메뉴 건너뛰기




Volumn 1824, Issue 11, 2012, Pages 1213-1222

Biotin synthase: Insights into radical-mediated carbon-sulfur bond formation

Author keywords

Biotin biosynthesis; Cofactor biosynthesis; Enzyme mechanism; Iron sulfur cluster; Radical enzyme

Indexed keywords

9 MERCAPTODETHIOBIOTIN; BIOTIN; BIOTIN DERIVATIVE; BIOTIN SYNTHASE; CARBON; CYTOCHROME P450; FATTY ACID SYNTHASE; HYDROGEN; IRON; IRON SULFUR PROTEIN; MALONYL COENZYME A; MALONYL COENZYME A DECARBOXYLASE; RADICAL; S ADENOSYLMETHIONINE; SULFUR; UNCLASSIFIED DRUG;

EID: 84866036753     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.01.010     Document Type: Review
Times cited : (67)

References (87)
  • 1
    • 68049092197 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin thiazole in Bacillus subtilis: Identification of the product of the thiazole synthase-catalyzed reaction
    • A. Hazra, A. Chatterjee, and T.P. Begley Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction J. Am. Chem. Soc. 131 2009 3225 3229
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3225-3229
    • Hazra, A.1    Chatterjee, A.2    Begley, T.P.3
  • 3
    • 0001565147 scopus 로고    scopus 로고
    • In vivo formation of CS bonds in biotin. An example of radical chemistry under reducing conditions
    • A. Marquet, D. Florentin, O. Ploux, and B. Tse Sum Bui In vivo formation of CS bonds in biotin. An example of radical chemistry under reducing conditions J. Phys. Org. Chem. 11 1998 529 535
    • (1998) J. Phys. Org. Chem. , vol.11 , pp. 529-535
    • Marquet, A.1    Florentin, D.2    Ploux, O.3    Tse Sum Bui, B.4
  • 6
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • J.R. Knowles The mechanism of biotin-dependent enzymes Annu. Rev. Biochem. 58 1989 195 221
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 8
    • 0042836452 scopus 로고
    • On the structures of some adducts of biotin with electrophiles: Does sulfur transannular interaction with the carbonyl group play a role in the chemistry or biochemistry of biotin?
    • A. Berkessel, and R. Breslow On the structures of some adducts of biotin with electrophiles: does sulfur transannular interaction with the carbonyl group play a role in the chemistry or biochemistry of biotin? Bioorg. Chem. 14 1986 249 261
    • (1986) Bioorg. Chem. , vol.14 , pp. 249-261
    • Berkessel, A.1    Breslow, R.2
  • 10
    • 0000631410 scopus 로고
    • Mechanisms of decarboxylation of carboxybiotin
    • P.A. Tipton, and W.W. Cleland Mechanisms of decarboxylation of carboxybiotin J. Am. Chem. Soc. 110 1988 5866 5869
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5866-5869
    • Tipton, P.A.1    Cleland, W.W.2
  • 11
    • 0013852012 scopus 로고
    • Studies of the mechanism of biotin catalysis
    • M. Caplow Studies of the mechanism of biotin catalysis J. Am. Chem. Soc. 87 1965 5774 5785
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 5774-5785
    • Caplow, M.1
  • 12
    • 77955927354 scopus 로고    scopus 로고
    • Biotin synthesis begins by hijacking the fatty acid synthetic pathway
    • S. Lin, R.E. Hanson, and J.E. Cronan Biotin synthesis begins by hijacking the fatty acid synthetic pathway Nat. Chem. Biol. 6 2010 682 688
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 682-688
    • Lin, S.1    Hanson, R.E.2    Cronan, J.E.3
  • 14
    • 0036797992 scopus 로고    scopus 로고
    • Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea
    • D.A. Rodionov, A.A. Mironov, and M.S. Gelfand Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea Genome Res. 12 2002 1507 1516
    • (2002) Genome Res. , vol.12 , pp. 1507-1516
    • Rodionov, D.A.1    Mironov, A.A.2    Gelfand, M.S.3
  • 15
    • 0026603151 scopus 로고
    • The 8-amino-7-oxopelargonate synthase from Bacillus sphaericus. Purification and preliminary characterization of the cloned enzyme overproduced in Escherichia coli
    • O. Ploux, and A. Marquet The 8-amino-7-oxopelargonate synthase from Bacillus sphaericus. Purification and preliminary characterization of the cloned enzyme overproduced in Escherichia coli Biochem. J. 283 1992 327 331
