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Volumn 43, Issue 51, 2004, Pages 16432-16441

Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; CARBON; ENZYME KINETICS; MONOMERS; SATURATION (MATERIALS COMPOSITION); SULFUR;

EID: 11144281247     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048040t     Document Type: Article
Times cited : (38)

References (44)
  • 1
    • 0035219736 scopus 로고    scopus 로고
    • Biosynthesis of biotin and lipoic acid
    • (Litwack, G., and Begley, T., Eds.), Academic Press, New York
    • Marquet, A., Tse Sum Bui, B., and Florentin, D. (2001) Biosynthesis of biotin and lipoic acid, in Vitamins and Hormones 61 (Litwack, G., and Begley, T., Eds.) pp 51-101, Academic Press, New York.
    • (2001) Vitamins and Hormones 61 , pp. 51-101
    • Marquet, A.1    Tse Sum Bui, B.2    Florentin, D.3
  • 2
    • 0035478708 scopus 로고    scopus 로고
    • Enzymology of carbon-sulfur bond formation
    • Marquet, A. (2001) Enzymology of carbon-sulfur bond formation, Curr. Opin. Chem. Biol. 5, 541-549.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 541-549
    • Marquet, A.1
  • 3
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information vizualization methods
    • Sofia, H. J., Chen, G., Hetzler, B. G., Reyes-Spindola, J. F., and Miller, N. E. (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information vizualization methods, Nucleic Acids Res. 29, 1097-1106.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 4
    • 0001565147 scopus 로고    scopus 로고
    • In vivo formation of C-S bonds in biotin. An example of radical chemistry under reducing conditions
    • Marquet, A., Florentin, D., Ploux, O., and Tse Sum Bui, B. (1998) In vivo formation of C-S bonds in biotin. An example of radical chemistry under reducing conditions, J. Phys. Org. Chem. 11, 529-536.
    • (1998) J. Phys. Org. Chem. , vol.11 , pp. 529-536
    • Marquet, A.1    Florentin, D.2    Ploux, O.3    Tse Sum Bui, B.4
  • 5
    • 0032521253 scopus 로고    scopus 로고
    • Biotin synthase from Escherichia coli: Isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use
    • Shaw, N. M., Birch, O. M., Tinschert, A., Venetz, V., Dietrich, R., and Savoy, L.-A. (1998) Biotin synthase from Escherichia coli: Isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use, Biochem. J. 330, 1079-1085.
    • (1998) Biochem. J. , vol.330 , pp. 1079-1085
    • Shaw, N.M.1    Birch, O.M.2    Tinschert, A.3    Venetz, V.4    Dietrich, R.5    Savoy, L.-A.6
  • 7
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • Ugulava, N. B., Gibney, B. R., and Jarrett, J. T. (2001) Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions, Biochemistry 40, 8343-8351.
    • (2001) Biochemistry , vol.40 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 10
    • 1242330269 scopus 로고    scopus 로고
    • Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase
    • Jameson, G. N. L., Cosper, M. M., Hernandez, H. L., Johnson, M. K., and Huynh, B. H. (2004) Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase, Biochemistry 43, 2022-2031.
    • (2004) Biochemistry , vol.43 , pp. 2022-2031
    • Jameson, G.N.L.1    Cosper, M.M.2    Hernandez, H.L.3    Johnson, M.K.4    Huynh, B.H.5
  • 11
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosyl-methionine-dependent radical enzyme
    • Berkovitch, F., Nicolet, Y., Wan, J. T., Jarrett, J. T., and Drennan, C. L. (2004) Crystal structure of biotin synthase, an S-adenosyl-methionine- dependent radical enzyme, Science 303, 76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 13
    • 0038575234 scopus 로고    scopus 로고
    • S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin?
    • Frey, P. A., and Magnusson, O. T. (2003) S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem. Rev. 103, 2129-2148.
    • (2003) Chem. Rev. , vol.103 , pp. 2129-2148
    • Frey, P.A.1    Magnusson, O.T.2
  • 14
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer, G., Moser, J., Heinz, D. W., Jahn, D., and Schubert, W.-D. (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes, EMBO J. 23, 6214-6224.
