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Volumn 54, Issue 25, 2015, Pages 3880-3889

Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DICHROISM; IRON; MAMMALS; MOBILE SECURITY; MOLECULES; PROTEINS; REACTION INTERMEDIATES; SULFUR;

EID: 84933544557     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5014497     Document Type: Article
Times cited : (62)

References (57)
  • 1
    • 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. (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.4
  • 2
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill, R. (2009) Function and biogenesis of iron-sulphur proteins Nature 460, 831-838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 3
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault, T. A. and Tong, W.-H. (2008) Iron-sulfur cluster biogenesis and human disease Trends Genet. 24, 398-407
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.-H.2
  • 4
    • 69849113825 scopus 로고    scopus 로고
    • Analysis of iron-sulfur protein maturation in eukaryotes
    • Pierik, A. J., Netz, D. J. A., and Lill, R. (2009) Analysis of iron-sulfur protein maturation in eukaryotes Nat. Protoc. 4, 753-766
    • (2009) Nat. Protoc. , vol.4 , pp. 753-766
    • Pierik, A.J.1    Netz, D.J.A.2    Lill, R.3
  • 5
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
    • Lill, R. and Mühlenhoff, U. (2008) Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases Annu. Rev. Biochem. 77, 22.21-22.32
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 2221-2232
    • Lill, R.1    Mühlenhoff, U.2
  • 6
    • 61349203895 scopus 로고    scopus 로고
    • The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis
    • Sheftel, A. D. and Lill, R. (2009) The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis Ann. Med. 41, 82-99
    • (2009) Ann. Med. , vol.41 , pp. 82-99
    • Sheftel, A.D.1    Lill, R.2
  • 7
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill, R. and Mühlenhoff, U. (2006) Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms Annu. Rev. Cell Dev. Biol. 22, 457-486
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Mühlenhoff, U.2
  • 8
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures Science 277, 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 9
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of l -cysteine catalyzed by the nifS gene product
    • Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Mechanism for the desulfurization of l -cysteine catalyzed by the nifS gene product Biochemistry 33, 4714-4720
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 10
    • 72449186508 scopus 로고    scopus 로고
    • Kinetic Analysis of Cysteine Desulfurase CD0387 from Synechocystis sp PCC 6803: Formation of the Persulfide Intermediate
    • Behshad, E. and Bollinger, J. (2009) Kinetic Analysis of Cysteine Desulfurase CD0387 from Synechocystis sp PCC 6803: Formation of the Persulfide Intermediate Biochemistry 48, 12014-12023
    • (2009) Biochemistry , vol.48 , pp. 12014-12023
    • Behshad, E.1    Bollinger, J.2
  • 11
    • 4644301523 scopus 로고    scopus 로고
    • Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
    • Behshad, E., Parkin, S. E., and Bollinger, J. M. (2004) Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants Biochemistry 43, 12220-12226
    • (2004) Biochemistry , vol.43 , pp. 12220-12226
    • Behshad, E.1    Parkin, S.E.2    Bollinger, J.M.3
  • 12
    • 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., Martelli, A., Colin, F., Page, A., Wattenhofer-Donzé, M., Reutenauer, L., and Puccio, H. (2011) Mammalian Frataxin: An Essential Function for Cellular Viability through an Interaction with a Preformed ISCU/NFS1/ISD11 Iron-Sulfur Assembly Complex PLoS One 6, e16199
    • (2011) PLoS One , vol.6
    • Schmucker, S.1    Martelli, A.2    Colin, F.3    Page, A.4    Wattenhofer-Donzé, M.5    Reutenauer, L.6    Puccio, H.7
  • 14
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam, A. C., Bornhovd, C., Prokisch, H., Neupert, W., and Hell, K. (2006) The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria EMBO J. 25, 174-183
    • (2006) EMBO J. , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhovd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 15
    • 80055094199 scopus 로고    scopus 로고
    • Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein
