메뉴 건너뛰기




Volumn 95, Issue 4, 2015, Pages 605-623

The iron-binding CyaY and IscX proteins assist the ISC-catalyzed Fe-S biogenesis in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE; IRON; IRON BINDING PROTEIN; PROTEIN CYAY; PROTEIN ISCX; SULFUR; UNCLASSIFIED DRUG; CYAY PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; IRON SULFUR PROTEIN; ISCX PROTEIN, E COLI;

EID: 84922626000     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12888     Document Type: Article
Times cited : (38)

References (83)
  • 1
    • 0033025239 scopus 로고    scopus 로고
    • Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient
    • Abdul-Tehrani, H., Hudson, A.J., Chang, Y.S., Timms, A.R., Hawkins, C., Williams, J.M., etal. (1999) Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J Bacteriol 181: 1415-1428.
    • (1999) J Bacteriol , vol.181 , pp. 1415-1428
    • Abdul-Tehrani, H.1    Hudson, A.J.2    Chang, Y.S.3    Timms, A.R.4    Hawkins, C.5    Williams, J.M.6
  • 2
    • 0036667986 scopus 로고    scopus 로고
    • A structural approach to understanding the iron-binding properties of phylogenetically different frataxins
    • Adinolfi, S., Trifuoggi, M., Politou, A.S., Martin, S., and Pastore, A. (2002) A structural approach to understanding the iron-binding properties of phylogenetically different frataxins. Hum Mol Genet 11: 1865-1877.
    • (2002) Hum Mol Genet , vol.11 , pp. 1865-1877
    • Adinolfi, S.1    Trifuoggi, M.2    Politou, A.S.3    Martin, S.4    Pastore, A.5
  • 3
    • 64049116040 scopus 로고    scopus 로고
    • Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
    • Adinolfi, S., Iannuzzi, C., Prischi, F., Pastore, C., Iametti, S., Martin, S.R., etal. (2009) Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nat Struct Mol Biol 16: 390-396.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 390-396
    • Adinolfi, S.1    Iannuzzi, C.2    Prischi, F.3    Pastore, C.4    Iametti, S.5    Martin, S.R.6
  • 4
    • 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
  • 5
    • 33749638768 scopus 로고    scopus 로고
    • GAA repeat expansion mutation mouse models of Friedreich ataxia exhibit oxidative stress leading to progressive neuronal and cardiac pathology
    • Al-Mahdawi, S., Pinto, R.M., Varshney, D., Lawrence, L., Lowrie, M.B., Hughes, S., etal. (2006) GAA repeat expansion mutation mouse models of Friedreich ataxia exhibit oxidative stress leading to progressive neuronal and cardiac pathology. Genomics 88: 580-590.
    • (2006) Genomics , vol.88 , pp. 580-590
    • Al-Mahdawi, S.1    Pinto, R.M.2    Varshney, D.3    Lawrence, L.4    Lowrie, M.B.5    Hughes, S.6
  • 6
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the KEIO collection
    • 2006 0008
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the KEIO collection. Mol Syst Biol 2: 2006 0008; doi:10.1038/msb4100050.
    • (2006) Mol Syst Biol , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 7
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: the assembly of iron-sulfur clusters in plants
    • Balk, J., and Pilon, M. (2011) Ancient and essential: the assembly of iron-sulfur clusters in plants. Trends Plant Sci 16: 218-226.
    • (2011) Trends Plant Sci , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 8
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: ancient structures, still full of surprises
    • Beinert, H. (2000) Iron-sulfur proteins: ancient structures, still full of surprises. J Biol Inorg Chem 5: 2-15.
    • (2000) J Biol Inorg Chem , vol.5 , pp. 2-15
    • Beinert, H.1
  • 9
    • 3342981572 scopus 로고    scopus 로고
    • Iron binding and oxidation kinetics in frataxin CyaY of Escherichia coli
    • Bou-Abdallah, F., Adinolfi, S., Pastore, A., Laue, T.M., and Chasteen, N.D. (2004) Iron binding and oxidation kinetics in frataxin CyaY of Escherichia coli. J Mol Biol 341: 605-615.
