 로고
    • IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli
    • Giel, J.L., Rodionov, D., Liu, M., Blattner, F.R., and Kiley, P.J. (2006) IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli. Mol Microbiol 60: 1058-1075.
    • (2006) Mol Microbiol , vol.60 , pp. 1058-1075
    • Giel, J.L.1    Rodionov, D.2    Liu, M.3    Blattner, F.R.4    Kiley, P.J.5
  • 27
    • 69949162828 scopus 로고    scopus 로고
    • Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes
    • Gupta, V., Sendra, M., Naik, S.G., Chahal, H.K., Huynh, B.H., Outten, F.W., etal. (2009) Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J Am Chem Soc 131: 6149-6153.
    • (2009) J Am Chem Soc , vol.131 , pp. 6149-6153
    • Gupta, V.1    Sendra, M.2    Naik, S.G.3    Chahal, H.K.4    Huynh, B.H.5    Outten, F.W.6
  • 28
    • 33845895269 scopus 로고    scopus 로고
    • Multiple regulators of the Flavohaemoglobin (hmp) gene of Salmonella enterica serovar Typhimurium include RamA, a transcriptional regulator conferring the multidrug resistance phenotype
    • Hernandez-Urzua, E., Zamorano-Sanchez, D.S., Ponce-Coria, J., Morett, E., Grogan, S., Poole, R.K., and Membrillo-Hernandez, J. (2007) Multiple regulators of the Flavohaemoglobin (hmp) gene of Salmonella enterica serovar Typhimurium include RamA, a transcriptional regulator conferring the multidrug resistance phenotype. Arch Microbiol 187: 67-77.
    • (2007) Arch Microbiol , vol.187 , pp. 67-77
    • Hernandez-Urzua, E.1    Zamorano-Sanchez, D.S.2    Ponce-Coria, J.3    Morett, E.4    Grogan, S.5    Poole, R.K.6    Membrillo-Hernandez, J.7
  • 29
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • Hoff, K.G., Silberg, J.J., and Vickery, L.E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc Natl Acad Sci USA 97: 7790-7795.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 30
    • 58149136356 scopus 로고    scopus 로고
    • Functional analysis of NsrR, a nitric oxide-sensing Rrf2 repressor in Neisseria gonorrhoeae
    • Isabella, V.M., Lapek, J.D., Jr, Kennedy, E.M., and Clark, V.L. (2009) Functional analysis of NsrR, a nitric oxide-sensing Rrf2 repressor in Neisseria gonorrhoeae. Mol Microbiol 71: 227-239.
    • (2009) Mol Microbiol , vol.71 , pp. 227-239
    • Isabella, V.M.1    Lapek Jr., J.D.2    Kennedy, E.M.3    Clark, V.L.4
  • 31
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang, S., and Imlay, J.A. (2010) Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol Microbiol 78: 1448-1467.
    • (2010) Mol Microbiol , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 32
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D.C., Dean, D.R., Smith, A.D., and Johnson, M.K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74: 247-281.
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 33
    • 34249857689 scopus 로고    scopus 로고
    • Escherichia coli di-iron YtfE protein is necessary for the repair of stress-damaged iron-sulfur clusters
    • Justino, M.C., Almeida, C.C., Teixeira, M., and Saraiva, L.M. (2007) Escherichia coli di-iron YtfE protein is necessary for the repair of stress-damaged iron-sulfur clusters. J Biol Chem 282: 10352-10359.
    • (2007) J Biol Chem , vol.282 , pp. 10352-10359
    • Justino, M.C.1    Almeida, C.C.2    Teixeira, M.3    Saraiva, L.M.4
  • 34
    • 0026548467 scopus 로고
    • The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii
    • Kennedy, C., and Dean, D. (1992) The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii. Mol Gen Genet 231: 494-498.
    • (1992) Mol Gen Genet , vol.231 , pp. 494-498
    • Kennedy, C.1    Dean, D.2
  • 35
    • 0030986002 scopus 로고    scopus 로고
    • Deletion of two downstream genes alters expression of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough
    • Keon, R.G., Fu, R., and Voordouw, G. (1997) Deletion of two downstream genes alters expression of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough. Arch Microbiol 167: 376-383.