    • Pandey, A., Yoon, H., Lyver, E. R., Dancis, A., and Pain, D. (2011) Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein J. Biol. Chem. 286, 38242-38252
    • (2011) J. Biol. Chem. , vol.286 , pp. 38242-38252
    • Pandey, A.1    Yoon, H.2    Lyver, E.R.3    Dancis, A.4    Pain, D.5
  • 16
    • 84855766784 scopus 로고    scopus 로고
    • Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis
    • Shi, Y., Ghosh, M., Kovtunovych, G., Crooks, D. R., and Rouault, T. A. (2012) Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis Biochim. Biophys. Acta 1823, 484-492
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 484-492
    • Shi, Y.1    Ghosh, M.2    Kovtunovych, G.3    Crooks, D.R.4    Rouault, T.A.5
  • 19
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • Uzarska, M. A., Dutkiewicz, R., Freibert, S. A., Lill, R., and Muehlenhoff, U. (2013) The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation Mol. Biol. Cell 24, 1830-1841
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1830-1841
    • Uzarska, M.A.1    Dutkiewicz, R.2    Freibert, S.A.3    Lill, R.4    Muehlenhoff, U.5
  • 20
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L. and Cupp-Vickery, J. (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.1    Cupp-Vickery, J.2
  • 21
    • 33748782301 scopus 로고    scopus 로고
    • HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction
    • Chandramouli, K. and Johnson, M. (2006) HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction Biochemistry 45, 11087-11095
    • (2006) Biochemistry , vol.45 , pp. 11087-11095
    • Chandramouli, K.1    Johnson, M.2
  • 23
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • Tsai, C. L. and Barondeau, D. P. (2010) Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex Biochemistry 49, 9132-9139
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.L.1    Barondeau, D.P.2
  • 24
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau, A.-L., O'Neill, H. A., Kennedy, M. C., Ikeda-Saito, M., Isaya, G., and Szweda, L. I. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity Science 305, 242-245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.-L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 25
    • 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. and Cowan, J. A. (2003) 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. 125, 6078-6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 26
    • 46049102185 scopus 로고    scopus 로고
    • Drosophila Frataxin: An Iron Chaperone during Cellular Fe-S Cluster Bioassembly
    • Kondapalli, K., Kok, N., Dancis, A., and Stemmler, T. L. (2008) Drosophila Frataxin: An Iron Chaperone during Cellular Fe-S Cluster Bioassembly Biochemistry 47, 6917-6927
    • (2008) Biochemistry , vol.47 , pp. 6917-6927
    • Kondapalli, K.1    Kok, N.2    Dancis, A.3    Stemmler, T.L.4
  • 27
    • 84864805076 scopus 로고    scopus 로고
    • Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria
    • Pandey, A., Yoon, H., Lyver, E. R., Dancis, A., and Pain, D. (2012) Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria Mitochondrion 12, 539-549
    • (2012) Mitochondrion , vol.12 , pp. 539-549
    • Pandey, A.1    Yoon, H.2    Lyver, E.R.3    Dancis, A.4    Pain, D.5
  • 28
    • 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., Gordon, D. M., Pain, J., Stemmler, T. L., Dancis, A., and Pain, D. (2013) 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. 288, 36773-36786
    • (2013) J. Biol. Chem. , vol.288 , pp. 36773-36786
    • Pandey, A.1    Gordon, D.M.2    Pain, J.3    Stemmler, T.L.4    Dancis, A.5    Pain, D.6
  • 29
    • 84905674436 scopus 로고    scopus 로고
    • Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry
    • Bridwell-Rabb, J., Fox, N. G., Tsai, C. L., Winn, A. M., and Barondeau, D. P. (2014) Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry Biochemistry 53, 4904-4913
    • (2014) Biochemistry , vol.53 , pp. 4904-4913
    • Bridwell-Rabb, J.1    Fox, N.G.2    Tsai, C.L.3    Winn, A.M.4    Barondeau, D.P.5
  • 30
    • 79960531239 scopus 로고    scopus 로고
    • Friedreich's Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron-Sulfur Cluster Assembly Complex
    • Tsai, C. L., Bridwell-Rabb, J., and Barondeau, D. P. (2011) Friedreich's Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron-Sulfur Cluster Assembly Complex Biochemistry 50, 6478-6487
    • (2011) Biochemistry , vol.50 , pp. 6478-6487
