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Volumn 52, Issue 23, 2013, Pages 4089-4096

Protected sulfur transfer reactions by the Escherichia coli Suf system

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC REACTIVITY; CATALYTIC TURNOVER; CYSTEINE DESULFURASE; KINETIC ANALYSIS; SEQUENTIAL TRANSFER; STIMULATORY EFFECTS; SULFUR TRANSFER REACTIONS; TRIS (2-CARBOXYETHYL) PHOSPHINE HYDROCHLORIDE (TCEP HCL);

EID: 84878909112     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4001479     Document Type: Article
Times cited : (43)

References (23)
  • 1
    • 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
  • 2
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: Delivering sulfur in biosynthetic pathways
    • Mueller, E. G. (2006) Trafficking in persulfides: Delivering sulfur in biosynthetic pathways Nat. Chem. Biol. 2, 185-194
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 3
    • 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. M., Jr. (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 Jr., J.M.2
  • 5
    • 79959190407 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: Versatile key players in biosynthetic pathways of sulfur-containing biofactors
    • Hidese, R., Mihara, H., and Esaki, N. (2011) Bacterial cysteine desulfurases: Versatile key players in biosynthetic pathways of sulfur-containing biofactors Appl. Microbiol. Biotechnol. 91, 47-61
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 47-61
    • Hidese, R.1    Mihara, H.2    Esaki, N.3
  • 6
    • 0037209757 scopus 로고    scopus 로고
    • Bacterial cysteine desulfurases: Their function and mechanisms
    • Mihara, H. and Esaki, N. (2002) Bacterial cysteine desulfurases: Their function and mechanisms Appl. Microbiol. Biotechnol. 60, 12-23
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 12-23
    • Mihara, H.1    Esaki, N.2
  • 7
    • 0037197897 scopus 로고    scopus 로고
    • Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
    • Kato, S., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T., and Esaki, N. (2002) Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly Proc. Natl. Acad. Sci. U.S.A. 99, 5948-5952
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5948-5952
    • Kato, S.1    Mihara, H.2    Kurihara, T.3    Takahashi, Y.4    Tokumoto, U.5    Yoshimura, T.6    Esaki, N.7
  • 8
    • 84868544593 scopus 로고    scopus 로고
    • The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU
    • Dai, Y. and Outten, F. W. (2012) The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU FEBS Lett. 586, 4016-4022
    • (2012) FEBS Lett. , vol.586 , pp. 4016-4022
    • Dai, Y.1    Outten, F.W.2
  • 9
    • 4644275046 scopus 로고    scopus 로고
    • Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
    • Tirupati, B., Vey, J. L., Drennan, C. L., and Bollinger, J. M., Jr. (2004) Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803 Biochemistry 43, 12210-12219
    • (2004) Biochemistry , vol.43 , pp. 12210-12219
    • Tirupati, B.1    Vey, J.L.2    Drennan, C.L.3    Bollinger Jr., J.M.4
  • 10
    • 0036562516 scopus 로고    scopus 로고
    • Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: Implications for its specificity toward selenocysteine
    • Mihara, H., Fujii, T., Kato, S., Kurihara, T., Hata, Y., and Esaki, N. (2002) Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: Implications for its specificity toward selenocysteine J. Biochem. 131, 679-685
    • (2002) J. Biochem. , vol.131 , pp. 679-685
    • Mihara, H.1    Fujii, T.2    Kato, S.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0345303679 scopus 로고    scopus 로고
    • Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE
    • Ollagnier-de-Choudens, S., Lascoux, D., Loiseau, L., Barras, F., Forest, E., and Fontecave, M. (2003) Mechanistic studies of the SufS-SufE cysteine desulfurase: Evidence for sulfur transfer from SufS to SufE FEBS Lett. 555, 263-267
    • (2003) FEBS Lett. , vol.555 , pp. 263-267
    • Ollagnier-De-Choudens, S.1    Lascoux, D.2    Loiseau, L.3    Barras, F.4    Forest, E.5    Fontecave, M.6
  • 16
    • 77957657538 scopus 로고    scopus 로고
    • Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis
    • Selbach, B., Earles, E., and Dos Santos, P. C. (2010) Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis Biochemistry 49, 8794-8802
    • (2010) Biochemistry , vol.49 , pp. 8794-8802
    • Selbach, B.1    Earles, E.2    Dos Santos, P.C.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0002652541 scopus 로고
    • Enzymatic transamination of pyridoxamine. I. with oxaloacetate and α-ketoglutarate
    • Wada, H. and Snell, E. E. (1962) Enzymatic transamination of pyridoxamine. I. With oxaloacetate and α-ketoglutarate J. Biol. Chem. 237, 127-32
    • (1962) J. Biol. Chem. , vol.237 , pp. 127-132
    • Wada, H.1    Snell, E.E.2
  • 21
    • 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., and Esaki, N. (2000) Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between l -cysteine desulfurase and l -selenocysteine lyase reactions J. Biochem. 127, 559-567
    • (2000) J. Biochem. , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 22
  • 23
    • 0015857036 scopus 로고
    • Steady-State Enzyme Kinetics with High Affinity Substrates or Inhibitors: A statistical treatment of dose-response curves
    • Henderson, P. J. (1973) Steady-State Enzyme Kinetics with High Affinity Substrates or Inhibitors: A statistical treatment of dose-response curves Biochem. J. 135, 101-107
    • (1973) Biochem. J. , vol.135 , pp. 101
    • Henderson, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.