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Volumn 1853, Issue 6, 2015, Pages 1436-1447

Assembly of Fe/S proteins in bacterial systems. Biochemistry of the bacterial ISC system

Author keywords

Fe S assembly; Fe S transfer; Frataxin; Iron sulfur; Protein complex; Protein protein interaction

Indexed keywords

ESCHERICHIA COLI PROTEIN; IRON; IRON SULFUR PROTEIN; PROTEIN BINDING;

EID: 84939946161     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.12.009     Document Type: Review
Times cited : (86)

References (120)
  • 1
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 2000, 5:2-15.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 2
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: ever-expanding roles
    • Fontecave M. Iron-sulfur clusters: ever-expanding roles. Nat. Chem. Biol. 2006, 2:171-174.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 3
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 4
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • Py B., Moreau P.L., Barras F. Fe-S clusters, fragile sentinels of the cell. Curr. Opin. Microbiol. 2011, 14:218-223.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 5
    • 0024743814 scopus 로고
    • Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
    • Jacobson M.R., et al. Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. Mol. Gen. Genet. 1989, 219:49-57.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 49-57
    • Jacobson, M.R.1
  • 6
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry
    • Frazzon J., Dean D.R. Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 2003, 7:166-173.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 7
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters
    • Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii.
    • Zheng L., Cash V.L., Flint D.H., Dean D.R. Assembly of iron-sulfur clusters. J. Biol. Chem. 1998, 273:13264-13272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 8
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi Y., Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 2002, 277:28380-28383.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 9
    • 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., Barras F. SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 2003, 22:427-437.
    • (2003) EMBO J. , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 10
    • 0034719118 scopus 로고    scopus 로고
    • Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori
    • Olson J.W., Agar J.N., Johnson M.K., Maier R.J. Characterization of the NifU and NifS Fe-S cluster formation proteins essential for viability in Helicobacter pylori. Biochemistry 2000, 39:16213-16219.
    • (2000) Biochemistry , vol.39 , pp. 16213-16219
    • Olson, J.W.1    Agar, J.N.2    Johnson, M.K.3    Maier, R.J.4
  • 11
    • 84880288137 scopus 로고    scopus 로고
    • Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly
    • Prischi F., et al. Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat. Commun. 2010, 1:95.
    • (2010) Nat. Commun. , vol.1 , pp. 95
    • Prischi, F.1
  • 12
    • 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., Kiley P.J. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:9009-9014.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 13
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
    • Mihara H., Kurihara T., Yoshimura T., Esaki N. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J. Biochem. Tokyo 2000, 127:559-567.
    • (2000) J. Biochem. Tokyo , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 14
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • Cupp-Vickery J.R., Urbina H., Vickery L.E. Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J. Mol. Biol. 2003, 330:1049-1059.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 15
    • 77951749014 scopus 로고    scopus 로고
    • Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions
    • Shi R., et al. Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions. PLoS Biol. 2010, 8:e1000354.
    • (2010) PLoS Biol. , vol.8 , pp. e1000354
    • Shi, R.1
  • 16
    • 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., et al. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 2000, 39:7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1
  • 17
    • 0034911990 scopus 로고    scopus 로고
    • Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins
    • Tokumoto U., Takahashi Y. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. Tokyo 2001, 130:63-71.
    • (2001) J. Biochem. Tokyo , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 19
    • 52049096425 scopus 로고    scopus 로고
    • The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis
    • Shimomura Y., Wada K., Fukuyama K., Takahashi Y. The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis. J. Mol. Biol. 2008, 383:133-143.
    • (2008) J. Mol. Biol. , vol.383 , pp. 133-143
    • Shimomura, Y.1    Wada, K.2    Fukuyama, K.3    Takahashi, Y.4
  • 20
    • 84866513533 scopus 로고    scopus 로고
    • Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins
    • Shakamuri P., Zhang B., Johnson M.K. Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins. J. Am. Chem. Soc. 2012, 134:15213-15216.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15213-15216
    • Shakamuri, P.1    Zhang, B.2    Johnson, M.K.3
  • 21
    • 34250187112 scopus 로고    scopus 로고
    • In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein
    • Unciuleac M.C., et al. In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry 2007, 46:6812-6821.
