메뉴 건너뛰기




Volumn 50, Issue 11, 2011, Pages 1582-1590

Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress

Author keywords

Chelatable iron pool; Dinitrosyl iron complex; Free radicals; Iron sulfur clusters; Nitric oxide

Indexed keywords

2,2' BIPYRIDINE; 3,3 BIS(2 AMINOETHYL) 1 HYDROXY 2 OXOTRIAZENE; ACONITATE HYDRATASE; BACTERIAL ENZYME; BACTERIAL PROTEIN; CHLORAMPHENICOL; DIHYDROXYACID DEHYDRATASE; DINITROSYL IRON COMPLEX; HEAT SHOCK COGNATE PROTEIN; HEAT SHOCK PROTEIN; HYDROLYASE; IRON; IRON COMPLEX; IRON SULFUR PROTEIN; NITRIC OXIDE; RECOMBINANT ACONITATE HYDRATASE B; RECOMBINANT PROTEIN; SINGLE STRANDED DNA BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SOXR; UNCLASSIFIED DRUG;

EID: 79955583925     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.03.005     Document Type: Article
Times cited : (39)

References (68)
  • 1
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • DOI 10.1042/0264-6021:3570593
    • W.K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615 (Pubitemid 32735142)
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 2
    • 75149193813 scopus 로고    scopus 로고
    • Mechanisms of nitrite reduction to nitric oxide in the heart and vessel wall
    • J.L. Zweier, H. Li, A. Samouilov, and X. Liu Mechanisms of nitrite reduction to nitric oxide in the heart and vessel wall Nitric Oxide 22 2010 83 90
    • (2010) Nitric Oxide , vol.22 , pp. 83-90
    • Zweier, J.L.1    Li, H.2    Samouilov, A.3    Liu, X.4
  • 3
    • 0042858242 scopus 로고    scopus 로고
    • Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the no-sensing regulator Fnr, and flavohemoglobin Hmp
    • DOI 10.1074/jbc.M303282200
    • H. Corker, and R.K. Poole Nitric oxide formation by Escherichia coli: dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp J. Biol. Chem. 278 2003 31584 31592 (Pubitemid 37048336)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31584-31592
    • Corker, H.1    Poole, R.K.2
  • 4
    • 0032789444 scopus 로고    scopus 로고
    • Nitric oxide: A unique endogenous signaling molecule in vascular biology
    • DOI 10.1023/A:1020150124721
    • L.J. Ignarro Nitric oxide: a unique endogenous signaling molecule in vascular biology Biosci. Rep. 19 1999 51 71 (Pubitemid 29334198)
    • (1999) Bioscience Reports , vol.19 , Issue.2 , pp. 51-71
    • Ignarro, L.J.1
  • 5
    • 0030937832 scopus 로고    scopus 로고
    • Nitric oxide and macrophage function
    • DOI 10.1146/annurev.immunol.15.1.323
    • J. MacMicking, Q.W. Xie, and C. Nathan Nitric oxide and macrophage function Annu. Rev. Immunol. 15 1997 323 350 (Pubitemid 27169284)
    • (1997) Annual Review of Immunology , vol.15 , pp. 323-350
    • MacMicking, J.1    Xie, Q.-W.2    Nathan, C.3
  • 7
    • 13244299310 scopus 로고    scopus 로고
    • New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide
    • DOI 10.1074/jbc.M411070200
    • M.C. Justino, J.B. Vicente, M. Teixeira, and L.M. Saraiva New genes implicated in the protection of anaerobically grown Escherichia coli against nitric oxide J. Biol. Chem. 280 2005 2636 2643 (Pubitemid 40189367)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2636-2643
    • Justino, M.C.1    Vicente, J.B.2    Teixeira, M.3    Saraiva, L.M.4
  • 9
    • 33947420458 scopus 로고    scopus 로고
    • Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S nitrosation
    • DOI 10.1128/JB.01354-06
    • S.T. Pullan, M.D. Gidley, R.A. Jones, J. Barrett, T.M. Stevanin, R.C. Read, J. Green, and R.K. Poole Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: unaltered methionine biosynthesis indicates lack of S nitrosation J. Bacteriol. 189 2007 1845 1855 (Pubitemid 46446147)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1845-1855
    • Pullan, S.T.1    Gidley, M.D.2    Jones, R.A.3    Barrett, J.4    Stevanin, T.M.5    Read, R.C.6    Green, J.7    Poole, R.K.8
  • 10
    • 59149092730 scopus 로고    scopus 로고
    • Metalloregulatory proteins and nitric oxide signalling in bacteria