    • Tsai, C.L.1    Bridwell-Rabb, J.2    Barondeau, D.P.3
  • 31
    • 80051779168 scopus 로고    scopus 로고
    • Structure-function analysis of Friedreich's ataxia mutants reveals determinants for frataxin binding and activation of the Fe-S assembly complex
    • Bridwell-Rabb, J., Winn, A. M., and Barondeau, D. P. (2011) Structure-function analysis of Friedreich's ataxia mutants reveals determinants for frataxin binding and activation of the Fe-S assembly complex Biochemistry 50, 7265-7274
    • (2011) Biochemistry , vol.50 , pp. 7265-7274
    • Bridwell-Rabb, J.1    Winn, A.M.2    Barondeau, D.P.3
  • 33
    • 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., Krebs, C., Frazzon, J., Huynh, B. H., Dean, D. R., and Johnson, M. (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.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.6
  • 34
    • 80955125480 scopus 로고    scopus 로고
    • Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins
    • Mühlenhoff, U., Richter, N., Pines, O., Pierik, A. J., and Lill, R. (2011) Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins J. Biol. Chem. 286, 41205-41216
    • (2011) J. Biol. Chem. , vol.286 , pp. 41205-41216
    • Mühlenhoff, U.1    Richter, N.2    Pines, O.3    Pierik, A.J.4    Lill, R.5
  • 36
    • 84862965275 scopus 로고    scopus 로고
    • Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
    • Kim, J. H., Tonelli, M., and Markley, J. L. (2012) Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Proc. Natl. Acad. Sci. U.S.A. 109, 454-459
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 454-459
    • Kim, J.H.1    Tonelli, M.2    Markley, J.L.3
  • 37
    • 65949090751 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Role of a semi-conserved histidine
    • Huang, J. and Cowan, J. A. (2009) Iron-sulfur cluster biosynthesis: Role of a semi-conserved histidine Chem. Commun. 21, 3071-3073
    • (2009) Chem. Commun. , vol.21 , pp. 3071-3073
    • Huang, J.1    Cowan, J.A.2
  • 38
    • 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., and Barondeau, D. P. (2012) Effector role reversal during evolution: The case of frataxin in Fe-S cluster biosynthesis Biochemistry 51, 2506-2514
    • (2012) Biochemistry , vol.51 , pp. 2506-2514
    • Bridwell-Rabb, J.1    Iannuzzi, C.2    Pastore, A.3    Barondeau, D.P.4
  • 39
    • 0029770685 scopus 로고    scopus 로고
    • Human ferredoxin: Overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants
    • Xia, B., Cheng, H., Bandarian, V., Reed, G. H., and Markley, J. L. (1996) Human ferredoxin: Overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants Biochemistry 35, 9488-9495
    • (1996) Biochemistry , vol.35 , pp. 9488-9495
    • Xia, B.1    Cheng, H.2    Bandarian, V.3    Reed, G.H.4    Markley, J.L.5
  • 40
    • 0021765424 scopus 로고
    • Enzymic synthesis of the iron-sulfur cluster of spinach ferredoxin
    • Pagani, S., Bonomi, F., and Cerletti, P. (1984) Enzymic synthesis of the iron-sulfur cluster of spinach ferredoxin Eur. J. Biochem. 142, 361-366
    • (1984) Eur. J. Biochem. , vol.142 , pp. 361-366
    • Pagani, S.1    Bonomi, F.2    Cerletti, P.3
  • 41
    • 54449085541 scopus 로고    scopus 로고
    • A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
    • Marelja, Z., Stöcklein, W., Nimtz, M., and Leimkühler, S. (2008) A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis J. Biol. Chem. 283, 25178-25185
    • (2008) J. Biol. Chem. , vol.283 , pp. 25178-25185
    • Marelja, Z.1    Stöcklein, W.2    Nimtz, M.3    Leimkühler, S.4
  • 42
    • 0000904065 scopus 로고
    • A direct microdetermination for sulfide
    • Siegel, L. M. (1965) A direct microdetermination for sulfide Anal. Biochem. 11, 126-132
    • (1965) Anal. Biochem. , vol.11 , pp. 126-132
    • Siegel, L.M.1
  • 43
    • 0023899855 scopus 로고
    • Rapid Colorimetric Micromethod for the Quantitation of Complexed Iron in Biological Samples
    • Fish, W. W. (1988) Rapid Colorimetric Micromethod for the Quantitation of Complexed Iron in Biological Samples Methods Enzymol. 158, 357-364
    • (1988) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 44
    • 33847670407 scopus 로고
    • Ferrozine: A new spectrophotmetric reagent for iron
    • Stookey, L. (1970) Ferrozine: A new spectrophotmetric reagent for iron Anal. Chem. 42, 779-781
    • (1970) Anal. Chem. , vol.42 , pp. 779-781
    • Stookey, L.1
  • 45