    • (2007) Biochemistry , vol.46 , pp. 6812-6821
    • Unciuleac, M.C.1
  • 22
    • 0037077310 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis
    • Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein.
    • Mansy S.S., Wu G., Surerus K.K., Cowan J.A. Iron-sulfur cluster biosynthesis. J. Biol. Chem. 2002, 277:21397-21404.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21397-21404
    • Mansy, S.S.1    Wu, G.2    Surerus, K.K.3    Cowan, J.A.4
  • 23
    • 7444266901 scopus 로고    scopus 로고
    • Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site
    • Ramelot T.A., et al. Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site. J. Mol. Biol. 2004, 344:567-583.
    • (2004) J. Mol. Biol. , vol.344 , pp. 567-583
    • Ramelot, T.A.1
  • 24
    • 67650033430 scopus 로고    scopus 로고
    • Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB
    • Kim J.H., et al. Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB. Biochemistry 2009, 48:6062-6071.
    • (2009) Biochemistry , vol.48 , pp. 6062-6071
    • Kim, J.H.1
  • 25
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
    • Huynen M.A., Snel B., Bork P., Gibson T.J. The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Hum. Mol. Genet. 2001, 10:2463-2468.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 26
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H., et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 2001, 27:181-186.
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1
  • 27
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff U., Richhardt N., Ristow M., Kispal G., Lill R. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 2002, 11:2025-2036.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 28
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • Rotig A., et al. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat. Genet. 1997, 17:215-217.
    • (1997) Nat. Genet. , vol.17 , pp. 215-217
    • Rotig, A.1
  • 29
    • 31344438920 scopus 로고    scopus 로고
    • Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo
    • Vivas E., Skovran E., Downs D.M. Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo. J. Bacteriol. 2006, 188:1175-1179.
    • (2006) J. Bacteriol. , vol.188 , pp. 1175-1179
    • Vivas, E.1    Skovran, E.2    Downs, D.M.3
  • 30
    • 0032797179 scopus 로고    scopus 로고
    • Knock-out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants
    • Li D.S., Ohshima K., Jiralerspong S., Bojanowski M.W., Pandolfo M. Knock-out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants. FEBS Lett. 1999, 456:13-16.
    • (1999) FEBS Lett. , vol.456 , pp. 13-16
    • Li, D.S.1    Ohshima, K.2    Jiralerspong, S.3    Bojanowski, M.W.4    Pandolfo, M.5
  • 31
    • 80052176407 scopus 로고    scopus 로고
    • The frataxin homologue Fra plays a key role in intracellular iron channeling in Bacillus subtilis
    • Albrecht A.G., et al. The frataxin homologue Fra plays a key role in intracellular iron channeling in Bacillus subtilis. Chembiochem 2011, 12:2052-2061.
    • (2011) Chembiochem , vol.12 , pp. 2052-2061
    • Albrecht, A.G.1
  • 32
    • 84896460464 scopus 로고    scopus 로고
    • Distinct roles of the Salmonella enterica serovar Typhimurium CyaY and YggX proteins in the biosynthesis and repair of iron-sulfur clusters
    • Velayudhan J., et al. Distinct roles of the Salmonella enterica serovar Typhimurium CyaY and YggX proteins in the biosynthesis and repair of iron-sulfur clusters. Infect. Immun. 2014, 82:1390-1401.
    • (2014) Infect. Immun. , vol.82 , pp. 1390-1401
    • Velayudhan, J.1
  • 33
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T., Cowan J.A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 2003, 125:6078-6084.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 34
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites
    • Nair M., et al. Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure 2004, 12:2037-2048.
    • (2004) Structure , vol.12 , pp. 2037-2048
    • Nair, M.1
  • 35
    • 33746883937 scopus 로고    scopus 로고
    • Monomeric yeast frataxin is an iron-binding protein
    • Cook J.D., et al. Monomeric yeast frataxin is an iron-binding protein. Biochemistry 2006, 45:7767-7777.
    • (2006) Biochemistry , vol.45 , pp. 7767-7777
    • Cook, J.D.1
  • 36
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites
    • Nair M., et al. Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Struct. Camb. 2004, 12:2037-2048.