    • S. Spiro Metalloregulatory proteins and nitric oxide signalling in bacteria Biochem. Soc. Trans. 36 2008 1160 1164
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1160-1164
    • Spiro, S.1
  • 11
    • 34249715269 scopus 로고    scopus 로고
    • Fe-S cluster proteins are intracellular targets for nitric oxide generated luminally at the gastro-oesophageal junction
    • DOI 10.1016/j.niox.2007.02.002, PII S1089860307000195
    • K. Asanuma, K. Iijima, N. Ara, T. Koike, J. Yoshitake, S. Ohara, T. Shimosegawa, and T. Yoshimura Fe-S cluster proteins are intracellular targets for nitric oxide generated luminally at the gastro-oesophageal junction Nitric Oxide 16 2007 395 402 (Pubitemid 46843606)
    • (2007) Nitric Oxide - Biology and Chemistry , vol.16 , Issue.4 , pp. 395-402
    • Asanuma, K.1    Iijima, K.2    Ara, N.3    Koike, T.4    Yoshitake, J.5    Ohara, S.6    Shimosegawa, T.7    Yoshimura, T.8
  • 12
    • 54249159666 scopus 로고    scopus 로고
    • Nitric oxide-induced bacteriostasis and modification of iron-sulphur proteins in Escherichia coli
    • B. Ren, N. Zhang, J. Yang, and H. Ding Nitric oxide-induced bacteriostasis and modification of iron-sulphur proteins in Escherichia coli Mol. Microbiol. 70 2008 953 964
    • (2008) Mol. Microbiol. , vol.70 , pp. 953-964
    • Ren, B.1    Zhang, N.2    Yang, J.3    Ding, H.4
  • 13
  • 14
    • 57449099080 scopus 로고    scopus 로고
    • Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster
    • E.T. Yukl, M.A. Elbaz, M.M. Nakano, and P. Moenne-Loccoz Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe-4S cluster Biochemistry 47 2008 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
  • 15
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • DOI 10.1146/annurev.biochem.74.082803.133518
    • D.C. Johnson, D.R. Dean, A.D. Smith, and M.K. Johnson Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74 2005 247 281 (Pubitemid 40995508)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 16
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • R. Lill Function and biogenesis of iron-sulphur proteins Nature 460 2009 831 838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 17
    • 56449093155 scopus 로고    scopus 로고
    • Reactions of synthetic [2Fe-2S] and [4Fe-4S] clusters with nitric oxide and nitrosothiols
    • T.C. Harrop, Z.J. Tonzetich, E. Reisner, and S.J. Lippard Reactions of synthetic [2Fe-2S] and [4Fe-4S] clusters with nitric oxide and nitrosothiols J. Am. Chem. Soc. 130 2008 15602 15610
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15602-15610
    • Harrop, T.C.1    Tonzetich, Z.J.2    Reisner, E.3    Lippard, S.J.4
  • 18
    • 67650540787 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes relevant to Rieske cluster nitrosylation
    • Z.J. Tonzetich, L.H. Do, and S.J. Lippard Dinitrosyl iron complexes relevant to Rieske cluster nitrosylation J. Am. Chem. Soc. 131 2009 7964 7965
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7964-7965
    • Tonzetich, Z.J.1    Do, L.H.2    Lippard, S.J.3
  • 19
    • 0030950713 scopus 로고    scopus 로고
    • Interplay between NO and [Fe-S] clusters: Relevance to biological systems
    • J.C. Drapier Interplay between NO and [Fe-S] clusters: relevance to biological systems Methods 11 1997 319 329
    • (1997) Methods , vol.11 , pp. 319-329
    • Drapier, J.C.1
  • 20
    • 0030873539 scopus 로고    scopus 로고
    • An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide
    • M.C. Kennedy, W.E. Antholine, and H. Beinert An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide J. Biol. Chem. 272 1997 20340 20347
    • (1997) J. Biol. Chem. , vol.272 , pp. 20340-20347
    • Kennedy, M.C.1    Antholine, W.E.2    Beinert, H.3
  • 21
    • 0041355842 scopus 로고    scopus 로고
    • Chemistry of nitric oxide with protein-bound iron sulfur centers. Insights on physiological reactivity
    • DOI 10.1021/ja9901056