    • (1992) Biochem. J. , vol.283 , pp. 327-331
    • Ploux, O.1    Marquet, A.2
  • 17
    • 0037159244 scopus 로고    scopus 로고
    • The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation
    • A.C. Eliot, J. Sandmark, G. Schneider, and J.F. Kirsch The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation Biochemistry 41 2002 12582 12589
    • (2002) Biochemistry , vol.41 , pp. 12582-12589
    • Eliot, A.C.1    Sandmark, J.2    Schneider, G.3    Kirsch, J.F.4
  • 18
    • 0030790705 scopus 로고    scopus 로고
    • Isolation and chemistry of the mixed anhydride intermediate in the reaction catalyzed by dethiobiotin synthetase
    • K.J. Gibson Isolation and chemistry of the mixed anhydride intermediate in the reaction catalyzed by dethiobiotin synthetase Biochemistry 36 1997 8474 8478
    • (1997) Biochemistry , vol.36 , pp. 8474-8478
    • Gibson, K.J.1
  • 19
    • 0038689709 scopus 로고
    • Zur biochemischen funktion des biotins. IV. Die biosynthese des biotins
    • A. Lezius, and E. Ringelmann Zur biochemischen funktion des biotins. IV. Die biosynthese des biotins Biochem. Z. 336 1963 510 525
    • (1963) Biochem. Z. , vol.336 , pp. 510-525
    • Lezius, A.1    Ringelmann, E.2
  • 21
    • 33745318572 scopus 로고
    • The possible synthesis of biotin from desthiobiotin by yeast and the anti-biotin effect of desthiobiotin for L. casei
    • K. Dittmer, D.B. Melville, and V. Du Vigneaud The possible synthesis of biotin from desthiobiotin by yeast and the anti-biotin effect of desthiobiotin for L. casei Science 99 1944 203 205
    • (1944) Science , vol.99 , pp. 203-205
    • Dittmer, K.1    Melville, D.B.2    Du Vigneaud, V.3
  • 22
    • 84866044908 scopus 로고
    • Conversion of desthiobiotin into biotin or biotinlike substances by some microorganisms
    • L. Leonian, and V. Lilly Conversion of desthiobiotin into biotin or biotinlike substances by some microorganisms J. Bacteriol. 49 1945 291
    • (1945) J. Bacteriol. , vol.49 , pp. 291
    • Leonian, L.1    Lilly, V.2
  • 23
    • 84866040047 scopus 로고
    • Microbiological activity of synthetic biotin, its optical isomers, and related compounds
    • J.L. Stokes, and M. Gunness Microbiological activity of synthetic biotin, its optical isomers, and related compounds J. Biol. Chem. 157 1945 121 126
    • (1945) J. Biol. Chem. , vol.157 , pp. 121-126
    • Stokes, J.L.1    Gunness, M.2
  • 24
    • 0014011723 scopus 로고
    • Direct evidence for the conversion of dethiobiotin to biotin in Aspergillus niger
    • J.P. Tepper, D.B. McCormick, and L.D. Wright Direct evidence for the conversion of dethiobiotin to biotin in Aspergillus niger J. Biol. Chem. 241 1966 5734 5735
    • (1966) J. Biol. Chem. , vol.241 , pp. 5734-5735
    • Tepper, J.P.1    McCormick, D.B.2    Wright, L.D.3
  • 25
    • 70449153782 scopus 로고
    • Biotin requirements of a mutant strain of Escherichia coli
    • R.B. Ferguson, and H.C. Lichstein Biotin requirements of a mutant strain of Escherichia coli Proc. Soc. Exp. Biol. Med. 95 1957 766 769
    • (1957) Proc. Soc. Exp. Biol. Med. , vol.95 , pp. 766-769
    • Ferguson, R.B.1    Lichstein, H.C.2
  • 27
    • 0014320426 scopus 로고
    • Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12
    • B. Rolfe, and M. Eisenberg Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12 J. Bacteriol. 96 1968 515 524
    • (1968) J. Bacteriol. , vol.96 , pp. 515-524
    • Rolfe, B.1    Eisenberg, M.2
  • 28
    • 0014181397 scopus 로고
    • Biosynthesis of biotin in microorganisms. VI. Further evidence for desthiobiotin as a precursor in Escherichia coli
    • C.H. Pai, and H.C. Lichstein Biosynthesis of biotin in microorganisms. VI. Further evidence for desthiobiotin as a precursor in Escherichia coli J. Bacteriol. 94 1967 1930 1933
    • (1967) J. Bacteriol. , vol.94 , pp. 1930-1933
    • Pai, C.H.1    Lichstein, H.C.2
  • 29
    • 0014691223 scopus 로고