    • (2004) Struct. Camb. , vol.12 , pp. 2037-2048
    • Nair, M.1
  • 37
    • 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., Fontecave M. 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. 2006, 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
  • 38
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O., et al. Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 2006, 15:467-479.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 467-479
    • Gakh, O.1
  • 39
    • 0033838364 scopus 로고    scopus 로고
    • Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia
    • Adamec J., et al. Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia. Am. J. Hum. Genet. 2000, 67:549-562.
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 549-562
    • Adamec, J.1
  • 40
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber J., Muhlenhoff U., Lill R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 2003, 4:906-911.
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 41
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • Aloria K., Schilke B., Andrew A., Craig E.A. Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo. EMBO Rep. 2004, 5:1096-1101.
    • (2004) EMBO Rep. , vol.5 , pp. 1096-1101
    • Aloria, K.1    Schilke, B.2    Andrew, A.3    Craig, E.A.4
  • 42
    • 78649644673 scopus 로고    scopus 로고
    • Normal and Friedreich ataxia cells express different isoforms of frataxin with complementary roles in iron-sulfur cluster assembly
    • Gakh O., et al. Normal and Friedreich ataxia cells express different isoforms of frataxin with complementary roles in iron-sulfur cluster assembly. J. Biol. Chem. 2010, 285:38486-38501.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38486-38501
    • Gakh, O.1
  • 43
    • 79551514731 scopus 로고    scopus 로고
    • Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
    • Schmucker S., et al. Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex. PLoS One 2011, 6:e16199.
    • (2011) PLoS One , vol.6 , pp. e16199
    • Schmucker, S.1
  • 44
    • 64049116040 scopus 로고    scopus 로고
    • Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
    • Adinolfi S., et al. Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nat. Struct. Mol. Biol. 2009, 16:390-396.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 390-396
    • Adinolfi, S.1
  • 45
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • Tsai C.L., Barondeau D.P. Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry 2010, 49:9132-9139.
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.L.1    Barondeau, D.P.2
  • 46
    • 0036559919 scopus 로고    scopus 로고
    • Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli
    • Tokumoto U., et al. Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. J. Biochem. Tokyo 2002, 131:713-719.
    • (2002) J. Biochem. Tokyo , vol.131 , pp. 713-719
    • Tokumoto, U.1
  • 47
    • 23044446243 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters
    • Shimomura Y., Takahashi Y., Kakuta Y., Fukuyama K. Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters. Proteins 2005, 60:566-569.
    • (2005) Proteins , vol.60 , pp. 566-569
    • Shimomura, Y.1    Takahashi, Y.2    Kakuta, Y.3    Fukuyama, K.4
  • 48
    • 33646490975 scopus 로고    scopus 로고
    • YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein?
    • Pastore C., et al. YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein?. Structure 2006, 14:857-867.
    • (2006) Structure , vol.14 , pp. 857-867
    • Pastore, C.1
  • 50
    • 80052141882 scopus 로고    scopus 로고
    • Binding energetics of ferredoxin-NADP+ reductase with ferredoxin and its relation to function
    • Lee Y.H., et al. Binding energetics of ferredoxin-NADP+ reductase with ferredoxin and its relation to function. Chembiochem 2011, 12:2062-2070.
    • (2011) Chembiochem , vol.12 , pp. 2062-2070
    • Lee, Y.H.1
  • 51
    • 79958159813 scopus 로고    scopus 로고
    • Chloroplast-targeted ferredoxin-NADP(+) oxidoreductase (FNR): structure, function and location
    • Mulo P. Chloroplast-targeted ferredoxin-NADP(+) oxidoreductase (FNR): structure, function and location. Biochim. Biophys. Acta 2011, 1807:927-934.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 927-934
    • Mulo, P.1
  • 52
    • 0029781334 scopus 로고    scopus 로고
    • The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters
    • Staples C.R., et al. The function and properties of the iron-sulfur center in spinach ferredoxin: thioredoxin reductase: a new biological role for iron-sulfur clusters. Biochemistry 1996, 35:11425-11434.
