메뉴 건너뛰기




Volumn 47, Issue 52, 2008, Pages 13736-13744

Formation and function of the manganese(iv)/iron(iii) cofactor in chlamydia trachomatis ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDIA TRACHOMATIS; CLASS I; COFACTORS; DIPHOSPHATES; HETEROBINUCLEAR; HYDROGEN ATOMS; METAL CLUSTER; NEAR-SURFACE; ONE-ELECTRON REDUCTIONS; PROTON COUPLED ELECTRON TRANSFERS; RIBONUCLEOSIDES; RIBONUCLEOTIDE REDUCTASE; STABLE RADICALS; THIYL RADICALS;

EID: 58849139303     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi8017625     Document Type: Review
Times cited : (49)

References (70)
  • 1
    • 0000289664 scopus 로고    scopus 로고
    • Mechanistic investigations of ribonucleotide reductases
    • (Poulter, C. D., Ed.) Elsevier, New York
    • Licht, S., and Stubbe, J. (1999) Mechanistic investigations of ribonucleotide reductases. In Comprehensive natural products chemistry (Poulter, C. D., Ed.) pp 163-203, Elsevier, New York.
    • (1999) Comprehensive Natural Products Chemistry , pp. 163-203
    • Licht, S.1    Stubbe, J.2
  • 3
    • 0031106730 scopus 로고    scopus 로고
    • The evolution of ribonucleotide reduction
    • Reichard, P. (1997) The evolution of ribonucleotide reduction. Trends Biochem. Sci. 22, 81-85.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 81-85
    • Reichard, P.1
  • 4
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe, J., and van der Donk, W. A. (1998) Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762.
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 5
    • 0026788358 scopus 로고
    • Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: Evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity
    • Mao, S. S., Yu, G. X., Chalfoun, D., and Stubbe, J. (1992) Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: Evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity. Biochemistry 31, 9752-9759.
    • (1992) Biochemistry , vol.31 , pp. 9752-9759
    • Mao, S.S.1    Yu, G.X.2    Chalfoun, D.3    Stubbe, J.4
  • 6
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing
    • Mao, S. S., Holler, T. P., Yu, G. X., Bollinger, J. M., Jr., Booker, S., Johnston, M. I., and Stubbe, J. (1992) A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing. Biochemistry 31, 9733-9743.
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Holler, T.P.2    Yu, G.X.3    Bollinger Jr., J.M.4    Booker, S.5    Johnston, M.I.6    Stubbe, J.7
  • 7
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., Gerfen, G. J., and Stubbe, J. (1996) Thiyl radicals in ribonucleotide reductases. Science 271, 477-481.
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 8
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U., and Eklund, H. (1994) Structure of ribonucleotide reductase protein R1. Nature 370, 533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 9
    • 0019182317 scopus 로고
    • On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli
    • Stubbe, J., and Ackles, D. (1980) On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. J. Biol. Chem. 255, 8027-8030.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8027-8030
    • Stubbe, J.1    Ackles, D.2
  • 10
    • 0041823734 scopus 로고    scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of E. coli class i ribonucleotide reductase
    • Ge, J., Yu, G., Ator, M. A., and Stubbe, J. (2003) Pre-steady-state and steady-state kinetic analysis of E. coli class I ribonucleotide reductase. Biochemistry 42, 10017-10083.
    • (2003) Biochemistry , vol.42 , pp. 10017-10083
    • Ge, J.1    Yu, G.2    Ator, M.A.3    Stubbe, J.4
  • 11
    • 0033603831 scopus 로고    scopus 로고
    • Class II ribonucleotide reductases catalyze carbon-cobalt bond reformation on every turnover
    • Licht, S. S., Lawrence, C. C., and Stubbe, J. (1999) Class II ribonucleotide reductases catalyze carbon-cobalt bond reformation on every turnover. J. Am. Chem. Soc. 121, 7463-7468.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7463-7468
    • Licht, S.S.1    Lawrence, C.C.2    Stubbe, J.3
  • 12
    • 0038208381 scopus 로고    scopus 로고
    • Radical initiation in the class i ribonucleotide reductase: Longrange proton-coupled electron transfer?