    • (2004) J Mol Biol , vol.341 , pp. 605-615
    • Bou-Abdallah, F.1    Adinolfi, S.2    Pastore, A.3    Laue, T.M.4    Chasteen, N.D.5
  • 10
    • 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
  • 11
    • 13344270899 scopus 로고    scopus 로고
    • Freidreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano, V., Montermini, L., Molto, M.D., Pianese, L., Cossee, M., Cavalcanti, F., etal. (1996) Freidreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271: 1423-1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossee, M.5    Cavalcanti, F.6
  • 12
    • 70449455583 scopus 로고    scopus 로고
    • The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer
    • Chahal, H.K., Dai, Y., Saini, A., Ayala-Castro, C., and Outten, F.W. (2009) The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer. Biochemistry 48: 10644-10653.
    • (2009) Biochemistry , vol.48 , pp. 10644-10653
    • Chahal, H.K.1    Dai, Y.2    Saini, A.3    Ayala-Castro, C.4    Outten, F.W.5
  • 13
    • 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.K. (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.K.2
  • 15
    • 12944257432 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family
    • Cho, S.J., Lee, M.G., Yang, J.K., Lee, J.Y., Song, H.K., and Suh, S.W. (2000) Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family. Proc Natl Acad Sci USA 97: 8932-8937.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8932-8937
    • Cho, S.J.1    Lee, M.G.2    Yang, J.K.3    Lee, J.Y.4    Song, H.K.5    Suh, S.W.6
  • 17
    • 84874322079 scopus 로고    scopus 로고
    • The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis
    • Dahl, J.U., Radon, C., Bühning, M., Nimtz, M., Leichert, L.I., Denis, Y., etal. (2013) The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis. J Biol Chem 288: 5426-5442.
    • (2013) J Biol Chem , vol.288 , pp. 5426-5442
    • Dahl, J.U.1    Radon, C.2    Bühning, M.3    Nimtz, M.4    Leichert, L.I.5    Denis, Y.6
  • 18
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 19
    • 34247197625 scopus 로고    scopus 로고
    • Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions
    • Ding, H., Yang, J., Coleman, L.C., and Yeung, S. (2007) Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions. J Biol Chem 282: 7997-8004.
    • (2007) J Biol Chem , vol.282 , pp. 7997-8004
    • Ding, H.1    Yang, J.2    Coleman, L.C.3    Yeung, S.4
  • 20
    • 84879615674 scopus 로고    scopus 로고
    • Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway
    • Ezraty, B., Vergnes, A., Banzhaf, M., Duverger, Y., Huguenot, A., Brochado, A.R., etal. (2013) Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway. Science 340: 1583-1587.
    • (2013) Science , vol.340 , pp. 1583-1587
    • Ezraty, B.1    Vergnes, A.2    Banzhaf, M.3    Duverger, Y.4    Huguenot, A.5    Brochado, A.R.6
  • 21
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury, F. (1999) Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett 456: 281-284.
    • (1999) FEBS Lett , vol.456 , pp. 281-284
    • Foury, F.1
  • 22
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast frataxin homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury, F., and Cazzalini, O. (1997) Deletion of the yeast frataxin homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett 411: 373-377.
    • (1997) FEBS Lett , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 23
    • 0030296878 scopus 로고    scopus 로고
    • Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction
    • Gibson, T.J., Koonin, E.V., Musco, G., Pastore, A., and Bork, P. (1996) Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction. Trends Neurosci 19: 465-468.
    • (1996) Trends Neurosci , vol.19 , pp. 465-468
    • Gibson, T.J.1    Koonin, E.V.2    Musco, G.3    Pastore, A.4    Bork, P.5
  • 24
    • 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., Nesbit, A.D., Mettert, E.L., Fleischhacker, A.S., Wanta, B.T., and Kiley, P.J. (2013) Regulation of iron-sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe-2S]-IscR in Escherichia coli. Mol Microbiol 87: 478-492.