    • Dethiobiotin synthesis from 7,8-diaminolargonic acid in cell-free extracts of a biotin auxotroph of Escherichia coli K-12
    • M.A. Eisenberg, and K. Krell Dethiobiotin synthesis from 7,8-diaminolargonic acid in cell-free extracts of a biotin auxotroph of Escherichia coli K-12 J. Biol. Chem. 244 1969 5503 5509
    • (1969) J. Biol. Chem. , vol.244 , pp. 5503-5509
    • Eisenberg, M.A.1    Krell, K.2
  • 30
    • 0014569933 scopus 로고
    • Biosynthesis of desthiobiotin in cell-free extracts of Escherichia coli
    • C.H. Pai Biosynthesis of desthiobiotin in cell-free extracts of Escherichia coli J. Bacteriol. 99 1969 696 701
    • (1969) J. Bacteriol. , vol.99 , pp. 696-701
    • Pai, C.H.1
  • 31
    • 0017579420 scopus 로고
    • On the mechanism of conversion of dethiobiotin to biotin in Escherichia coli
    • G. Guillerm, F. Frappier, M. Gaudry, and A. Marquet On the mechanism of conversion of dethiobiotin to biotin in Escherichia coli Biochimie 59 1977 119 121
    • (1977) Biochimie , vol.59 , pp. 119-121
    • Guillerm, G.1    Frappier, F.2    Gaudry, M.3    Marquet, A.4
  • 32
    • 0018598151 scopus 로고
    • On the mechanism of conversion of dethiobiotin to biotin in Escherichia coli. Discussion of the occurrence of an intermediate hydroxylation
    • F. Frappier, G. Guillerm, A.G. Salib, and A. Marquet On the mechanism of conversion of dethiobiotin to biotin in Escherichia coli. Discussion of the occurrence of an intermediate hydroxylation Biochem. Biophys. Res. Commun. 91 1979 521 527
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 521-527
    • Frappier, F.1    Guillerm, G.2    Salib, A.G.3    Marquet, A.4
  • 33
    • 0017313956 scopus 로고
    • Biotin biosynthesis. 1. The incorporation of specifically tritiated dethiobiotin into biotin
    • R.J. Parry, and M.G. Kunitani Biotin biosynthesis. 1. The incorporation of specifically tritiated dethiobiotin into biotin J. Am. Chem. Soc. 98 1976 4024 4026
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 4024-4026
    • Parry, R.J.1    Kunitani, M.G.2
  • 35
    • 0020065440 scopus 로고
    • Mode of action of the biotin antimetabolites actithiazic acid and alpha-methyldethiobiotin
    • M.A. Eisenberg, and S.C. Hsiung Mode of action of the biotin antimetabolites actithiazic acid and alpha-methyldethiobiotin Antimicrob. Agents Chemother. 21 1982 5 10
    • (1982) Antimicrob. Agents Chemother. , vol.21 , pp. 5-10
    • Eisenberg, M.A.1    Hsiung, S.C.2
  • 38
    • 0028280411 scopus 로고
    • Biotin synthase: Purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product
    • I. Sanyal, G. Cohen, and D.H. Flint Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product Biochemistry 33 1994 3625 3631
    • (1994) Biochemistry , vol.33 , pp. 3625-3631
    • Sanyal, I.1    Cohen, G.2    Flint, D.H.3
  • 39
    • 0028071086 scopus 로고
    • Flavodoxin is required for conversion of dethiobiotin to biotin in Escherichia coli
    • O. Ifuku, N. Koga, S. Haze, J. Kishimoto, and Y. Wachi Flavodoxin is required for conversion of dethiobiotin to biotin in Escherichia coli Eur. J. Biochem. 224 1994 173 178
    • (1994) Eur. J. Biochem. , vol.224 , pp. 173-178
    • Ifuku, O.1    Koga, N.2    Haze, S.3    Kishimoto, J.4    Wachi, Y.5
  • 40
    • 0029047343 scopus 로고
    • Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro
    • O.M. Birch, M. Fuhrmann, and N.M. Shaw Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro J. Biol. Chem. 270 1995 19158 19165
    • (1995) J. Biol. Chem. , vol.270 , pp. 19158-19165
    • Birch, O.M.1    Fuhrmann, M.2    Shaw, N.M.3
  • 42
    • 0035902555 scopus 로고    scopus 로고
    • Spectroscopic changes during a single turnover of biotin synthase: Destruction of a [2Fe-2S] cluster accompanies sulfur insertion
    • N.B. Ugulava, C.J. Sacanell, and J.T. Jarrett Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion Biochemistry 40 2001 8352 8358
    • (2001) Biochemistry , vol.40 , pp. 8352-8358
    • Ugulava, N.B.1    Sacanell, C.J.2    Jarrett, J.T.3