    • Stubbe, J., Nocera, D. G., Yee, C. S., and Chang, M. C. Y. (2003) Radical initiation in the class I ribonucleotide reductase: Longrange proton-coupled electron transfer? Chem. Rev. 103, 2167-2202.
    • (2003) Chem. Rev. , vol.103 , pp. 2167-2202
    • Stubbe, J.1    Nocera, D.G.2    Yee, C.S.3    Chang, M.C.Y.4
  • 13
    • 0037396273 scopus 로고    scopus 로고
    • Di-iron-tyrosyl radical ribonucleotide reductases
    • Stubbe, J. (2003) Di-iron-tyrosyl radical ribonucleotide reductases. Curr. Opin. Chem. Biol. 7, 183-188.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 183-188
    • Stubbe, J.1
  • 14
    • 0037080335 scopus 로고    scopus 로고
    • A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- And dATP-induced oligomerization of the large subunit
    • Kashlan, O. B., Scott, C. P., Lear, J. D., and Cooperman, B. S. (2002) A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit. Biochemistry 41, 462-474.
    • (2002) Biochemistry , vol.41 , pp. 462-474
    • Kashlan, O.B.1    Scott, C.P.2    Lear, J.D.3    Cooperman, B.S.4
  • 15
    • 0034528765 scopus 로고    scopus 로고
    • Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis
    • Roshick, C., Iliffe-Lee, E. R., and McClarty, G. (2000) Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis. J. Biol. Chem. 275, 38111-38119.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38111-38119
    • Roshick, C.1    Iliffe-Lee, E.R.2    McClarty, G.3
  • 16
    • 3042728737 scopus 로고    scopus 로고
    • The radical site in Chlamydial, ribonucleotide reductase defines a new R2 subclass
    • Högbom, M., Stenmark, P., Voevodskaya, N., McClarty, G., Gräslund, A., and Nordlund, P. (2004) The radical site in Chlamydial, ribonucleotide reductase defines a new R2 subclass. Science 305, 245-248.
    • (2004) Science , vol.305 , pp. 245-248
    • Högbom, M.1    Stenmark, P.2    Voevodskaya, N.3    McClarty, G.4    Gräslund, A.5    Nordlund, P.6
  • 19
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • Bollinger, J. M., Jr., Edmondson, D. E., Huynh, B. H., Filley, J., Norton, J. R., and Stubbe, J. (1991) Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science 253, 292-298.
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger Jr., J.M.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, J.4    Norton, J.R.5    Stubbe, J.6
  • 20
    • 41449098456 scopus 로고    scopus 로고
    • Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase
    • Hristova, D., Wu, C.-H., Jiang, W., Krebs, C., and Stubbe, J. (2008) Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase. Biochemistry 47, 3989-3999.
    • (2008) Biochemistry , vol.47 , pp. 3989-3999
    • Hristova, D.1    Wu, C.-H.2    Jiang, W.3    Krebs, C.4    Stubbe, J.5
  • 21
    • 35348849676 scopus 로고    scopus 로고
    • YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase
    • Wu, C.-H., Jiang, W., Krebs, C., and Stubbe, J. (2007) YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase. Biochemistry 46, 11577-11588.
    • (2007) Biochemistry , vol.46 , pp. 11577-11588
    • Wu, C.-H.1    Jiang, W.2    Krebs, C.3    Stubbe, J.4
  • 22
    • 47349123990 scopus 로고    scopus 로고
    • NrdI essentiality for class Ib ribonucleotide reduction in Streptococcus pyogenes
    • Roca, I., Torrents, E., Sahlin, M., Gibert, I., and Sjöberg, B.-M. (2008) NrdI essentiality for class Ib ribonucleotide reduction in Streptococcus pyogenes. J. Bacteriol. 190, 4849-4858.