    • (2003) EMBO J. , vol.23 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.-D.5
  • 15
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • Hänzelmann, P., and Schindelin, H. (2004) Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans, Proc. Natl. Acad. Sci. U.S.A. 101, 12870-12875.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12870-12875
    • Hänzelmann, P.1    Schindelin, H.2
  • 16
    • 0029564157 scopus 로고
    • Highly purified biotin synthase can transform dethiobiotin into biotin in the absence of any other protein, in the presence of photoreduced deazaflavin
    • Méjean, A., Tse Sum Bui, B., Florentin, D., Ploux, O., Izumi, Y., and Marquet, A. (1995) Highly purified biotin synthase can transform dethiobiotin into biotin in the absence of any other protein, in the presence of photoreduced deazaflavin, Biochem. Biophys. Res. Commun. 217, 1231-1237.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1231-1237
    • Méjean, A.1    Tse Sum Bui, B.2    Florentin, D.3    Ploux, O.4    Izumi, Y.5    Marquet, A.6
  • 18
    • 0035902555 scopus 로고    scopus 로고
    • Spectroscopic changes during a single turnover of biotin synthase: Destruction of a [2Fe-2S] cluster accompanies sulfur insertion
    • Ugulava, N. B., Sacanell, C. J., and Jarrett, J. T. (2001) Spectroscopic changes during a single turnover of biotin synthase: Destruction of a [2Fe-2S] cluster accompanies sulfur insertion, Biochemistry 40, 8352-8358.
    • (2001) Biochemistry , vol.40 , pp. 8352-8358
    • Ugulava, N.B.1    Sacanell, C.J.2    Jarrett, J.T.3
  • 19
  • 20
    • 0000638382 scopus 로고    scopus 로고
    • Enzyme-mediated sulphide production for the reconstitution of [2Fe-2S] clusters into apo-biotin synthase of Escherichia coli. Sulphide transfer from cysteine to biotin
    • Tse Sum Bui, B., Escalettes, F., Chottard, G., Florentin, D., and Marquet, A. (2000) Enzyme-mediated sulphide production for the reconstitution of [2Fe-2S] clusters into apo-biotin synthase of Escherichia coli. Sulphide transfer from cysteine to biotin, Eur. J. Biochem. 459, 2688-2694.
    • (2000) Eur. J. Biochem. , vol.459 , pp. 2688-2694
    • Tse Sum Bui, B.1    Escalettes, F.2    Chottard, G.3    Florentin, D.4    Marquet, A.5
  • 21
    • 0030051242 scopus 로고    scopus 로고
    • Escherichia coli biotin synthase: An investigation into the factors required for its activity and its sulfur donor
    • Sanyal, I., Gibson, K. J., and Flint, D. H. (1996) Escherichia coli biotin synthase: An investigation into the factors required for its activity and its sulfur donor, Arch. Biochem. Biophys. 326, 48-56.
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 48-56
    • Sanyal, I.1    Gibson, K.J.2    Flint, D.H.3
  • 22
    • 0034607801 scopus 로고    scopus 로고
    • Identification of the [Fe-S] cluster-binding residues of Escherichia coli biotin synthase
    • McIver, L., Baxter, R. L., and Campopiano, D. J. (2000) Identification of the [Fe-S] cluster-binding residues of Escherichia coli biotin synthase, J. Biol. Chem. 275, 13888-13894.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13888-13894
    • McIver, L.1    Baxter, R.L.2    Campopiano, D.J.3
  • 24
    • 0034595376 scopus 로고    scopus 로고
    • Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters
    • Ugulava, N. B., Gibney, B. R., and Jarrett, J. T. (2000) Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters, Biochemistry 39, 5206-5214.
    • (2000) Biochemistry , vol.39 , pp. 5206-5214
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 25
    • 0037132531 scopus 로고    scopus 로고
    • The PLP-dependent biotin synthase from Escherichia coli: Mechanistic studies
    • Ollagnier-de Choudens, S., Mulliez, E., and Fontecave, M. (2002) The PLP-dependent biotin synthase from Escherichia coli: Mechanistic studies, FEBS Lett. 535, 465-468.
    • (2002) FEBS Lett. , vol.535 , pp. 465-468
    • Ollagnier-De Choudens, S.1    Mulliez, E.2    Fontecave, M.3
  • 26
    • 0001199518 scopus 로고
    • Biotin biosynthesis: Synthesis and biological evaluation of the putative intermediate thiols
    • Marquet, A., Frappier, F., Guillerm, G., Azoulay, M., Florentin, D., and Tabet, J.-C. (1993) Biotin biosynthesis: Synthesis and biological evaluation of the putative intermediate thiols, J. Am. Chem. Soc. 115, 2139-2145.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2139-2145
    • Marquet, A.1    Frappier, F.2    Guillerm, G.3    Azoulay, M.4    Florentin, D.5    Tabet, J.-C.6
  • 29
    • 0016976361 scopus 로고
    • 5-Deaza- and 5-Thiariboflavins: A simple pathway to antimetabolites of vitamin B2
    • Janda, M., and Hemmerich, P. (1976) 5-Deaza- and 5-Thiariboflavins: A simple pathway to antimetabolites of vitamin B2, Angew. Chem. 15, 443-444.