    • M.W. Foster, and J.A. Cowan Chemistry of nitric oxide with protein-bound iron sulfur centers: insights on physiological reactivity J. Am. Chem. Soc. 121 1999 4093 4100 (Pubitemid 29220282)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.17 , pp. 4093-4100
    • Foster, M.W.1    Cowan, J.A.2
  • 22
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers SoxR transcription activator
    • DOI 10.1073/pnas.97.10.5146
    • H. Ding, and B. Demple Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator Proc. Natl. Acad. Sci. USA 97 2000 5146 5150 (Pubitemid 30313686)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.10 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 23
    • 0036646484 scopus 로고    scopus 로고
    • NO sensing by FNR: Regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp
    • DOI 10.1093/emboj/cdf339
    • H. Cruz-Ramos, J. Crack, G. Wu, M.N. Hughes, C. Scott, A.J. Thomson, J. Green, and R.K. Poole NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp EMBO J. 21 2002 3235 3244 (Pubitemid 34760556)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3235-3244
    • Cruz-Ramos, H.1    Crack, J.2    Wu, G.3    Hughes, M.N.4    Scott, C.5    Thomson, A.J.6    Green, J.7    Poole, R.K.8
  • 24
    • 0037757545 scopus 로고    scopus 로고
    • Reversible inactivation of E. coli endonuclease III via modification of its [4Fe-4S] cluster by nitric oxide
    • DOI 10.1016/S1568-7864(03)00065-X
    • P.A. Rogers, L. Eide, A. Klungland, and H. Ding Reversible inactivation of E. coli endonuclease III by nitric oxide via modification of its [4Fe-4S] cluster DNA Repair 2 2003 809 817 (Pubitemid 36776286)
    • (2003) DNA Repair , vol.2 , Issue.7 , pp. 809-817
    • Rogers, P.A.1    Eide, L.2    Klungland, A.3    Ding, H.4
  • 25
    • 59849094881 scopus 로고    scopus 로고
    • Reactivity of nitric oxide with the [4Fe-4S] cluster of dihydroxyacid dehydratase from Escherichia coli
    • X. Duan, J. Yang, B. Ren, G. Tan, and H. Ding Reactivity of nitric oxide with the [4Fe-4S] cluster of dihydroxyacid dehydratase from Escherichia coli Biochem. J. 417 2009 783 789
    • (2009) Biochem. J. , vol.417 , pp. 783-789
    • Duan, X.1    Yang, J.2    Ren, B.3    Tan, G.4    Ding, H.5
  • 26
    • 64149092801 scopus 로고    scopus 로고
    • Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster
    • B. Ren, X. Duan, and H. Ding Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster J. Biol. Chem. 284 2009 4829 4835
    • (2009) J. Biol. Chem. , vol.284 , pp. 4829-4835
    • Ren, B.1    Duan, X.2    Ding, H.3
  • 27
    • 77953540441 scopus 로고    scopus 로고
    • Oxygen is required for the l-cysteine-mediated decomposition of the protein-bound dinitrosyl iron complexes
    • J. Yang, X. Duan, A.P. Landry, and H. Ding Oxygen is required for the l-cysteine-mediated decomposition of the protein-bound dinitrosyl iron complexes Free Radic. Biol. Med. 49 2010 268 274
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 268-274
    • Yang, J.1    Duan, X.2    Landry, A.P.3    Ding, H.4
  • 28
    • 0020610161 scopus 로고
    • Nitrite inhibition of Clostridium botulinum: Electron spin resonance detection of iron-nitric oxide complexes
    • D. Reddy, J.R. Lancaster Jr., and D.P. Cornforth Nitrite inhibition of Clostridium botulinum: electron spin resonance detection of iron-nitric oxide complexes Science 221 1983 769 770 (Pubitemid 13030637)
    • (1983) Science , vol.221 , Issue.4612 , pp. 769-770
    • Reddy, D.1    Lancaster Jr., J.R.2    Cornforth, D.P.3
  • 29
    • 0025117611 scopus 로고
    • EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
    • J.R. Lancaster Jr., and J.B. Hibbs Jr. EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages Proc. Natl. Acad. Sci. USA 87 1990 1223 1227
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1223-1227
    • Lancaster Jr., J.R.1    Hibbs Jr., J.B.2
  • 30
    • 0025830402 scopus 로고