    • (1997) Arch Microbiol , vol.167 , pp. 376-383
    • Keon, R.G.1    Fu, R.2    Voordouw, G.3
  • 36
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley, P.J., and Beinert, H. (2003) The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol 6: 181-185.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 37
    • 84860318059 scopus 로고    scopus 로고
    • Global transcriptional control by NsrR in Bacillus subtilis
    • Kommineni, S., Lama, A., Popescu, B., and Nakano, M.M. (2012) Global transcriptional control by NsrR in Bacillus subtilis. J Bacteriol 194: 1679-1688.
    • (2012) J Bacteriol , vol.194 , pp. 1679-1688
    • Kommineni, S.1    Lama, A.2    Popescu, B.3    Nakano, M.M.4
  • 39
    • 0000405377 scopus 로고
    • Notes on the use of propagation of error formulas
    • Ku, H.H. (1966) Notes on the use of propagation of error formulas. J Res 70: 263-273.
    • (1966) J Res , vol.70 , pp. 263-273
    • Ku, H.H.1
  • 40
    • 33745217828 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
    • Layer, G., Ollagnier-de Choudens, S., Sanakis, Y., and Fontecave, M. (2006) Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J Biol Chem 281: 16256-16263.
    • (2006) J Biol Chem , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier-de Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 42
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill, R., and Muhlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu Rev Biochem 77: 669-700.
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 43
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M., and Barras, F. (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278: 38352-38359.
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 44
    • 35348876543 scopus 로고    scopus 로고
    • ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli
    • Loiseau, L., Gerez, C., Bekker, M., Ollagnier-de Choudens, S., Py, B., Sanakis, Y., etal. (2007) ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc Natl Acad Sci USA 104: 13626-13631.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13626-13631
    • Loiseau, L.1    Gerez, C.2    Bekker, M.3    Ollagnier-de Choudens, S.4    Py, B.5    Sanakis, Y.6
  • 45
    • 0030611120 scopus 로고    scopus 로고
    • Roles of RpoS (sigmaS), IHF and ppGpp in the expression of the hmp gene encoding the flavohemoglobin (Hmp) of Escherichia coli K-12
    • Membrillo-Hernandez, J., Cook, G.M., and Poole, R.K. (1997) Roles of RpoS (sigmaS), IHF and ppGpp in the expression of the hmp gene encoding the flavohemoglobin (Hmp) of Escherichia coli K-12. Mol Gen Genet 254: 599-603.
    • (1997) Mol Gen Genet , vol.254 , pp. 599-603
    • Membrillo-Hernandez, J.1    Cook, G.M.2    Poole, R.K.3
  • 46
    • 0031844664 scopus 로고    scopus 로고
    • A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region
    • Membrillo-Hernandez, J., Coopamah, M.D., Channa, A., Hughes, M.N., and Poole, R.K. (1998) A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol Microbiol 29: 1101-1112.
    • (1998) Mol Microbiol , vol.29 , pp. 1101-1112
    • Membrillo-Hernandez, J.1    Coopamah, M.D.2    Channa, A.3    Hughes, M.N.4    Poole, R.K.5
  • 47
    • 56249090364 scopus 로고    scopus 로고
    • The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR
    • Mettert, E.L., Outten, F.W., Wanta, B., and Kiley, P.J. (2008) The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR. J Mol Biol 384: 798-811.
    • (2008) J Mol Biol , vol.384 , pp. 798-811
    • Mettert, E.L.1    Outten, F.W.2    Wanta, B.3    Kiley, P.J.4
  • 48
  • 49
    • 0037415722 scopus 로고    scopus 로고
    • SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin, L., Loiseau, L., Expert, D., and Barras, F. (2003) SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J 22: 427-437.
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 50
    • 61349134073 scopus 로고    scopus 로고
    • Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation
    • Nesbit, A.D., Giel, J.L., Rose, J.C., and Kiley, P.J. (2009) Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation. J Mol Biol 387: 28-41.
    • (2009) J Mol Biol , vol.387 , pp. 28-41
    • Nesbit, A.D.1    Giel, J.L.2    Rose, J.C.3    Kiley, P.J.4
  • 51
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten, F.W., Wood, M.J., Munoz, F.M., and Storz, G. (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278: 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 52
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F.W., Djaman, O., and Storz, G. (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52: 861-872.
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 53
    • 40449114521 scopus 로고    scopus 로고
    • Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers
    • Overton, T.W., Justino, M.C., Li, Y., Baptista, J.M., Melo, A.M., Cole, J.A., and Saraiva, L.M. (2008) Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers. J Bacteriol 190: 2004-2013.