    • (1996) Biochemistry , vol.35 , pp. 11425-11434
    • Staples, C.R.1
  • 54
    • 0035909064 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters
    • Kakuta Y., Horio T., Takahashi Y., Fukuyama K. Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters. Biochemistry 2001, 40:11007-11012.
    • (2001) Biochemistry , vol.40 , pp. 11007-11012
    • Kakuta, Y.1    Horio, T.2    Takahashi, Y.3    Fukuyama, K.4
  • 55
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange H., Kaut A., Kispal G., Lill R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:1050-1055.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 56
    • 34250192575 scopus 로고    scopus 로고
    • Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein
    • Chandramouli K., et al. Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein. Biochemistry 2007, 46:6804-6811.
    • (2007) Biochemistry , vol.46 , pp. 6804-6811
    • Chandramouli, K.1
  • 57
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • Ollagnier-de-Choudens S., Mattioli T., Takahashi Y., Fontecave M. Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 2001, 276:22604-22607.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22604-22607
    • Ollagnier-de-Choudens, S.1    Mattioli, T.2    Takahashi, Y.3    Fontecave, M.4
  • 58
    • 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., Vickery L.E. Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:7790-7795.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 59
    • 0035910560 scopus 로고    scopus 로고
    • The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
    • Silberg J.J., Hoff K.G., Tapley T.L., Vickery L.E. The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 2001, 276:1696-1700.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1696-1700
    • Silberg, J.J.1    Hoff, K.G.2    Tapley, T.L.3    Vickery, L.E.4
  • 60
    • 0141844533 scopus 로고    scopus 로고
    • Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
    • Hoff K.G., Cupp-Vickery J.R., Vickery L.E. Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. J. Biol. Chem. 2003, 278:37582-37589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37582-37589
    • Hoff, K.G.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 61
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery J.R., Peterson J.C., Ta D.T., Vickery L.E. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J. Mol. Biol. 2004, 342:1265-1278.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 62
    • 3142653172 scopus 로고    scopus 로고
    • Preferential substrate binding orientation by the molecular chaperone HscA
    • Tapley T.L., Vickery L.E. Preferential substrate binding orientation by the molecular chaperone HscA. J. Biol. Chem. 2004, 279:28435-28442.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28435-28442
    • Tapley, T.L.1    Vickery, L.E.2
  • 63
    • 51549120794 scopus 로고    scopus 로고
    • Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU
    • Fuzery A.K., et al. Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU. Biochemistry 2008, 47:9394-9404.
    • (2008) Biochemistry , vol.47 , pp. 9394-9404
    • Fuzery, A.K.1
  • 64
    • 15544365805 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis
    • Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity.
    • Wu S.P., Mansy S.S., Cowan J.A. Iron-sulfur cluster biosynthesis. Biochemistry 2005, 44:4284-4293.
    • (2005) Biochemistry , vol.44 , pp. 4284-4293
    • Wu, S.P.1    Mansy, S.S.2    Cowan, J.A.3
  • 65
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff U., Gerber J., Richhardt N., Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. Embo J. 2003, 22:4815-4825.
    • (2003) Embo J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 66
    • 33748782301 scopus 로고    scopus 로고
    • HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction
    • Chandramouli K., Johnson M.K. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 2006, 45:11087-11095.
    • (2006) Biochemistry , vol.45 , pp. 11087-11095
    • Chandramouli, K.1    Johnson, M.K.2
  • 67
    • 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., Barras F. Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet. 2009, 5:e1000497.
    • (2009) PLoS Genet. , vol.5 , pp. e1000497
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 68
    • 0346727446 scopus 로고    scopus 로고
    • Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold
    • Bilder P.W., Ding H., Newcomer M.E. Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry 2004, 43:133-139.
    • (2004) Biochemistry , vol.43 , pp. 133-139
    • Bilder, P.W.1    Ding, H.2    Newcomer, M.E.3
  • 69
    • 1842526422 scopus 로고    scopus 로고
    • Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli
    • Cupp-Vickery J.R., Silberg J.J., Ta D.T., Vickery L.E. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. J. Mol. Biol. 2004, 338:127-137.
    • (2004) J. Mol. Biol. , vol.338 , pp. 127-137
    • Cupp-Vickery, J.R.1    Silberg, J.J.2    Ta, D.T.3    Vickery, L.E.4
  • 70
    • 0035923420 scopus 로고    scopus 로고
    • IscA, an alternate scaffold for Fe-S cluster biosynthesis
    • Krebs C., et al. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry 2001, 40:14069-14080.