    • 0027174668 scopus 로고
    • A comparison of bathophenanthrolinedisulfonic acid and ferrozine as chelators of iron(II) in reduction reactions
    • Cowart, R. E., Singleton, F. L., and Hind, J. S. (1993) A comparison of bathophenanthrolinedisulfonic acid and ferrozine as chelators of iron(II) in reduction reactions Anal. Biochem. 211, 151-155
    • (1993) Anal. Biochem. , vol.211 , pp. 151-155
    • Cowart, R.E.1    Singleton, F.L.2    Hind, J.S.3
  • 46
    • 84884852556 scopus 로고    scopus 로고
    • Arabidopsis thaliana Nfu2 Accommodates [2Fe-2S] or [4Fe-4S] Clusters and Is Competent for in Vitro Maturation of Chloroplast [2Fe-2S] and [4Fe-4S] Cluster-Containing Proteins
    • Gao, H. Y., Subramanian, S., Couturier, J., Naik, S. G., Kim, S. K., Leustek, T., Knaff, D. B., Wu, H. C., Vignols, F., Huynh, B. H., Rouhier, N., and Johnson, M. K. (2013) Arabidopsis thaliana Nfu2 Accommodates [2Fe-2S] or [4Fe-4S] Clusters and Is Competent for in Vitro Maturation of Chloroplast [2Fe-2S] and [4Fe-4S] Cluster-Containing Proteins Biochemistry 52, 6633-6645
    • (2013) Biochemistry , vol.52 , pp. 6633-6645
    • Gao, H.Y.1    Subramanian, S.2    Couturier, J.3    Naik, S.G.4    Kim, S.K.5    Leustek, T.6    Knaff, D.B.7    Wu, H.C.8    Vignols, F.9    Huynh, B.H.10    Rouhier, N.11    Johnson, M.K.12
  • 47
    • 80155203873 scopus 로고    scopus 로고
    • Facilitated Transfer of IscU-[2Fe2S] Clusters by Chaperone-Mediated Ligand Exchange
    • Bonomi, F., Iametti, S., Morleo, A., Ta, D., and Vickery, L. E. (2011) Facilitated Transfer of IscU-[2Fe2S] Clusters by Chaperone-Mediated Ligand Exchange Biochemistry 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
  • 48
    • 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., and Cowan, J. A. (2002) Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein J. Biol. Chem. 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
  • 49
    • 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., and Johnson, M. K. (2012) Spectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA Biochemistry 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
  • 50
    • 0030019087 scopus 로고    scopus 로고
    • Circular dichroism and X-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form
    • Ryle, M. J., Lanzilotta, W. N., Seefeldt, L. C., Scarrow, R. C., and Jensen, G. M. (1996) Circular dichroism and X-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form J. Biol. Chem. 271, 1551-1557
    • (1996) J. Biol. Chem. , vol.271 , pp. 1551-1557
    • Ryle, M.J.1    Lanzilotta, W.N.2    Seefeldt, L.C.3    Scarrow, R.C.4    Jensen, G.M.5
  • 51
    • 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
  • 53
    • 1842451306 scopus 로고
    • Mössbauer studies of iron sulphide minerals
    • Garg, V. K. (1980) Mössbauer studies of iron sulphide minerals Rev. Bras. Fis. 10, 535-558
    • (1980) Rev. Bras. Fis. , vol.10 , pp. 535-558
    • Garg, V.K.1
  • 54
    • 84979160994 scopus 로고    scopus 로고
    • The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology
    • Rouault, T. A. Ed. Walter de Gruyter, Berlin
    • Chakrabarti, M. and Lindahl, P. A. (2014) The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology. In Iron Sulfur Clusters in Chemistry and Biology (Rouault, T. A., Ed.) pp 49-75, Walter de Gruyter, Berlin.
    • (2014) Iron Sulfur Clusters in Chemistry and Biology , pp. 49-75
    • Chakrabarti, M.1    Lindahl, P.A.2
  • 55
    • 84866996636 scopus 로고    scopus 로고
    • RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins
    • Lanz, N. D., Grove, T. L., Gogonea, C. B., Lee, K. H., Krebs, C., and Booker, S. J. (2012) RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins Methods Enzymol. 516, 125-152
    • (2012) Methods Enzymol. , vol.516 , pp. 125-152
    • Lanz, N.D.1    Grove, T.L.2    Gogonea, C.B.3    Lee, K.H.4    Krebs, C.5    Booker, S.J.6
  • 57
    • 84921033132 scopus 로고    scopus 로고
    • Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways
    • Vranish, J. N., Russell, W. K., Yu, L. E., Cox, R. M., Russell, D. H., and Barondeau, D. P. (2015) Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways J. Am. Chem. Soc. 137, 390-398
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 390-398
    • Vranish, J.N.1    Russell, W.K.2    Yu, L.E.3    Cox, R.M.4    Russell, D.H.5    Barondeau, D.P.6


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