  • 43
    • 0019807234 scopus 로고
    • On the biosynthesis of biotin in Achromobacter IVSW. A reinvestigation
    • F. Frappier, and A. Marquet On the biosynthesis of biotin in Achromobacter IVSW. A reinvestigation. Biochem. Biophys. Res. Commun. 103 1981 1288 1293
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 1288-1293
    • Frappier, F.1    Marquet, A.2
  • 44
    • 0030051242 scopus 로고    scopus 로고
    • Escherichia coli biotin synthase: An investigation into the factors required for its activity and its sulfur donor
    • I. Sanyal, K.J. Gibson, and D.H. Flint Escherichia coli biotin synthase: an investigation into the factors required for its activity and its sulfur donor Arch. Biochem. Biophys. 326 1996 48 56
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 48-56
    • Sanyal, I.1    Gibson, K.J.2    Flint, D.H.3
  • 46
    • 36048943610 scopus 로고    scopus 로고
    • In vivo resolution of conflicting in vitro results: Synthesis of biotin from dethiobiotin does not require pyridoxal phosphate
    • A.M. Abdel-Hamid, and J.E. Cronan In vivo resolution of conflicting in vitro results: synthesis of biotin from dethiobiotin does not require pyridoxal phosphate Chem. Biol. 14 2007 1215 1220
    • (2007) Chem. Biol. , vol.14 , pp. 1215-1220
    • Abdel-Hamid, A.M.1    Cronan, J.E.2
  • 47
    • 1242285458 scopus 로고    scopus 로고
    • Characterization of the cofactor composition of Escherichia coli biotin synthase
    • M. Cosper, G. Jameson, H. Hernández, C. Krebs, B. Huynh, and M. Johnson Characterization of the cofactor composition of Escherichia coli biotin synthase Biochemistry 43 2004 2007 2021
    • (2004) Biochemistry , vol.43 , pp. 2007-2021
    • Cosper, M.1    Jameson, G.2    Hernández, H.3    Krebs, C.4    Huynh, B.5    Johnson, M.6
  • 48
    • 11144281247 scopus 로고    scopus 로고
    • Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates
    • B. Tse Sum Bui, M. Lotierzo, F. Escalettes, D. Florentin, and A. Marquet Further investigation on the turnover of Escherichia coli biotin synthase with dethiobiotin and 9-mercaptodethiobiotin as substrates Biochemistry 43 2004 16432 16441
    • (2004) Biochemistry , vol.43 , pp. 16432-16441
    • Tse Sum Bui, B.1    Lotierzo, M.2    Escalettes, F.3    Florentin, D.4    Marquet, A.5
  • 49
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: Flavodoxin and NADPH: Flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase
    • H.P. Blaschkowski, G. Neuer, M. Ludwig-Festl, and J. Knappe Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase Eur. J. Biochem. 123 1982 563 569
    • (1982) Eur. J. Biochem. , vol.123 , pp. 563-569
    • Blaschkowski, H.P.1    Neuer, G.2    Ludwig-Festl, M.3    Knappe, J.4
  • 50
    • 0034644695 scopus 로고    scopus 로고
    • MioC Is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro
    • O.M. Birch, K.S. Hewitson, M. Fuhrmann, K. Burgdorf, J.E. Baldwin, P.L. Roach, and N.M. Shaw MioC Is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro J. Biol. Chem. 275 2000 32277 32280
    • (2000) J. Biol. Chem. , vol.275 , pp. 32277-32280
    • Birch, O.M.1    Hewitson, K.S.2    Fuhrmann, M.3    Burgdorf, K.4    Baldwin, J.E.5    Roach, P.L.6    Shaw, N.M.7
  • 51
    • 33845921565 scopus 로고    scopus 로고
    • Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both apo- and holo-forms: Implications for cofactor binding and electron transfer
    • Y. Hu, Y. Li, X. Zhang, X. Guo, B. Xia, and C. Jin Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both apo- and holo-forms: implications for cofactor binding and electron transfer J. Biol. Chem. 281 2006 35454 35466
    • (2006) J. Biol. Chem. , vol.281 , pp. 35454-35466
    • Hu, Y.1    Li, Y.2    Zhang, X.3    Guo, X.4    Xia, B.5    Jin, C.6
  • 53
    • 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
    • D. Guianvarc'h, D. Florentin, B. Tse Sum Bui, F. Nunzi, and A. Marquet 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 1997 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