    • (2001) Biochemistry , vol.40 , pp. 14069-14080
    • Krebs, C.1
  • 71
    • 84867533021 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA
    • Mapolelo D.T., Zhang B., Naik S.G., Huynh B.H., Johnson M.K. Spectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA. Biochemistry 2012, 51:8071-8084.
    • (2012) Biochemistry , vol.51 , pp. 8071-8084
    • Mapolelo, D.T.1    Zhang, B.2    Naik, S.G.3    Huynh, B.H.4    Johnson, M.K.5
  • 72
    • 33745271510 scopus 로고    scopus 로고
    • The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold
    • Morimoto K., et al. The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold. J. Mol. Biol. 2006, 360:117-132.
    • (2006) J. Mol. Biol. , vol.360 , pp. 117-132
    • Morimoto, K.1
  • 73
    • 34447098988 scopus 로고    scopus 로고
    • The IscA from Acidithiobacillus ferrooxidans is an iron-sulfur protein which assemble the [Fe(4)S(4)] cluster with intracellular iron and sulfur
    • Zeng J., et al. The IscA from Acidithiobacillus ferrooxidans is an iron-sulfur protein which assemble the [Fe(4)S(4)] cluster with intracellular iron and sulfur. Arch. Biochem. Biophys. 2007, 463:237-244.
    • (2007) Arch. Biochem. Biophys. , vol.463 , pp. 237-244
    • Zeng, J.1
  • 74
    • 24044536614 scopus 로고    scopus 로고
    • Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU
    • Ding H., Harrison K., Lu J. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J. Biol. Chem. 2005, 280:30432-30437.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30432-30437
    • Ding, H.1    Harrison, K.2    Lu, J.3
  • 75
    • 2142654882 scopus 로고    scopus 로고
    • Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
    • Ding H., Clark R.J. Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem. J. 2004, 379:433-440.
    • (2004) Biochem. J. , vol.379 , pp. 433-440
    • Ding, H.1    Clark, R.J.2
  • 76
    • 84867499418 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of iron-bound forms of Azotobacter vinelandii (Nif)IscA
    • Mapolelo D.T., Zhang B., Naik S.G., Huynh B.H., Johnson M.K. Spectroscopic and functional characterization of iron-bound forms of Azotobacter vinelandii (Nif)IscA. Biochemistry 2012, 51:8056-8070.
    • (2012) Biochemistry , vol.51 , pp. 8056-8070
    • Mapolelo, D.T.1    Zhang, B.2    Naik, S.G.3    Huynh, B.H.4    Johnson, M.K.5
  • 77
    • 84876147476 scopus 로고    scopus 로고
    • Characterization of iron-sulfur cluster assembly protein IscA from Acidithiobacillus ferrooxidans
    • Qian L., Zheng C., Liu J. Characterization of iron-sulfur cluster assembly protein IscA from Acidithiobacillus ferrooxidans. Biochemistry (Mosc) 2013, 78:244-251.
    • (2013) Biochemistry (Mosc) , vol.78 , pp. 244-251
    • Qian, L.1    Zheng, C.2    Liu, J.3
  • 78
    • 78649847037 scopus 로고    scopus 로고
    • In vivo evidence for the iron-binding activity of an iron-sulfur cluster assembly protein IscA in Escherichia coli
    • Wang W., et al. In vivo evidence for the iron-binding activity of an iron-sulfur cluster assembly protein IscA in Escherichia coli. Biochem. J. 2010, 432:429-436.
    • (2010) Biochem. J. , vol.432 , pp. 429-436
    • Wang, W.1
  • 79
    • 80955125480 scopus 로고    scopus 로고
    • Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins
    • Muhlenhoff U., Richter N., Pines O., Pierik A.J., Lill R. Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins. J. Biol. Chem. 2011, 286:41205-41216.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41205-41216
    • Muhlenhoff, U.1    Richter, N.2    Pines, O.3    Pierik, A.J.4    Lill, R.5
  • 80
    • 38749100215 scopus 로고    scopus 로고
    • Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli
    • Lu J., Yang J., Tan G., Ding H. Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli. Biochem. J. 2008, 409:535-543.