    • (2013) Mol Microbiol , vol.87 , pp. 478-492
    • Giel, J.L.1    Nesbit, A.D.2    Mettert, E.L.3    Fleischhacker, A.S.4    Wanta, B.T.5    Kiley, P.J.6
  • 25
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoteur
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoteur. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 26
    • 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., and Gibson, T.J. (2001) The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Hum Mol Genet 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
  • 27
    • 79960634008 scopus 로고    scopus 로고
    • The role of CyaY in iron-sulfur cluster assembly on the E.coli IscU scaffold protein
    • Iannuzzi, C., Adinolfi, S., Howes, B.D., Garcia-Serres, R., Cemancey, M., Latour, J.M., etal. (2011) The role of CyaY in iron-sulfur cluster assembly on the E.coli IscU scaffold protein. PLoS ONE 6: e21992.
    • (2011) PLoS ONE , vol.6 , pp. e21992
    • Iannuzzi, C.1    Adinolfi, S.2    Howes, B.D.3    Garcia-Serres, R.4    Cemancey, M.5    Latour, J.M.6
  • 28
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi, Y., Shigi, N., Kato, J., Nishimura, A., and Suzuki, T. (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell 21: 97-108.
    • (2006) Mol Cell , vol.21 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 29
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang, S., and Imlay, J.A. (2010) Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol Microbiol 78: 1448-1467.
    • (2010) Mol Microbiol , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 30
    • 13244289800 scopus 로고    scopus 로고
    • Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function
    • Kang, Y., Weber, K.D., Qiu, Y., Kiley, P.J., and Blattner, F.R. (2005) Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function. J Bacteriol 187: 1135-1160.
    • (2005) J Bacteriol , vol.187 , pp. 1135-1160
    • Kang, Y.1    Weber, K.D.2    Qiu, Y.3    Kiley, P.J.4    Blattner, F.R.5
  • 31
    • 33750083296 scopus 로고    scopus 로고
    • Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
    • Kessler, D. (2006) Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol Rev 30: 825-840.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 825-840
    • Kessler, D.1
  • 32
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K., and Imlay, J.A. (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93: 13635-13640.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 33
    • 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., and Markley, J.L. (2013) [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 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
  • 34
    • 84901940422 scopus 로고    scopus 로고
    • Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli
    • Kim, J.H., Bothe, J.R., Frederick, R.O., Holder, J.C., and Markley, J.L. (2014) Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli. J Am Chem Soc 136: 7933-7942.
    • (2014) J Am Chem Soc , vol.136 , pp. 7933-7942
    • Kim, J.H.1    Bothe, J.R.2    Frederick, R.O.3    Holder, J.C.4    Markley, J.L.5
  • 35
    • 78249254576 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of succinate: quinone reductase from Thermus thermophilus
    • Kolaj-Robin, O., O'Kane, S.R., Nitschke, W., Léger, C., Baymann, F., and Soulimane, T. (2011) Biochemical and biophysical characterization of succinate: quinone reductase from Thermus thermophilus. Biochim Biophys Acta 1807: 68-79.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 68-79
    • Kolaj-Robin, O.1    O'Kane, S.R.2    Nitschke, W.3    Léger, C.4    Baymann, F.5    Soulimane, T.6
  • 36
    • 33745217828 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis; characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
    • Layer, G., Ollagnier de Choudens, S., Sanakis, Y., and Fontecave, M. (2006) Iron-sulfur cluster biosynthesis; characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J Biol Chem 281: 16256-16263.
    • (2006) J Biol Chem , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier de Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 37
    • 1642565394 scopus 로고    scopus 로고
    • Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor
    • Lee, J.H., Yeo, W.S., and Roe, J.H. (2004) Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor. Mol Microbiol 51: 1745-1755.
    • (2004) Mol Microbiol , vol.51 , pp. 1745-1755
    • Lee, J.H.1    Yeo, W.S.2    Roe, J.H.3
  • 38
    • 57349087129 scopus 로고    scopus 로고
    • Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli
    • Lee, K.C., Yeo, W.S., and Roe, J.H. (2008) Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli. J Bacteriol 190: 8244-8247.
    • (2008) J Bacteriol , vol.190 , pp. 8244-8247
    • Lee, K.C.1    Yeo, W.S.2    Roe, J.H.3
  • 39
    • 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., and Pandolfo, M. (1999) Knock-out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants. FEBS Lett 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
  • 40
    • 84864296714 scopus 로고    scopus 로고
    • The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
    • Lill, R., Hoffmann, B., Molik, S., Pierik, A.J., Rietzschel, N., Stehling, O., etal. (2012) The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim Biophys Acta 1823: 1491-14508.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 1491-14508
    • Lill, R.1    Hoffmann, B.2    Molik, S.3    Pierik, A.J.4    Rietzschel, N.5    Stehling, O.6
  • 41
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier de Choudens, S., Nachin, L., Fontecave, M., and Barras, F. (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278: 38352-38359.