    • Nitric oxide, a biological effector: Electron paramagnetic resonance detection of nitrosyl-iron-protein complexes in whole cells
    • Y. Henry, C. Ducrocq, J.C. Drapier, D. Servent, C. Pellat, and A. Guissani Nitric oxide, a biological effector: electron paramagnetic resonance detection of nitrosyl-iron-protein complexes in whole cells Eur. Biophys. J. 20 1991 1 15
    • (1991) Eur. Biophys. J. , vol.20 , pp. 1-15
    • Henry, Y.1    Ducrocq, C.2    Drapier, J.C.3    Servent, D.4    Pellat, C.5    Guissani, A.6
  • 31
    • 0025788509 scopus 로고
    • Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages
    • J.C. Drapier, C. Pellat, and Y. Henry Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages J. Biol. Chem. 266 1991 10162 10167 (Pubitemid 21906782)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.16 , pp. 10162-10167
    • Drapier, J.-C.1    Pellat, C.2    Henry, Y.3
  • 33
    • 0034646693 scopus 로고    scopus 로고
    • Cellular non-heme iron content is a determinant of nitric oxide-mediated apoptosis, necrosis, and caspase inhibition
    • DOI 10.1074/jbc.275.15.10954
    • Y.M. Kim, H.T. Chung, R.L. Simmons, and T.R. Billiar Cellular non-heme iron content is a determinant of nitric oxide- mediated apoptosis, necrosis, and caspase inhibition J. Biol. Chem. 275 2000 10954 10961 (Pubitemid 30212732)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 10954-10961
    • Kim, Y.-M.1    Chung, H.-T.2    Simmons, R.L.3    Billiar, T.R.4
  • 34
    • 33646732642 scopus 로고    scopus 로고
    • Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1
    • R.N. Watts, C. Hawkins, P. Ponka, and D.R. Richardson Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1 Proc. Natl. Acad. Sci. USA 103 2006 7670 7675
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7670-7675
    • Watts, R.N.1    Hawkins, C.2    Ponka, P.3    Richardson, D.R.4
  • 35
    • 57649194797 scopus 로고    scopus 로고
    • Nitric oxide-induced conversion of cellular chelatable iron into macromolecule-bound paramagnetic dinitrosyliron complexes
    • J.C. Toledo Jr., C.A. Bosworth, S.W. Hennon, H.A. Mahtani, H.A. Bergonia, and J.R. Lancaster Jr. Nitric oxide-induced conversion of cellular chelatable iron into macromolecule-bound paramagnetic dinitrosyliron complexes J. Biol. Chem. 283 2008 28926 28933
    • (2008) J. Biol. Chem. , vol.283 , pp. 28926-28933
    • Toledo Jr., J.C.1    Bosworth, C.A.2    Hennon, S.W.3    Mahtani, H.A.4    Bergonia, H.A.5    Lancaster Jr., J.R.6
  • 36
    • 63849086054 scopus 로고    scopus 로고
    • Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide
    • C.A. Bosworth, J.C. Toledo Jr., J.W. Zmijewski, Q. Li, and J.R. Lancaster Jr. Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide Proc. Natl. Acad. Sci. USA 106 2009 4671 4676
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4671-4676
    • Bosworth, C.A.1    Toledo Jr., J.C.2    Zmijewski, J.W.3    Li, Q.4    Lancaster Jr., J.R.5
  • 39
    • 0036525945 scopus 로고    scopus 로고
    • Non-heme iron nitrosyls in biology
    • A.R. Butler, and I.L. Megson Non-heme iron nitrosyls in biology Chem. Rev. 102 2002 1155 1166
    • (2002) Chem. Rev. , vol.102 , pp. 1155-1166
    • Butler, A.R.1    Megson, I.L.2
  • 40
    • 40949165720 scopus 로고    scopus 로고
    • The nitric oxide-iron interplay in mammalian cells: Transport and storage of dinitrosyl iron complexes
    • D.R. Richardson, and H.C. Lok The nitric oxide-iron interplay in mammalian cells: transport and storage of dinitrosyl iron complexes Biochim. Biophys. Acta 1780 2008 638 651
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 638-651
    • Richardson, D.R.1    Lok, H.C.2
  • 41
    • 67649781729 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes with thiolate ligands: Physico-chemistry, biochemistry and physiology
    • A.F. Vanin Dinitrosyl iron complexes with thiolate ligands: physico-chemistry, biochemistry and physiology Nitric Oxide 21 2009 1 13
    • (2009) Nitric Oxide , vol.21 , pp. 1-13
    • Vanin, A.F.1