    • (2008) Biochem. J. , vol.409 , pp. 535-543
    • Lu, J.1    Yang, J.2    Tan, G.3    Ding, H.4
  • 81
    • 84873673139 scopus 로고    scopus 로고
    • Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis
    • Landry A.P., Cheng Z., Ding H. Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis. Dalton Trans. 2013, 42:3100-3106.
    • (2013) Dalton Trans. , vol.42 , pp. 3100-3106
    • Landry, A.P.1    Cheng, Z.2    Ding, H.3
  • 82
    • 8644240051 scopus 로고    scopus 로고
    • SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly
    • Ollagnier-de-Choudens S., Sanakis Y., Fontecave M. SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly. J. Biol. Inorg. Chem. 2004, 9:828-838.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 828-838
    • Ollagnier-de-Choudens, S.1    Sanakis, Y.2    Fontecave, M.3
  • 83
    • 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., et al. ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:13626-13631.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 13626-13631
    • Loiseau, L.1
  • 84
    • 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., et al. 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. 2009, 131:6149-6153.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6149-6153
    • Gupta, V.1
  • 85
    • 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., Ding H. 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. 2009, 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
  • 86
    • 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., Sawers R.G. A-type carrier protein ErpA is essential for formation of an active formate-nitrate respiratory pathway in Escherichia coli K-12. J. Bacteriol. 2012, 194:346-353.
    • (2012) J. Bacteriol. , vol.194 , pp. 346-353
    • Pinske, C.1    Sawers, R.G.2
  • 87
    • 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., Sawers R.G. 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 2012, 7:e31755.
    • (2012) PLoS One , vol.7 , pp. e31755
    • Pinske, C.1    Sawers, R.G.2
  • 88
    • 84866876886 scopus 로고    scopus 로고
    • Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein
    • Zhang B., et al. Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:15734-15739.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15734-15739
    • Zhang, B.1
  • 89
    • 84930157010 scopus 로고    scopus 로고
    • Escherichia coli RIC is able to donate iron to iron-sulfur clusters
    • Nobre L.S., et al. Escherichia coli RIC is able to donate iron to iron-sulfur clusters. PLoS One 2014, 9:e95222.
    • (2014) PLoS One , vol.9 , pp. e95222
    • Nobre, L.S.1
  • 91
    • 84861856399 scopus 로고    scopus 로고
    • Characterization of the [2Fe-2S] cluster of Escherichia coli transcription factor IscR
    • Fleischhacker A.S., et al. Characterization of the [2Fe-2S] cluster of Escherichia coli transcription factor IscR. Biochemistry 2012, 51:4453-4462.
    • (2012) Biochemistry , vol.51 , pp. 4453-4462
    • Fleischhacker, A.S.1
  • 92
    • 84873058881 scopus 로고    scopus 로고
    • In vivo [Fe-S] cluster acquisition by IscR and NsrR, two stress regulators in Escherichia coli
    • Vinella D., Loiseau L., Ollagnier de Choudens S., Fontecave M., Barras F. In vivo [Fe-S] cluster acquisition by IscR and NsrR, two stress regulators in Escherichia coli. Mol. Microbiol. 2013, 87:493-508.
    • (2013) Mol. Microbiol. , vol.87 , pp. 493-508
    • Vinella, D.1    Loiseau, L.2    Ollagnier de Choudens, S.3    Fontecave, M.4    Barras, F.5
  • 93
    • 84878896186 scopus 로고    scopus 로고
    • Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity
    • Rajagopalan S., et al. Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat. Struct. Mol. Biol. 2013, 20:740-747.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 740-747
    • Rajagopalan, S.1
  • 94
    • 84873059613 scopus 로고    scopus 로고
    • Regulation of iron-sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe-2S]-IscR in Escherichia coli
    • Giel J.L., et al. Regulation of iron-sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe-2S]-IscR in Escherichia coli. Mol. Microbiol. 2013, 87:478-492.