    • (2008) J Bacteriol , vol.190 , pp. 2004-2013
    • Overton, T.W.1    Justino, M.C.2    Li, Y.3    Baptista, J.M.4    Melo, A.M.5    Cole, J.A.6    Saraiva, L.M.7
  • 54
    • 70350144292 scopus 로고    scopus 로고
    • NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility
    • Partridge, J.D., Bodenmiller, D.M., Humphrys, M.S., and Spiro, S. (2009) NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility. Mol Microbiol 73: 680-694.
    • (2009) Mol Microbiol , vol.73 , pp. 680-694
    • Partridge, J.D.1    Bodenmiller, D.M.2    Humphrys, M.S.3    Spiro, S.4
  • 55
    • 0032933919 scopus 로고    scopus 로고
    • SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli
    • Patzer, S.I., and Hantke, K. (1999) SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J Bacteriol 181: 3307-3309.
    • (1999) J Bacteriol , vol.181 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 56
    • 84857408142 scopus 로고    scopus 로고
    • Delivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA
    • Pinske, C., and Sawers, R.G. (2012a) Delivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA. PLoS ONE 7: e31755.
    • (2012) PLoS ONE , vol.7
    • Pinske, C.1    Sawers, R.G.2
  • 57
    • 84855895055 scopus 로고    scopus 로고
    • A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12
    • Pinske, C., and Sawers, R.G. (2012b) A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12. J Bacteriol 194: 346-353.
    • (2012) J Bacteriol , vol.194 , pp. 346-353
    • Pinske, C.1    Sawers, R.G.2
  • 58
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • Poole, R.K., Anjum, M.F., Membrillo-Hernandez, J., Kim, S.O., Hughes, M.N., and Stewart, V. (1996) Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J Bacteriol 178: 5487-5492.
    • (1996) J Bacteriol , vol.178 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hernandez, J.3    Kim, S.O.4    Hughes, M.N.5    Stewart, V.6
  • 60
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: bacterial strategies
    • Py, B., and Barras, F. (2010) Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 8: 436-446.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 61
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • Py, B., Moreau, P.L., and Barras, F. (2011) Fe-S clusters, fragile sentinels of the cell. Curr Opin Microbiol 14: 218-223.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 62
    • 84867044598 scopus 로고    scopus 로고
    • Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier
    • Py, B., Gerez, C., Angelini, S., Planel, R., Vinella, D., Loiseau, L., etal. (2012) Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier. Mol Microbiol 86: 155-171.
    • (2012) Mol Microbiol , vol.86 , pp. 155-171
    • Py, B.1    Gerez, C.2    Angelini, S.3    Planel, R.4    Vinella, D.5    Loiseau, L.6
  • 63
    • 51549086290 scopus 로고    scopus 로고
    • Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate
    • Rankin, L.D., Bodenmiller, D.M., Partridge, J.D., Nishino, S.F., Spain, J.C., and Spiro, S. (2008) Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate. J Bacteriol 190: 6170-6177.
    • (2008) J Bacteriol , vol.190 , pp. 6170-6177
    • Rankin, L.D.1    Bodenmiller, D.M.2    Partridge, J.D.3    Nishino, S.F.4    Spain, J.C.5    Spiro, S.6
  • 64
    • 60649117402 scopus 로고    scopus 로고
    • Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein
    • Riboldi, G.P., Verli, H., and Frazzon, J. (2009) Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein. BMC Biochem 10: 3.
    • (2009) BMC Biochem , vol.10 , pp. 3
    • Riboldi, G.P.1    Verli, H.2    Frazzon, J.3
  • 65
    • 85044710067 scopus 로고    scopus 로고
    • Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks
    • Rodionov, D.A., Dubchak, I.L., Arkin, A.P., Alm, E.J., and Gelfand, M.S. (2005) Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks. PLoS Comput Biol 1: e55.
    • (2005) PLoS Comput Biol , vol.1
    • Rodionov, D.A.1    Dubchak, I.L.2    Arkin, A.P.3    Alm, E.J.4    Gelfand, M.S.5
  • 66
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz, C.J., Djaman, O., Imlay, J.A., and Kiley, P.J. (2000) The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc Natl Acad Sci USA 97: 9009-9014.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 67
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C.J., Giel, J.L., Patschkowski, T., Luther, C., Ruzicka, F.J., Beinert, H., and Kiley, P.J. (2001) IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc Natl Acad Sci USA 98: 14895-14900.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 68
    • 33947540909 scopus 로고    scopus 로고
    • The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA
    • Sendra, M., Ollagnier de Choudens, S., Lascoux, D., Sanakis, Y., and Fontecave, M. (2007) The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett 581: 1362-1368.