  • 42
    • 0034098690 scopus 로고    scopus 로고
    • The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex
    • DOI 10.1254/jjp.82.95
    • T. Ueno, and T. Yoshimura The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex Jpn. J. Pharmacol. 82 2000 95 101 (Pubitemid 30153589)
    • (2000) Japanese Journal of Pharmacology , vol.82 , Issue.2 , pp. 95-101
    • Ueno, T.1    Yoshimura, T.2
  • 44
    • 0027637998 scopus 로고
    • Dinitrosyl complexes of iron with thiol-containing ligands and their reverse conversion into nitrosothiols
    • A.F. Vanin, I.V. Malenkova, O.I. Mordvintsev, and A. Miul'sh Dinitrosyl complexes of iron with thiol-containing ligands and their reverse conversion into nitrosothiols Biokhimiia 58 1993 1094 1103
    • (1993) Biokhimiia , vol.58 , pp. 1094-1103
    • Vanin, A.F.1    Malenkova, I.V.2    Mordvintsev, O.I.3    Miul'Sh, A.4
  • 45
    • 38749100215 scopus 로고    scopus 로고
    • Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli
    • DOI 10.1042/BJ20071166
    • J. Lu, J. Yang, G. Tan, and H. Ding Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli Biochem. J. 409 2008 535 543 (Pubitemid 351184972)
    • (2008) Biochemical Journal , vol.409 , Issue.2 , pp. 535-543
    • Lu, J.1    Yang, J.2    Tan, G.3    Ding, H.4
  • 46
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogs are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
    • G. Tan, J. Lu, J.P. Bitoun, H. Huang, and H. Ding IscA/SufA paralogs are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions Biochem. J. 420 2009 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
  • 47
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • DOI 10.1128/JB.185.1.221-230.2003
    • S. Varghese, Y. Tang, and J.A. Imlay Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion J. Bacteriol. 185 2003 221 230 (Pubitemid 36008840)
    • (2003) Journal of Bacteriology , vol.185 , Issue.1 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 48
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • D.H. Flint, M.H. Emptage, M.G. Finnegan, W. Fu, and M.K. Johnson The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase J. Biol. Chem. 268 1993 14732 14742 (Pubitemid 23206613)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 49
    • 0030903131 scopus 로고    scopus 로고
    • Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • L.E. Vickery, J.J. Silberg, and D.T. Ta Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli Protein Sci. 6 1997 1047 1056 (Pubitemid 27194145)
    • (1997) Protein Science , vol.6 , Issue.5 , pp. 1047-1056
    • Vickery, L.E.1    Silberg, J.J.2    Ta, D.T.3
  • 50
    • 48249095036 scopus 로고    scopus 로고
    • Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease i
    • D. Lu, and J.L. Keck Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I Proc. Natl. Acad. Sci. USA 105 2008 9169 9174
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9169-9174
    • Lu, D.1    Keck, J.L.2
  • 51
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • M. Kitagawa, T. Ara, M. Arifuzzaman, T. Ioka-Nakamichi, E. Inamoto, H. Toyonaga, and H. Mori Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research DNA Res. 12 2005 291 299
    • (2005) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 53
    • 0035903119 scopus 로고    scopus 로고
    • L-Cysteine-mediated destabilization of dinitrosyl iron complexes in proteins
    • P.A. Rogers, and H. Ding l-Cysteine-mediated destabilization of dinitrosyl iron complexes in proteins J. Biol. Chem. 276 2001 30980 30986
    • (2001) J. Biol. Chem. , vol.276 , pp. 30980-30986
    • Rogers, P.A.1    Ding, H.2
  • 54
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • DOI 10.1074/jbc.273.21.13264
    • L. Zheng, V.L. Cash, D.H. Flint, and D.R. Dean Assembly of iron-sulfur clusters: identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii J. Biol. Chem. 273 1998 13264 13272 (Pubitemid 28246899)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 55