    • (2008) J. Bacteriol. , vol.190 , pp. 4849-4858
    • Roca, I.1    Torrents, E.2    Sahlin, M.3    Gibert, I.4    Sjöberg, B.-M.5
  • 23
    • 55749110597 scopus 로고    scopus 로고
    • NrdI, an unusual flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • Cotruvo, J. A., Jr., and Stubbe, J. (2008) NrdI, an unusual flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 105, 14383-14388.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14383-14388
    • Cotruvo Jr., J.A.1    Stubbe, J.2
  • 25
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase
    • Sturgeon, B. E., Burdi, D., Chen, S., Huynh, B. H., Edmondson, D. E., Stubbe, J., and Hoffman, B. M. (1996) Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase. J. Am. Chem. Soc. 118, 7551-7557.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7551-7557
    • Sturgeon, B.E.1    Burdi, D.2    Chen, S.3    Huynh, B.H.4    Edmondson, D.E.5    Stubbe, J.6    Hoffman, B.M.7
  • 26
    • 0032506972 scopus 로고    scopus 로고
    • EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor
    • Riggs-Gelasco, P. J., Shu, L., Chen, S., Burdi, D., Huynh, B. H., Que, L., Jr., and Stubbe, J. (1998) EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor. J. Am. Chem. Soc. 120, 849-860.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 849-860
    • Riggs-Gelasco, P.J.1    Shu, L.2    Chen, S.3    Burdi, D.4    Huynh, B.H.5    Que Jr., L.6    Stubbe, J.7
  • 29
    • 33750337763 scopus 로고    scopus 로고
    • Density functional theory study of Fe(IV) d-d optical transitions in activesite models of class i ribonucleotide reductase intermediate X with vertical self-consistent reaction field methods
    • Han, W.-C., Liu, T., Lovell, T., and Noodleman, L. (2006) Density functional theory study of Fe(IV) d-d optical transitions in activesite models of class I ribonucleotide reductase intermediate X with vertical self-consistent reaction field methods. Inorg. Chem. 45, 8533-8542.
    • (2006) Inorg. Chem. , vol.45 , pp. 8533-8542
    • Han, W.-C.1    Liu, T.2    Lovell, T.3    Noodleman, L.4
  • 31
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • Baldwin, J., Krebs, C., Ley, B. A., Edmondson, D. E., Huynh, B. H., and Bollinger, J. M., Jr. (2000) Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical. J. Am. Chem. Soc. 122, 12195-12206.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 32
    • 0029987181 scopus 로고    scopus 로고
    • Mechanism of assembly of the diferric cluster-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase from the diferrous form of the R2 subunit
    • Tong, W. H., Chen, S., Lloyd, S. C., Edmondson, D. E., Huynh, B. H., and Stubbe, J. (1996) Mechanism of assembly of the diferric cluster-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase from the diferrous form of the R2 subunit. J. Am. Chem. Soc. 118, 2107-2108.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2107-2108
    • Tong, W.H.1    Chen, S.2    Lloyd, S.C.3    Edmondson, D.E.4    Huynh, B.H.5    Stubbe, J.6
  • 33
    • 0029379564 scopus 로고
    • Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Liu, K. E., Valentine, A. M., Wang, D., Huynh, B. H., Edmondson, D. E., Salifoglou, A., and Lippard, S. J. (1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J. Am. Chem. Soc. 117, 10174-10185.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10174-10185
    • Liu, K.E.1    Valentine, A.M.2    Wang, D.3    Huynh, B.H.4    Edmondson, D.E.5    Salifoglou, A.6    Lippard, S.J.7
  • 36
    • 33847058857 scopus 로고    scopus 로고
    • (μ-1,2-Peroxo)diiron(III/ III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse
    • Yun, D., García-Serres, R., Chicalese, B. M., An, Y. H., Huynh, B. H., and Bollinger, J. M., Jr. (2007) (μ-1,2-Peroxo)diiron(III/ III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry 46, 1925-1932.
    • (2007) Biochemistry , vol.46 , pp. 1925-1932
    • Yun, D.1    García-Serres, R.2    Chicalese, B.M.3    An, Y.H.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 37
    • 2442664147 scopus 로고    scopus 로고
    • Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase
    • Saleh, L., Krebs, C., Ley, B. A., Naik, S., Huynh, B. H., and Bollinger, J. M., Jr. (2004) Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase. Biochemistry 43, 5953-5964.