  • 54
    • 0032521253 scopus 로고    scopus 로고
    • Biotin synthase from Escherichia coli: Isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use
    • N.M. Shaw, O.M. Birch, A. Tinschert, V. Venetz, R. Dietrich, and L.A. Savoy Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use Biochem. J. 330 1998 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
  • 55
    • 0033594329 scopus 로고    scopus 로고
    • Biotin synthase mechanism: Evidence for hydrogen transfer from the substrate into deoxyadenosine
    • F. Escalettes, D. Florentin, B. Tse Sum Bui, D. Lesage, and A. Marquet Biotin synthase mechanism: evidence for hydrogen transfer from the substrate into deoxyadenosine J. Am. Chem. Soc. 121 1999 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
  • 56
    • 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 visualization methods
    • H.J. Sofia, G. Chen, B.G. Hetzler, J.F. Reyes-Spindola, and N.E. Miller Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods Nucleic Acids Res. 29 2001 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
  • 57
    • 0033969775 scopus 로고    scopus 로고
    • Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase
    • K.S. Hewitson, J.E. Baldwin, N.M. Shaw, and P.L. Roach Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase FEBS Lett. 466 2000 372 376
    • (2000) FEBS Lett. , vol.466 , pp. 372-376
    • Hewitson, K.S.1    Baldwin, J.E.2    Shaw, N.M.3    Roach, P.L.4
  • 59
    • 9744258825 scopus 로고    scopus 로고
    • The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase
    • J.T. Jarrett The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase Arch. Biochem. Biophys. 433 2005 312 321
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 312-321
    • Jarrett, J.T.1
  • 62
    • 0034595376 scopus 로고    scopus 로고
    • Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron is required for conversion of [2Fe-2S] to [4Fe-4S] clusters
    • N.B. Ugulava, B.R. Gibney, and J.T. Jarrett Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron is required for conversion of [2Fe-2S] to [4Fe-4S] clusters Biochemistry 39 2000 5206 5214
    • (2000) Biochemistry , vol.39 , pp. 5206-5214
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 63
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • N.B. Ugulava, B.R. Gibney, and J.T. Jarrett Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions Biochemistry 40 2001 8343 8351
    • (2001) Biochemistry , vol.40 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 65
    • 0037432317 scopus 로고    scopus 로고
    • Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB
    • N.B. Ugulava, K.K. Frederick, and J.T. Jarrett Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB Biochemistry 42 2003 2708 2719
    • (2003) Biochemistry , vol.42 , pp. 2708-2719
    • Ugulava, N.B.1    Frederick, K.K.2    Jarrett, J.T.3
  • 66
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • F. Berkovitch, Y. Nicolet, J.T. Wan, J.T. Jarrett, and C.L. Drennan Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme Science 303 2004 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
  • 70
    • 0037174377 scopus 로고    scopus 로고
    • An anchoring role for FeS clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme
    • C.J. Walsby, D. Ortillo, W.E. Broderick, J.B. Broderick, and B.M. Hoffman An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme J. Am. Chem. Soc. 124 2002 11270 11271
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 72
    • 79955083639 scopus 로고    scopus 로고
    • Generation of adenosyl radical from S-adenosylmethionine (SAM) in biotin synthase
    • T. Kamachi, T. Kouno, K. Doitomi, and K. Yoshizawa Generation of adenosyl radical from S-adenosylmethionine (SAM) in biotin synthase J. Inorg. Biochem. 105 2011 850 857
    • (2011) J. Inorg. Biochem. , vol.105 , pp. 850-857
    • Kamachi, T.1    Kouno, T.2    Doitomi, K.3    Yoshizawa, K.4
  • 73
    • 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