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in Archaea and plastids
    • DOI 10.1074/jbc.C200365200
    • Y. Takahashi, and U. Tokumoto A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids J. Biol. Chem. 277 2002 28380 28383 (Pubitemid 41079260)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.32 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 56
    • 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
    • V. Gupta, M. Sendra, S.G. Naik, H.K. Chahal, B.H. Huynh, F.W. Outten, M. Fontecave, and S. Ollagnier de Choudens 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 2009 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    Fontecave, M.7    Ollagnier De Choudens, S.8
  • 58
    • 0036249684 scopus 로고    scopus 로고
    • The chelatable iron pool in living cells: A methodically defined quantity
    • DOI 10.1515/BC.2002.051
    • F. Petrat, H. de Groot, R. Sustmann, and U. Rauen The chelatable iron pool in living cells: a methodically defined quantity Biol. Chem. 383 2002 489 502 (Pubitemid 34506286)
    • (2002) Biological Chemistry , vol.383 , Issue.3-4 , pp. 489-502
    • Petrat, F.1    De Groot, H.2    Sustmann, R.3    Rauen, U.4
  • 59
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • R.K. Poole, M.F. Anjum, J. Membrillo-Hernandez, S.O. Kim, M.N. Hughes, and V. Stewart Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 J. Bacteriol. 178 1996 5487 5492 (Pubitemid 26304384)
    • (1996) Journal of Bacteriology , vol.178 , Issue.18 , 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
  • 62
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage
    • DOI 10.1016/S0891-5849(02)00825-0, PII S0891584902008250
    • G. Cairo, S. Recalcati, A. Pietrangelo, and G. Minotti The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage Free Radic. Biol. Med. 32 2002 1237 1243 (Pubitemid 34607627)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 63
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • T. Rouault, and R. Klausner Regulation of iron metabolism in eukaryotes Curr. Top. Cell Regul. 35 1997 1 19
    • (1997) Curr. Top. Cell Regul. , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 64
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • DOI 10.1111/j.1365-2958.2004.04025.x
    • F.W. Outten, O. Djaman, and G. Storz A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli Mol. Microbiol. 52 2004 861 872 (Pubitemid 38621754)
    • (2004) Molecular Microbiology , vol.52 , Issue.3 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 66
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding
    • N. Khoroshilova, H. Beinert, and P.J. Kiley Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding Proc. Natl. Acad. Sci. USA 92 1995 2499 2503
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2499-2503
    • Khoroshilova, N.1    Beinert, H.2    Kiley, P.J.3
  • 67
    • 79953298366 scopus 로고    scopus 로고
    • Iron-containing transcription factors and their roles as sensors
    • A.S. Fleischhacker, and P.J. Kiley Iron-containing transcription factors and their roles as sensors Curr. Opin. Chem. Biol. 15 2011 335 341
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 335-341
    • Fleischhacker, A.S.1    Kiley, P.J.2
  • 68
    • 70349330788 scopus 로고    scopus 로고
    • Anionic mixed thiolate-sulfide-bridged Roussin's red esters [(NO)2Fe(mu-SR)(mu-S)Fe(NO)2]- (R = Et, Me, Ph): A key intermediate for transformation of dinitrosyl iron complexes (DNICs) to [2Fe-2S] clusters
    • T.T. Lu, H.W. Huang, and W.F. Liaw Anionic mixed thiolate-sulfide-bridged Roussin's red esters [(NO)2Fe(mu-SR)(mu-S)Fe(NO)2]- (R = Et, Me, Ph): a key intermediate for transformation of dinitrosyl iron complexes (DNICs) to [2Fe-2S] clusters Inorg. Chem. 48 2009 9027 9035
    • (2009) Inorg. Chem. , vol.48 , pp. 9027-9035
    • Lu, T.T.1    Huang, H.W.2    Liaw, W.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.