    • (2004) Biochemistry , vol.43 , pp. 5953-5964
    • Saleh, L.1    Krebs, C.2    Ley, B.A.3    Naik, S.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 38
    • 0344236128 scopus 로고    scopus 로고
    • Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl radicals in the R2 subunit of the E. coli ribonucleotide reductase
    • Bennati, M., Weber, A., Antonic, J., Perlstein, D. L., Robblee, J. H., and Stubbe, J. (2003) Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl radicals in the R2 subunit of the E. coli ribonucleotide reductase. J. Am. Chem. Soc. 125, 14988-14989.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14988-14989
    • Bennati, M.1    Weber, A.2    Antonic, J.3    Perlstein, D.L.4    Robblee, J.H.5    Stubbe, J.6
  • 39
    • 27544491667 scopus 로고    scopus 로고
    • EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase
    • Bennati, M., Robblee, J. H., Mugnaini, V., Stubbe, J., Freed, J. H., and Borbat, P. (2005) EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase. J. Am. Chem. Soc. 127, 15014-15015.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15014-15015
    • Bennati, M.1    Robblee, J.H.2    Mugnaini, V.3    Stubbe, J.4    Freed, J.H.5    Borbat, P.6
  • 40
    • 0026652152 scopus 로고
    • Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction
    • Climent, I., Sjöberg, B.-M., and Huang, C. Y. (1992) Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction. Biochemistry 31, 4801-4807.
    • (1992) Biochemistry , vol.31 , pp. 4801-4807
    • Climent, I.1    Sjöberg, B.-M.2    Huang, C.Y.3
  • 41
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase
    • Ekberg, M., Sahlin, M., Eriksson, M., and Sjöberg, B.-M. (1996) Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase. J. Biol. Chem. 271, 20655-20659.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20655-20659
    • Ekberg, M.1    Sahlin, M.2    Eriksson, M.3    Sjöberg, B.-M.4
  • 42
    • 0028963767 scopus 로고
    • Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase
    • Rova, U., Goodtzova, K., Ingemarson, R., Behravan, C., Gräslund, A., and Thelander, L. (1995) Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase. Biochemistry 34, 4267-4275.
    • (1995) Biochemistry , vol.34 , pp. 4267-4275
    • Rova, U.1    Goodtzova, K.2    Ingemarson, R.3    Behravan, C.4    Gräslund, A.5    Thelander, L.6
  • 43
    • 0033588374 scopus 로고    scopus 로고
    • 370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway
    • 370 of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway. J. Biol. Chem. 274, 23746-23751.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23746-23751
    • Rova, U.1    Adrait, A.2    Pötsch, S.3    Gräslund, A.4    Thelander, L.5
  • 44
    • 33746263668 scopus 로고    scopus 로고
    • 2 activation by protein R2 of Escherichia coli ribonucleotide reductase: Relevance to R1-R2 radical transfer in nucleotide reduction
    • 2 activation by protein R2 of Escherichia coli ribonucleotide reductase: Relevance to R1-R2 radical transfer in nucleotide reduction. Biochemistry 45, 8823-8830.
    • (2006) Biochemistry , vol.45 , pp. 8823-8830
    • Saleh, L.1    Bollinger Jr., J.M.2
  • 46
    • 33644647904 scopus 로고    scopus 로고
    • Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the β2 subunit of E. coli ribonucleotide reductase
    • Seyedsayamdost, M. R., and Stubbe, J. (2006) Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the β2 subunit of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 128, 2522-2523.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2522-2523
    • Seyedsayamdost, M.R.1    Stubbe, J.2
  • 47
    • 33847666363 scopus 로고    scopus 로고
    • 356DOPA- β2 heterodimer of E. coli ribonucleotide reductase
    • 356DOPA-β2 heterodimer of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 129, 2226-2227.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2226-2227
    • Seyedsayamdost, M.R.1    Stubbe, J.2
  • 50
    • 34250811950 scopus 로고    scopus 로고
    • The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S=1 ground state
    • Jiang, W., Bollinger, J. M., Jr., and Krebs, C. (2007) The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S=1 ground state. J. Am. Chem. Soc. 129, 7504-7505.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7504-7505