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier de Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 42
    • 84874644140 scopus 로고    scopus 로고
    • The rotavirus nonstructural protein NSP5 coordinates a [2Fe-2S] iron-sulfur cluster that modulates interaction to RNA
    • Martin, D., Charpilienne, A., Parent, A., Boussac, A., D'Autreaux, B., Poupon, J., and Poncet, D. (2013) The rotavirus nonstructural protein NSP5 coordinates a [2Fe-2S] iron-sulfur cluster that modulates interaction to RNA. FASEB J 27: 1074-1083.
    • (2013) FASEB J , vol.27 , pp. 1074-1083
    • Martin, D.1    Charpilienne, A.2    Parent, A.3    Boussac, A.4    D'Autreaux, B.5    Poupon, J.6    Poncet, D.7
  • 43
    • 77957376210 scopus 로고    scopus 로고
    • A forward-genetic screen and dynamic analysis of lambda phage host-dependencies reveals an extensive interaction network and a new anti-viral strategy
    • Maynard, N.D., Birch, E.W., Sanghvi, J.C., Chen, L., Gutschow, M.V., and Covert, M.W. (2010) A forward-genetic screen and dynamic analysis of lambda phage host-dependencies reveals an extensive interaction network and a new anti-viral strategy. PLoS Genet 6: e1001017.
    • (2010) PLoS Genet , vol.6 , pp. e1001017
    • Maynard, N.D.1    Birch, E.W.2    Sanghvi, J.C.3    Chen, L.4    Gutschow, M.V.5    Covert, M.W.6
  • 44
    • 84856604776 scopus 로고    scopus 로고
    • Competing pathways control host resistance to virus via tRNA modification and programmed ribosomal frameshifting
    • Maynard, N.D., Macklin, D.N., Kirkegaard, K., and Covert, M.W. (2012) Competing pathways control host resistance to virus via tRNA modification and programmed ribosomal frameshifting. Mol Syst Biol 8: 567; doi:10.1038/msb.2011.101.
    • (2012) Mol Syst Biol , vol.8 , pp. 567
    • Maynard, N.D.1    Macklin, D.N.2    Kirkegaard, K.3    Covert, M.W.4
  • 45
    • 56249090364 scopus 로고    scopus 로고
    • The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR
    • Mettert, E.L., Outten, F.W., Wanta, B., and Kiley, P.J. (2008) The impact of O(2) on the Fe-S cluster biogenesis requirements of Escherichia coli FNR. J Mol Biol 384: 798-811.
    • (2008) J Mol Biol , vol.384 , pp. 798-811
    • Mettert, E.L.1    Outten, F.W.2    Wanta, B.3    Kiley, P.J.4
  • 46
    • 0003785155 scopus 로고
    • New York: Cold Spring Harbor Laboratory Press. Cold Spring Harbor.
    • Miller, J.H. (1972) Experiments in Molecular Genetics. New York: Cold Spring Harbor Laboratory Press. Cold Spring Harbor.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 47
    • 7944225865 scopus 로고    scopus 로고
    • Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites
    • Nair, M., Adinolfi, S., Pastore, C., Kelly, G., Temussi, P., and Pastore, A. (2004) Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure 12: 2037-2048.
    • (2004) Structure , vol.12 , pp. 2037-2048
    • Nair, M.1    Adinolfi, S.2    Pastore, C.3    Kelly, G.4    Temussi, P.5    Pastore, A.6
  • 48
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten, F.W., Wood, M.J., Munoz, F.M., and Storz, G. (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278: 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 49
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F.W., Djaman, O., and Storz, G. (2004) A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52: 861-872.
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 50
    • 84880346984 scopus 로고    scopus 로고
    • Frataxin: a protein in search for a function
    • Pastore, A., and Puccio, H. (2013) Frataxin: a protein in search for a function. J Neurochem 1: 43-52.