    • (2013) Mol. Microbiol. , vol.87 , pp. 478-492
    • Giel, J.L.1
  • 95
    • 77955426294 scopus 로고    scopus 로고
    • Of the vulnerability of orphan complex proteins: the case study of the E. coli IscU and IscS proteins
    • Prischi F., et al. Of the vulnerability of orphan complex proteins: the case study of the E. coli IscU and IscS proteins. Protein Expr. Purif. 2010, 73:161-166.
    • (2010) Protein Expr. Purif. , vol.73 , pp. 161-166
    • Prischi, F.1
  • 96
    • 84880288137 scopus 로고    scopus 로고
    • Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly
    • Prischi F., et al. Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat. Commun. 2010, 1:95.
    • (2010) Nat. Commun. , vol.1 , pp. 95
    • Prischi, F.1
  • 97
    • 84861489997 scopus 로고    scopus 로고
    • (IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer
    • Marinoni E.N., et al. (IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer. Angew. Chem. Int. Ed. 2012, 51:5439-5442.
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 5439-5442
    • Marinoni, E.N.1
  • 98
    • 84873655381 scopus 로고    scopus 로고
    • Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus
    • Yamanaka Y., et al. Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus. Dalton Trans. 2013, 42:3092-3099.
    • (2013) Dalton Trans. , vol.42 , pp. 3092-3099
    • Yamanaka, Y.1
  • 99
    • 79960634008 scopus 로고    scopus 로고
    • The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein
    • e21992
    • Iannuzzi C., et al. The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein. PLoS One 2011, 6(e21992).
    • (2011) PLoS One , vol.6
    • Iannuzzi, C.1
  • 100
    • 84859178535 scopus 로고    scopus 로고
    • Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis
    • Bridwell-Rabb J., Iannuzzi C., Pastore A., Barondeau D.P. Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis. Biochemistry 2012, 51:2506-2514.
    • (2012) Biochemistry , vol.51 , pp. 2506-2514
    • Bridwell-Rabb, J.1    Iannuzzi, C.2    Pastore, A.3    Barondeau, D.P.4
  • 101
    • 84891379841 scopus 로고    scopus 로고
    • Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly
    • Pandey A., et al. Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly. J. Biol. Chem. 2013, 288:36773-36786.
    • (2013) J. Biol. Chem. , vol.288 , pp. 36773-36786
    • Pandey, A.1
  • 102
    • 84872552094 scopus 로고    scopus 로고
    • Mammalian frataxin controls sulfur production and iron entry during de novo Fe4S4 cluster assembly
    • Colin F., et al. Mammalian frataxin controls sulfur production and iron entry during de novo Fe4S4 cluster assembly. J. Am. Chem. Soc. 2013, 135:733-740.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 733-740
    • Colin, F.1
  • 103
    • 64049116040 scopus 로고    scopus 로고
    • Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
    • Adinolfi S., et al. Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nat. Struct. Mol. Biol. 2009, 16:390-396.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 390-396
    • Adinolfi, S.1
  • 104
    • 84878638881 scopus 로고    scopus 로고
    • [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin
    • Kim J.H., Frederick R.O., Reinen N.M., Troupis A.T., Markley J.L. [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin. J. Am. Chem. Soc. 2013, 135:8117-8120.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8117-8120
    • Kim, J.H.1    Frederick, R.O.2    Reinen, N.M.3    Troupis, A.T.4    Markley, J.L.5
  • 105
    • 84883178528 scopus 로고    scopus 로고
    • Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS
    • Yan R., et al. Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS. J. Biol. Chem. 2013, 288:24777-24787.
    • (2013) J. Biol. Chem. , vol.288 , pp. 24777-24787
    • Yan, R.1
  • 106
    • 0035823859 scopus 로고    scopus 로고
    • Sulfur transfer from IscS to IscU: the first step in iron-sulfur cluster biosynthesis
    • Smith A.D., et al. Sulfur transfer from IscS to IscU: the first step in iron-sulfur cluster biosynthesis. J. Am. Chem. Soc. 2001, 123:11103-11104.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11103-11104
    • Smith, A.D.1
  • 107
    • 84866139470 scopus 로고    scopus 로고
    • Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
    • Kim J.H., Tonelli M., Frederick R.O., Chow D.C., Markley J.L. Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU). J. Biol. Chem. 2012, 287:31406-31413.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31406-31413
    • Kim, J.H.1    Tonelli, M.2    Frederick, R.O.3    Chow, D.C.4    Markley, J.L.5
  • 108
    • 80155203873 scopus 로고    scopus 로고
    • Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange
    • Bonomi F., Iametti S., Morleo A., Ta D., Vickery L.E. Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange. Biochemistry 2011, 50:9641-9650.