    • Jiang, W.1    Bollinger Jr., J.M.2    Krebs, C.3
  • 51
    • 0015890741 scopus 로고
    • Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme
    • Atkin, C. L., Thelander, L., Reichard, P., and Lang, G. (1973) Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme. J. Biol. Chem. 248, 7464-7472.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7464-7472
    • Atkin, C.L.1    Thelander, L.2    Reichard, P.3    Lang, G.4
  • 53
    • 0017239363 scopus 로고
    • Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2′-substituted ribonucleoside diphosphates
    • Thelander, L., Larsson, B., Hobbs, J., and Eckstein, F. (1976) Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2′-substituted ribonucleoside diphosphates. J. Biol. Chem. 251, 1398-1405.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1398-1405
    • Thelander, L.1    Larsson, B.2    Hobbs, J.3    Eckstein, F.4
  • 54
    • 0021099682 scopus 로고
    • A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxyribonucleoside diphosphates
    • Sjöberg, B.-M., Gräslund, A., and Eckstein, F. (1983) A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxyribonucleoside diphosphates. J. Biol. Chem. 258, 8060-8067.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8060-8067
    • Sjöberg, B.-M.1    Gräslund, A.2    Eckstein, F.3
  • 55
    • 21144470706 scopus 로고    scopus 로고
    • Structure of the nitrogen-centered radical formed during inactivation of E. coli ribonucleotide reductase by 2′-azido-2′-deoxyuridine- 5′-diphosphate: Trapping of the 3′-ketonucleotide
    • Fritscher, J., Artin, E., Wnuk, S., Bar, G., Robblee, J. H., Kacprzak, S., Kaupp, M., Griffin, R. G., Bennati, M., and Stubbe, J. (2005) Structure of the nitrogen-centered radical formed during inactivation of E. coli ribonucleotide reductase by 2′-azido-2′-deoxyuridine-5′- diphosphate: Trapping of the 3′-ketonucleotide. J. Am. Chem. Soc. 127, 7729-7738.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7729-7738
    • Fritscher, J.1    Artin, E.2    Wnuk, S.3    Bar, G.4    Robblee, J.H.5    Kacprzak, S.6    Kaupp, M.7    Griffin, R.G.8    Bennati, M.9    Stubbe, J.10
  • 56
    • 34447282627 scopus 로고    scopus 로고
    • High catalytic activity achieved with a mixed manganeseiron site in protein R2 of Chlamydia ribonucleotide reductase
    • Voevodskaya, N., Lendzian, F., Ehrenberg, A., and Gräslund, A. (2007) High catalytic activity achieved with a mixed manganeseiron site in protein R2 of Chlamydia ribonucleotide reductase. FEBS Lett. 581, 3351-3355.
    • (2007) FEBS Lett. , vol.581 , pp. 3351-3355
    • Voevodskaya, N.1    Lendzian, F.2    Ehrenberg, A.3    Gräslund, A.4
  • 57
    • 57049085691 scopus 로고    scopus 로고
    • The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: Structure, assembly, radical initiation, and evolution
    • DOI: 10.1016/j.sbi.2008.11.007
    • Bollinger, J. M., Jr., Jiang, W., Green, M. T., and Krebs, C. (2008) The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: Structure, assembly, radical initiation, and evolution. Curr. Opin. Struct. Biol., DOI: 10.1016/j.sbi.2008.11.007.
    • (2008) Curr. Opin. Struct. Biol.
    • Bollinger Jr., J.M.1    Jiang, W.2    Green, M.T.3    Krebs, C.4
  • 58
    • 34547616469 scopus 로고    scopus 로고
    • A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase
    • Jiang, W., Hoffart, L. M., Krebs, C., and Bollinger, J. M., Jr. (2007) A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase. Biochemistry 46, 8709-8716.
    • (2007) Biochemistry , vol.46 , pp. 8709-8716
    • Jiang, W.1    Hoffart, L.M.2    Krebs, C.3    Bollinger Jr., J.M.4
  • 59
    • 0000016184 scopus 로고
    • Electronic structure of dimanganese(II, III) and dimanganese(III, IV) complexes and dimanganese catalase enzyme: A general EPR spectral simulation approach
    • Zheng, M., Khangulov, S. V., Dismukes, G. C., and Barynin, V. V. (1994) Electronic structure of dimanganese(II, III) and dimanganese(III, IV) complexes and dimanganese catalase enzyme: A general EPR spectral simulation approach. Inorg. Chem. 33, 382-387.