    • (2013) J Neurochem , vol.1 , pp. 43-52
    • Pastore, A.1    Puccio, H.2
  • 51
    • 33646490975 scopus 로고    scopus 로고
    • YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein?
    • Pastore, C., Adinolfi, S., Huynen, M.A., Rybin, V., Martin, S., Mayer, M., etal. (2006) YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? Structure 14: 857-867.
    • (2006) Structure , vol.14 , pp. 857-867
    • Pastore, C.1    Adinolfi, S.2    Huynen, M.A.3    Rybin, V.4    Martin, S.5    Mayer, M.6
  • 52
    • 34547760795 scopus 로고    scopus 로고
    • Understanding the binding properties of an unusual metal-binding protein, a study of bacterial frataxin
    • Pastore, C., Franzese, M., Sica, F., Temussi, P., and Pastore, A. (2007) Understanding the binding properties of an unusual metal-binding protein, a study of bacterial frataxin. FEBS J 274: 4199-4210.
    • (2007) FEBS J , vol.274 , pp. 4199-4210
    • Pastore, C.1    Franzese, M.2    Sica, F.3    Temussi, P.4    Pastore, A.5
  • 53
    • 34548363856 scopus 로고    scopus 로고
    • Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH: ubiquinone oxidoreductase
    • Pohl, T., Walter, J., Stolpe, S., Soufo, J.H., Grauman, P.L., and Friedrich, T. (2007) Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH: ubiquinone oxidoreductase. BMC Biochem 8: 13.
    • (2007) BMC Biochem , vol.8 , pp. 13
    • Pohl, T.1    Walter, J.2    Stolpe, S.3    Soufo, J.H.4    Grauman, P.L.5    Friedrich, T.6
  • 54
    • 84880288137 scopus 로고    scopus 로고
    • Structural bases for the interaction of frataxin with the central components of iron-sulfur cluster assembly
    • Prischi, F., Konarev, P.V., Iannuzzi, C., Pastore, C., Adinolfi, S., Martin, S.R., etal. (2010) Structural bases for the interaction of frataxin with the central components of iron-sulfur cluster assembly. Nat Commun 1: 95; doi: 10.1038/ncomms1097.
    • (2010) Nat Commun , vol.1 , pp. 95
    • Prischi, F.1    Konarev, P.V.2    Iannuzzi, C.3    Pastore, C.4    Adinolfi, S.5    Martin, S.R.6
  • 55
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: bacterial strategies
    • Py, B., and Barras, F. (2010) Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 8: 436-446.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 56
    • 84867044598 scopus 로고    scopus 로고
    • Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier
    • Py, B., Gerez, C., Angelini, S., Planel, R., Vinella, D., Loiseau, L., etal. (2012) Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier. Mol Microbiol 86: 155-171.
    • (2012) Mol Microbiol , vol.86 , pp. 155-171
    • Py, B.1    Gerez, C.2    Angelini, S.3    Planel, R.4    Vinella, D.5    Loiseau, L.6
  • 57
    • 84878896186 scopus 로고    scopus 로고
    • Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity
    • Rajagopalan, S., Teter, S.J., Zwart, P.H., Brennan, R.G., Phillips, K.J., and Kiley, P.J. (2013) Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat Struct Mol Biol 20: 740-747.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 740-747
    • Rajagopalan, S.1    Teter, S.J.2    Zwart, P.H.3    Brennan, R.G.4    Phillips, K.J.5    Kiley, P.J.6
  • 59
    • 84884901489 scopus 로고    scopus 로고
    • Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity
    • Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., and Barras, F. (2013) Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity. Biochim Biophys Acta 1827: 923-937.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 923-937
    • Roche, B.1    Aussel, L.2    Ezraty, B.3    Mandin, P.4    Py, B.5    Barras, F.6
  • 60
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich's ataxia
    • Rötig, A., de Lonlay, P., Chretien, D., Foury, F., Koenig, M., Sidi, D., etal. (1997) Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich's ataxia. Nat Genet 17: 215-217.