    • (2007) FEBS Lett , vol.581 , pp. 1362-1368
    • Sendra, M.1    Ollagnier de Choudens, S.2    Lascoux, D.3    Sanakis, Y.4    Fontecave, M.5
  • 69
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R.W., Houman, F., and Kleckner, N. (1987) Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53: 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 70
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem 277: 28380-28383.
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 71
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
    • Tan, G., Lu, J., Bitoun, J.P., Huang, H., and Ding, H. (2009) IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions. Biochem J 420: 463-472.
    • (2009) Biochem J , vol.420 , pp. 463-472
    • Tan, G.1    Lu, J.2    Bitoun, J.P.3    Huang, H.4    Ding, H.5
  • 72
    • 61449135987 scopus 로고    scopus 로고
    • Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica
    • Thorgersen, M.P., and Downs, D.M. (2009) Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 155: 295-304.
    • (2009) Microbiology , vol.155 , pp. 295-304
    • Thorgersen, M.P.1    Downs, D.M.2
  • 73
    • 4644354002 scopus 로고    scopus 로고
    • Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
    • Tokumoto, U., Kitamura, S., Fukuyama, K., and Takahashi, Y. (2004) Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J Biochem 136: 199-209.
    • (2004) J Biochem , vol.136 , pp. 199-209
    • Tokumoto, U.1    Kitamura, S.2    Fukuyama, K.3    Takahashi, Y.4
  • 74
    • 72049124821 scopus 로고    scopus 로고
    • The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein
    • Trotter, V., Vinella, D., Loiseau, L., Ollagnier de Choudens, S., Fontecave, M., and Barras, F. (2009) The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol 74: 1527-1542.
    • (2009) Mol Microbiol , vol.74 , pp. 1527-1542
    • Trotter, V.1    Vinella, D.2    Loiseau, L.3    Ollagnier de Choudens, S.4    Fontecave, M.5    Barras, F.6
  • 75
    • 56649095726 scopus 로고    scopus 로고
    • The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster
    • Tucker, N.P., Hicks, M.G., Clarke, T.A., Crack, J.C., Chandra, G., Le Brun, N.E., etal. (2008) The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster. PLoS ONE 3: e3623.
    • (2008) PLoS ONE , vol.3
    • Tucker, N.P.1    Hicks, M.G.2    Clarke, T.A.3    Crack, J.C.4    Chandra, G.5    Le Brun, N.E.6
  • 76
    • 77950862348 scopus 로고    scopus 로고
    • There's NO stopping NsrR, a global regulator of the bacterial NO stress response
    • Tucker, N.P., Le Brun, N.E., Dixon, R., and Hutchings, M.I. (2010) There's NO stopping NsrR, a global regulator of the bacterial NO stress response. Trends Microbiol 18: 149-156.
    • (2010) Trends Microbiol , vol.18 , pp. 149-156
    • Tucker, N.P.1    Le Brun, N.E.2    Dixon, R.3    Hutchings, M.I.4
  • 77
    • 33846972315 scopus 로고    scopus 로고
    • The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence
    • Velayudhan, J., Castor, M., Richardson, A., Main-Hester, K.L., and Fang, F.C. (2007) The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. Mol Microbiol 63: 1495-1507.
    • (2007) Mol Microbiol , vol.63 , pp. 1495-1507
    • Velayudhan, J.1    Castor, M.2    Richardson, A.3    Main-Hester, K.L.4    Fang, F.C.5
  • 78
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L.E., and Cupp-Vickery, J.R. (2007) Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit Rev Biochem Mol Biol 42: 95-111.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 79
    • 0034528869 scopus 로고    scopus 로고
    • Selected amplification of the cell division genes ftsQ-ftsA-ftsZ in Escherichia coli
    • Vinella, D., Cashel, M., and D'Ari, R. (2000) Selected amplification of the cell division genes ftsQ-ftsA-ftsZ in Escherichia coli. Genetics 156: 1483-1492.