    • (1994) Inorg. Chem. , vol.33 , pp. 382-387
    • Zheng, M.1    Khangulov, S.V.2    Dismukes, G.C.3    Barynin, V.V.4
  • 61
    • 0027454094 scopus 로고
    • Transient intermediates of the methane monooxygenase catalytic cycle
    • Lee, S. K., Nesheim, J. C,. and Lipscomb, J. D. (1993) Transient intermediates of the methane monooxygenase catalytic cycle. J. Biol. Chem. 268, 21569-21577.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21569-21577
    • Lee, S.K.1    Nesheim, J.C.2    Lipscomb, J.D.3
  • 63
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B.-M., and Eklund, H. (1990) Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598.
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjöberg, B.-M.2    Eklund, H.3
  • 64
    • 0032558402 scopus 로고    scopus 로고
    • Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms
    • Eriksson, M., Jordan, A., and Eklund, H. (1998) Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms. Biochemistry 37, 13359-13369.
    • (1998) Biochemistry , vol.37 , pp. 13359-13369
    • Eriksson, M.1    Jordan, A.2    Eklund, H.3
  • 65
    • 49749105567 scopus 로고    scopus 로고
    • Branched activation and catalysis-specific pathways for electron relay to the manganese/ iron cofactor in ribonucleotide reductase from Chlamydia trachomatis
    • Jiang, W., Saleh, L., Barr, E. W., Xie, J., Maslak Gardner, M., Krebs, C., and Bollinger, J. M., Jr. (2008) Branched activation-and catalysis-specific pathways for electron relay to the manganese/ iron cofactor in ribonucleotide reductase from Chlamydia trachomatis. Biochemistry 47, 8477-8484.
    • (2008) Biochemistry , vol.47 , pp. 8477-8484
    • Jiang, W.1    Saleh, L.2    Barr, E.W.3    Xie, J.4    Maslak Gardner, M.5    Krebs, C.6    Bollinger Jr., J.M.7
  • 66
    • 42049105952 scopus 로고    scopus 로고
    • Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide
    • Jiang, W., Xie, J., Nørgaard, H., Bollinger, J. M., Jr., and Krebs, C. (2008) Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide. Biochemistry 47, 4477-4483.
    • (2008) Biochemistry , vol.47 , pp. 4477-4483
    • Jiang, W.1    Xie, J.2    Nørgaard, H.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 67
  • 68
    • 0023931727 scopus 로고
    • Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme
    • Willing, A., Follmann, H., and Auling, G. (1988) Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme. Eur. J. Biochem. 170, 603-611.
    • (1988) Eur. J. Biochem. , vol.170 , pp. 603-611
    • Willing, A.1    Follmann, H.2    Auling, G.3
  • 69
    • 0034682758 scopus 로고    scopus 로고
    • The active form of the R2F protein of class Ib ribonucleotide reductase from Corynebacterium ammoniagenes is a diferric protein
    • Huque, Y., Fieschi, F., Torrents, E., Gibert, I., Eliasson, R., Reichard, P., Sahlin, M., and Sjöberg, B.-M. (2000) The active form of the R2F protein of class Ib ribonucleotide reductase from Corynebacterium ammoniagenes is a diferric protein. J. Biol. Chem. 275, 25365-25371.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25365-25371
    • Huque, Y.1    Fieschi, F.2    Torrents, E.3    Gibert, I.4    Eliasson, R.5    Reichard, P.6    Sahlin, M.7    Sjöberg, B.-M.8
  • 70
    • 0032507265 scopus 로고    scopus 로고
    • Characterization of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly
    • Valentine, A. M., Tavares, P., Pereira, A. S., Davydov, R., Krebs, C., Hoffman, B. M., Edmondson, D. E., Huynh, B. H., and Lippard, S. J. (1998) Characterization of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly. J. Am. Chem. Soc. 120, 2190-2191.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2190-2191
    • Valentine, A.M.1    Tavares, P.2    Pereira, A.S.3    Davydov, R.4    Krebs, C.5    Hoffman, B.M.6    Edmondson, D.E.7    Huynh, B.H.8    Lippard, S.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.