    • (1997) Nat Genet , vol.17 , pp. 215-217
    • Rötig, A.1    de Lonlay, P.2    Chretien, D.3    Foury, F.4    Koenig, M.5    Sidi, D.6
  • 61
    • 78049288246 scopus 로고    scopus 로고
    • SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB
    • Saini, A., Mapolelo, D.T., Chahal, H.K., Johnson, M.K., and Outten, F.W. (2010) SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry 49: 9402-9412.
    • (2010) Biochemistry , vol.49 , pp. 9402-9412
    • Saini, A.1    Mapolelo, D.T.2    Chahal, H.K.3    Johnson, M.K.4    Outten, F.W.5
  • 62
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz, C.J., Djaman, O., Imlay, J.A., and Kiley, P.J. (2000) The cysteine desulfurase, IscS, has a major role in vivo Fe-S cluster formation in Escherichia coli. Proc Natl Acad Sci USA 97: 9009-9014.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 63
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C.J., Giel, J.L., Patschkowski, T., Luther, C., Ruzicka, F.J., Beinert, H., and Kiley, P.J. (2001) IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc Natl Acad Sci USA 98: 14895-14900.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 64
    • 10344238617 scopus 로고    scopus 로고
    • Are respiratory enzymes the primary sources of intracellular hydrogen peroxide ?
    • Seaver, L.C., and Imlay, J.A. (2004) Are respiratory enzymes the primary sources of intracellular hydrogen peroxide ? J Biol Chem 279: 48742-48750.
    • (2004) J Biol Chem , vol.279 , pp. 48742-48750
    • Seaver, L.C.1    Imlay, J.A.2
  • 65
    • 77951749014 scopus 로고    scopus 로고
    • Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions
    • Shi, R., Proteau, A., Villarroya, M., Moukadiri, I., Zhang, L., Trempe, J.F., etal. (2010) Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions. PLoS Biol 8: e1000354.
    • (2010) PLoS Biol , vol.8 , pp. e1000354
    • Shi, R.1    Proteau, A.2    Villarroya, M.3    Moukadiri, I.4    Zhang, L.5    Trempe, J.F.6
  • 66
    • 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., and Fukuyama, K. (2005) Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters. Proteins 60: 566-569.
    • (2005) Proteins , vol.60 , pp. 566-569
    • Shimomura, Y.1    Takahashi, Y.2    Kakuta, Y.3    Fukuyama, K.4
  • 67
    • 84879552436 scopus 로고    scopus 로고
    • Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster
    • Tam, W., Pell, L.G., Bona, D., Tsai, A., Dai, X.X., Edwards, A.M., etal. (2013) Tail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster. J Mol Biol 425: 2450-2462.
    • (2013) J Mol Biol , vol.425 , pp. 2450-2462
    • Tam, W.1    Pell, L.G.2    Bona, D.3    Tsai, A.4    Dai, X.X.5    Edwards, A.M.6
  • 68
    • 61449135987 scopus 로고    scopus 로고
    • Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica
    • Thorgersen, M.P., and Downs, D.M. (2009) Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 155: 295-304.
    • (2009) Microbiology , vol.155 , pp. 295-304
    • Thorgersen, M.P.1    Downs, D.M.2
  • 69
    • 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., and Takahashi, Y. (2001) Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J Biochem 130: 63-71.
    • (2001) J Biochem , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 70
    • 72049124821 scopus 로고    scopus 로고
    • The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein
    • Trotter, V., Vinella, D., Loiseau, L., Ollagnier de Choudens, S., Fontecave, M., and Barras, F. (2009) The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol 74: 1527-1542.
    • (2009) Mol Microbiol , vol.74 , pp. 1527-1542
    • Trotter, V.1    Vinella, D.2    Loiseau, L.3    Ollagnier de Choudens, S.4    Fontecave, M.5    Barras, F.6
  • 71
    • 33846972315 scopus 로고    scopus 로고
    • The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence
    • Velayudhan, J., Castor, M., Richardson, A., Main-Hester, K.L., and Fang, F.C. (2007) The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. Mol Microbiol 63: 1495-1507.