    • (2011) Biochemistry , vol.50 , pp. 9641-9650
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 109
    • 57049159293 scopus 로고    scopus 로고
    • Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones
    • Bonomi F., Iametti S., Morleo A., Ta D., Vickery L.E. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Biochemistry 2008, 47:12795-12801.
    • (2008) Biochemistry , vol.47 , pp. 12795-12801
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 110
    • 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., et al. NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions. J. Biol. Chem. 2008.
    • (2008) J. Biol. Chem.
    • Angelini, S.1
  • 111
    • 84872956374 scopus 로고    scopus 로고
    • Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity
    • Roche B., et al. Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity. Biochim. Biophys. Acta 2013, 1827:455-469.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 455-469
    • Roche, B.1
  • 112
    • 3042641171 scopus 로고    scopus 로고
    • Evolution and cellular function of monothiol glutaredoxins: involvement in iron-sulphur cluster assembly
    • Vilella F., et al. Evolution and cellular function of monothiol glutaredoxins: involvement in iron-sulphur cluster assembly. Comp. Funct. Genom. 2004, 5:328-341.
    • (2004) Comp. Funct. Genom. , vol.5 , pp. 328-341
    • Vilella, F.1
  • 113
    • 76349122676 scopus 로고    scopus 로고
    • Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast
    • Kim K.D., Chung W.H., Kim H.J., Lee K.C., Roe J.H. Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast. Biochem. Biophys. Res. Commun. 2010, 392:467-472.
    • (2010) Biochem. Biophys. Res. Commun. , vol.392 , pp. 467-472
    • Kim, K.D.1    Chung, W.H.2    Kim, H.J.3    Lee, K.C.4    Roe, J.H.5
  • 114
    • 84873672762 scopus 로고    scopus 로고
    • Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking
    • Mapolelo D.T., et al. Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking. Dalton Trans. 2013, 42:3107-3115.
    • (2013) Dalton Trans. , vol.42 , pp. 3107-3115
    • Mapolelo, D.T.1
  • 115
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 2002, 13:1109-1121.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 116
    • 41949108097 scopus 로고    scopus 로고
    • Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters
    • Bandyopadhyay S., et al. Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters. Embo J. 2008, 27:1122-1133.
    • (2008) Embo J. , vol.27 , pp. 1122-1133
    • Bandyopadhyay, S.1
  • 117
    • 67650077717 scopus 로고    scopus 로고
    • Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin
    • Iwema T., et al. Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin. Biochemistry 2009, 48:6041-6043.
    • (2009) Biochemistry , vol.48 , pp. 6041-6043
    • Iwema, T.1
  • 118
    • 84899624154 scopus 로고    scopus 로고
    • [2Fe-2S] cluster transfer in iron-sulfur protein biogenesis
    • Banci L., et al. [2Fe-2S] cluster transfer in iron-sulfur protein biogenesis. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:6203-6208.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 6203-6208
    • Banci, L.1
  • 119
    • 84878839839 scopus 로고    scopus 로고
    • Levels of control exerted by the Isc iron-sulfur cluster system on biosynthesis of the formate hydrogenlyase complex
    • Pinske C., Jaroschinsky M., Sawers R.G. Levels of control exerted by the Isc iron-sulfur cluster system on biosynthesis of the formate hydrogenlyase complex. Microbiology 2013, 159:1179-1189.
    • (2013) Microbiology , vol.159 , pp. 1179-1189
    • Pinske, C.1    Jaroschinsky, M.2    Sawers, R.G.3
  • 120
    • 23644456197 scopus 로고    scopus 로고
    • Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU
    • Ding B., Smith E.S., Ding H. Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem. J. 2005, 389:797-802.
    • (2005) Biochem. J. , vol.389 , pp. 797-802
    • Ding, B.1    Smith, E.S.2    Ding, H.3


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