    • (1976) Angew. Chem. , vol.15 , pp. 443-444
    • Janda, M.1    Hemmerich, P.2
  • 30
    • 0000546802 scopus 로고
    • Biotin biosynthesis: Preparation of the postulated intermediate thiol
    • Even, L., Florentin, D., and Marquet, A. (1990) Biotin biosynthesis: Preparation of the postulated intermediate thiol, Bull. Soc. Chim. Fr. 127, 758-768.
    • (1990) Bull. Soc. Chim. Fr. , vol.127 , pp. 758-768
    • Even, L.1    Florentin, D.2    Marquet, A.3
  • 31
    • 0029304419 scopus 로고
    • Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli
    • Ohshiro, T., Yamamoto, M., Tse Sum Bui, B., Florentin, D., Marquet, A., and Izumi, Y. (1995) Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli, Biosci., Biotechnol., Biochem. 59, 943-944.
    • (1995) Biosci., Biotechnol., Biochem. , vol.59 , pp. 943-944
    • Ohshiro, T.1    Yamamoto, M.2    Tse Sum Bui, B.3    Florentin, D.4    Marquet, A.5    Izumi, Y.6
  • 32
    • 0031577321 scopus 로고    scopus 로고
    • Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical
    • Guianvarc'h, D., Florentin, D., Tse Sum Bui, B., Nunzi, F., and Marquet, A. (1997) Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical, Biochem. Biophys. Res. Commun. 236, 402-406.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 402-406
    • Guianvarc'h, D.1    Florentin, D.2    Tse Sum Bui, B.3    Nunzi, F.4    Marquet, A.5
  • 33
    • 0023198883 scopus 로고
    • Biotin assay using lyophilized and glycerol-suspended cultures
    • Izumi, Y., Osakai, M., and Yamada, H. (1987) Biotin assay using lyophilized and glycerol-suspended cultures, J. Microbiol. Methods 6, 237-246.
    • (1987) J. Microbiol. Methods , vol.6 , pp. 237-246
    • Izumi, Y.1    Osakai, M.2    Yamada, H.3
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0023899855 scopus 로고    scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish, W. W. (1998) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples, Methods Enzymol. 158, 357-364.
    • (1998) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 36
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert, H. (1983) Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins, Anal. Biochem. 131, 373-378.
    • (1983) Anal. Biochem. , vol.131 , pp. 373-378
    • Beinert, H.1
  • 37
    • 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
  • 38
  • 40
    • 0027490950 scopus 로고
    • Biotin biosynthesis in higher plant cells. Identification of intermediates
    • Baldet, P., Gerbling, H., Axiotis, S., and Douce, R. (1993) Biotin biosynthesis in higher plant cells. Identification of intermediates, Eur. J. Biochem. 217, 479-485.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 479-485
    • Baldet, P.1    Gerbling, H.2    Axiotis, S.3    Douce, R.4
  • 42
    • 33845183210 scopus 로고
    • Absolute rate expressions for the abstraction of hydrogen by primary, secondary, and tertiary alkyl radicals from thiophenol
    • Franz, J. A., Bushaw, B. A., and Alnajjar, M. S. (1989) Absolute rate expressions for the abstraction of hydrogen by primary, secondary, and tertiary alkyl radicals from thiophenol, J. Am. Chem. Soc. 111, 268-275.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 268-275
    • Franz, J.A.1    Bushaw, B.A.2    Alnajjar, M.S.3
  • 43
    • 0033594329 scopus 로고    scopus 로고
    • Biotin synthase mechanism: Evidence for hydrogen transfer from the substrate into deoxyadenosine
    • Escalettes, F., Florentin, D., Tse Sum Bui, B., Lesage, D., and Marquet, A. (1999) Biotin synthase mechanism: Evidence for hydrogen transfer from the substrate into deoxyadenosine, J. Am. Chem. Soc. 121, 3571-3578.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3571-3578
    • Escalettes, F.1    Florentin, D.2    Tse Sum Bui, B.3    Lesage, D.4    Marquet, A.5
  • 44
    • 0023952439 scopus 로고
    • The state of cluster sulfhydryl and sulfide of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme
    • Kennedy, M. C., and Beinert, H. (1988) The state of cluster sulfhydryl and sulfide of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme, J. Biol. Chem. 263, 8194-8198.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8194-8198
    • Kennedy, M.C.1    Beinert, H.2


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