    • (2007) Mol Microbiol , vol.63 , pp. 1495-1507
    • Velayudhan, J.1    Castor, M.2    Richardson, A.3    Main-Hester, K.L.4    Fang, F.C.5
  • 72
    • 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., Karlinsev, J.E., Frawley, E.R., Becker, L.A., Nartea, M., and Fang, F.C. (2014) Distinct roles of the Salmonella enterica serovar Typhimurium CyaY and YggX proteins in the biosynthesis and repair of iron-sulfur clusters. Infect Immun 82: 1390-1401.
    • (2014) Infect Immun , vol.82 , pp. 1390-1401
    • Velayudhan, J.1    Karlinsev, J.E.2    Frawley, E.R.3    Becker, L.A.4    Nartea, M.5    Fang, F.C.6
  • 73
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L.E., and Cupp-Vickery, J.R. (2007) Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit Rev Biochem Mol Biol 42: 95-111.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 74
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • Vinella, D., Brochier-Armanet, C., Loiseau, L., Talla, E., and Barras, F. (2009) Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet 5: e1000497.
    • (2009) PLoS Genet , vol.5 , pp. e1000497
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 75
    • 84873058881 scopus 로고    scopus 로고
    • In vivo [Fe-S] cluster acquisition by IscS and NsrR, two stress regulators in Escherichia coli
    • Vinella, D., Loiseau, L., Ollagnier de Choudens, S., Fontecave, M., and Barras, F. (2013) In vivo [Fe-S] cluster acquisition by IscS and NsrR, two stress regulators in Escherichia coli. Mol Microbiol 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
  • 76
    • 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., and Downs, D.M. (2006) Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo. J Bacteriol 188: 1175-1179.
    • (2006) J Bacteriol , vol.188 , pp. 1175-1179
    • Vivas, E.1    Skovran, E.2    Downs, D.M.3
  • 77
    • 77954920916 scopus 로고    scopus 로고
    • Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor
    • Wollers, S., Layer, G., Garcia-Serres, R., Signor, L., Clemancey, M., Latour, J.M., etal. (2010) Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor. J Biol Chem 285: 23331-23341.
    • (2010) J Biol Chem , vol.285 , pp. 23331-23341
    • Wollers, S.1    Layer, G.2    Garcia-Serres, R.3    Signor, L.4    Clemancey, M.5    Latour, J.M.6
  • 78
    • 57349135303 scopus 로고    scopus 로고
    • Dissecting the role of the N-terminal region of the Escherichia coli global transcription factor FNR
    • Yan, A., and Kiley, P.J. (2008) Dissecting the role of the N-terminal region of the Escherichia coli global transcription factor FNR. J Bacteriol 190: 8230-8233.
    • (2008) J Bacteriol , vol.190 , pp. 8230-8233
    • Yan, A.1    Kiley, P.J.2
  • 79
    • 84883178528 scopus 로고    scopus 로고
    • Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS
    • Yan, R., Konarev, P.V., Iannuzzi, C., Adinolfi, S., Roche, B., Kelly, G., etal. (2013) Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS. J Biol Chem 288: 24777-24787.
    • (2013) J Biol Chem , vol.288 , pp. 24777-24787
    • Yan, R.1    Konarev, P.V.2    Iannuzzi, C.3    Adinolfi, S.4    Roche, B.5    Kelly, G.6
  • 80
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo, W.S., Lee, J.H., and Roe, J.H. (2006) IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol Microbiol 61: 206-218.
    • (2006) Mol Microbiol , vol.61 , pp. 206-218
    • Yeo, W.S.1    Lee, J.H.2    Roe, J.H.3
  • 81
    • 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
  • 82
    • 77449106447 scopus 로고    scopus 로고
    • IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
    • Zhang, W., Urban, A., Mihara, H., Leimkuehler, S., Kurihara, T., and Esaki, N. (2010) IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. J Biol Chem 285: 2302-2308.
    • (2010) J Biol Chem , vol.285 , pp. 2302-2308
    • Zhang, W.1    Urban, A.2    Mihara, H.3    Leimkuehler, S.4    Kurihara, T.5    Esaki, N.6
  • 83
    • 0344198175 scopus 로고    scopus 로고
    • Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study
    • Zhao, Z., Rothery, R.A., and Weiner, J.H. (2003) Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study. Biochemistry 42: 14225-14233.
    • (2003) Biochemistry , vol.42 , pp. 14225-14233
    • Zhao, Z.1    Rothery, R.A.2    Weiner, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.