    • (2000) Genetics , vol.156 , pp. 1483-1492
    • Vinella, D.1    Cashel, M.2    D'Ari, R.3
  • 80
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • Vinella, D., Brochier-Armanet, C., Loiseau, L., Talla, E., and Barras, F. (2009) Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet 5: e1000497.
    • (2009) PLoS Genet , vol.5
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 81
    • 84855878361 scopus 로고    scopus 로고
    • Evidence that the folate-dependent proteins YgfZ and MnmEG have opposing effects on growth and on activity of the iron-sulfur enzyme MiaB
    • Waller, J.C., Ellens, K.W., Hasnain, G., Alvarez, S., Rocca, J.R., and Hanson, A.D. (2012) Evidence that the folate-dependent proteins YgfZ and MnmEG have opposing effects on growth and on activity of the iron-sulfur enzyme MiaB. J Bacteriol 194: 362-367.
    • (2012) J Bacteriol , vol.194 , pp. 362-367
    • Waller, J.C.1    Ellens, K.W.2    Hasnain, G.3    Alvarez, S.4    Rocca, J.R.5    Hanson, A.D.6
  • 82
    • 77954920916 scopus 로고    scopus 로고
    • Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor
    • Wollers, S., Layer, G., Garcia-Serres, R., Signor, L., Clemancey, M., Latour, J.M., etal. (2010) Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor. J Biol Chem 285: 23331-23341.
    • (2010) J Biol Chem , vol.285 , pp. 23331-23341
    • Wollers, S.1    Layer, G.2    Garcia-Serres, R.3    Signor, L.4    Clemancey, M.5    Latour, J.M.6
  • 83
    • 60849099323 scopus 로고    scopus 로고
    • IscR controls iron-dependent biofilm formation in Escherichia coli by regulating type I fimbria expression
    • Wu, Y., and Outten, F.W. (2009) IscR controls iron-dependent biofilm formation in Escherichia coli by regulating type I fimbria expression. J Bacteriol 191: 1248-1257.
    • (2009) J Bacteriol , vol.191 , pp. 1248-1257
    • Wu, Y.1    Outten, F.W.2
  • 84
    • 54349118938 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis systems and their crosstalk
    • Xu, X.M., and Moller, S.G. (2008) Iron-sulfur cluster biogenesis systems and their crosstalk. Chembiochem 9: 2355-2362.
    • (2008) Chembiochem , vol.9 , pp. 2355-2362
    • Xu, X.M.1    Moller, S.G.2
  • 85
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo, W.S., Lee, J.H., Lee, K.C., and Roe, J.H. (2006) IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol Microbiol 61: 206-218.
    • (2006) Mol Microbiol , vol.61 , pp. 206-218
    • Yeo, W.S.1    Lee, J.H.2    Lee, K.C.3    Roe, J.H.4
  • 86
    • 80054720193 scopus 로고    scopus 로고
    • The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes
    • Yeung, N., Gold, B., Liu, N.L., Prathapam, R., Sterling, H.J., Willams, E.R., and Butland, G. (2011) The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes. Biochemistry 50: 8957-8969.
    • (2011) Biochemistry , vol.50 , pp. 8957-8969
    • Yeung, N.1    Gold, B.2    Liu, N.L.3    Prathapam, R.4    Sterling, H.J.5    Willams, E.R.6    Butland, G.7
  • 87
    • 0347622754 scopus 로고    scopus 로고
    • pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12
    • Yohannes, E., Barnhart, D.M., and Slonczewski, J.L. (2004) pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12. J Bacteriol 186: 192-199.
    • (2004) J Bacteriol , vol.186 , pp. 192-199
    • Yohannes, E.1    Barnhart, D.M.2    Slonczewski, J.L.3
  • 88
    • 57449099080 scopus 로고    scopus 로고
    • Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster (dagger)
    • Yukl, E.T., Elbaz, M.A., Nakano, M.M., and Moenne-Loccoz, P. (2008) Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster (dagger). Biochemistry 47: 13084-13092.
    • (2008) Biochemistry , vol.47 , pp. 13084-13092
    • Yukl, E.T.1    Elbaz, M.A.2    Nakano, M.M.3    Moenne-Loccoz, P.4
  • 89
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng, L., and Dean, D.R. (1994) Catalytic formation of a nitrogenase iron-sulfur cluster. J Biol Chem 269: 18723-18726.
    • (1994) J Biol Chem , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2


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