    • A. Mejean, B. Tse Sum Bui, D. Florentin, O. Ploux, Y. Izumi, and A. Marquet 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 1995 1231 1237
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1231-1237
    • Mejean, A.1    Tse Sum Bui, B.2    Florentin, D.3    Ploux, O.4    Izumi, Y.5    Marquet, A.6
  • 77
    • 50849090609 scopus 로고    scopus 로고
    • 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase
    • A.M. Taylor, C.E. Farrar, and J.T. Jarrett 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase Biochemistry 47 2008 9309 9317
    • (2008) Biochemistry , vol.47 , pp. 9309-9317
    • Taylor, A.M.1    Farrar, C.E.2    Jarrett, J.T.3
  • 78
    • 64849087619 scopus 로고    scopus 로고
    • Protein residues that control the reaction trajectory in S-adenosylmethionine radical enzymes: Mutagenesis of asparagine 153 and aspartate 155 in Escherichia coli biotin synthase
    • C.E. Farrar, and J.T. Jarrett Protein residues that control the reaction trajectory in S-adenosylmethionine radical enzymes: mutagenesis of asparagine 153 and aspartate 155 in Escherichia coli biotin synthase Biochemistry 48 2009 2448 2458
    • (2009) Biochemistry , vol.48 , pp. 2448-2458
    • Farrar, C.E.1    Jarrett, J.T.2
  • 79
    • 78649312971 scopus 로고    scopus 로고
    • Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules
    • C.E. Farrar, K.K.W. Siu, P.L. Howell, and J.T. Jarrett Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules Biochemistry 49 2010 9985 9996
    • (2010) Biochemistry , vol.49 , pp. 9985-9996
    • Farrar, C.E.1    Siu, K.K.W.2    Howell, P.L.3    Jarrett, J.T.4
  • 80
    • 80052738180 scopus 로고    scopus 로고
    • Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase
    • A.M. Taylor, S. Stoll, R.D. Britt, and J.T. Jarrett Reduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9- mercaptodethiobiotin in Escherichia coli biotin synthase Biochemistry 50 2011 7953 7963
    • (2011) Biochemistry , vol.50 , pp. 7953-7963
    • Taylor, A.M.1    Stoll, S.2    Britt, R.D.3    Jarrett, J.T.4
  • 82
    • 0037132531 scopus 로고    scopus 로고
    • The PLP-dependent biotin synthase from Escherichia coli: Mechanistic studies
    • S. Ollagnier de Choudens, E. Mulliez, and M. Fontecave The PLP-dependent biotin synthase from Escherichia coli: mechanistic studies FEBS Lett. 532 2002 465 468
    • (2002) FEBS Lett. , vol.532 , pp. 465-468
    • Ollagnier De Choudens, S.1    Mulliez, E.2    Fontecave, M.3
  • 83
    • 19544377011 scopus 로고    scopus 로고
    • A nucleosidase required for in vivo function of the S-adenosyl-l- methionine radical enzyme, biotin synthase
    • E. Choi-Rhee, and J.E. Cronan A nucleosidase required for in vivo function of the S-adenosyl-l-methionine radical enzyme, biotin synthase Chem. Biol. 12 2005 589 593
    • (2005) Chem. Biol. , vol.12 , pp. 589-593
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 84
    • 0002226173 scopus 로고
    • Thermochemistry and kinetics of sulfur-containing molecules and radicals
    • S.W. Bensen Thermochemistry and kinetics of sulfur-containing molecules and radicals Chem. Rev. 78 1978 23 35
    • (1978) Chem. Rev. , vol.78 , pp. 23-35
    • Bensen, S.W.1
  • 85
    • 0037393779 scopus 로고    scopus 로고
    • Bond dissociation energies of organic molecules
    • S.J. Blanksby, and G.B. Ellison Bond dissociation energies of organic molecules Acc. Chem. Res. 36 2003 255 263
    • (2003) Acc. Chem. Res. , vol.36 , pp. 255-263
    • Blanksby, S.J.1    Ellison, G.B.2
  • 87
    • 0034743723 scopus 로고    scopus 로고
    • Ab-initio molecular geometry and normal coordinate analysis of tetrahydrothiophene molecule
    • T.M. El-Gogary Ab-initio molecular geometry and normal coordinate analysis of tetrahydrothiophene molecule Spectrochim. Acta A Mol. Biomol. Spectrosc. 57 2001 1405 1415
    • (2001) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.57 , pp. 1405-1415
    • El-Gogary, T.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.