메뉴 건너뛰기




Volumn 40, Issue 3, 2012, Pages 523-530

The prototypic class Ia ribonucleotide reductase from Escherichia coli: Still surprising after all these years

Author keywords

Allostery; Conformational equilibrium; Feedback regulation; Nucleotide biosynthesis; Oligomerization; Protein protein interaction

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; OLIGOMER; RIBONUCLEOTIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE CLASS IA; TYROSINE; UNCLASSIFIED DRUG;

EID: 84861500520     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120081     Document Type: Conference Paper
Times cited : (11)

References (53)
  • 1
    • 82755165376 scopus 로고    scopus 로고
    • Increase in dNTP pool size during the DNA damage response plays a key role in spontaneous and induced-mutagenesis in Escherichia coli
    • Gon, S., Napolitano, R., Rocha, W., Coulon, S. and Fuchs, R.P. (2011) Increase in dNTP pool size during the DNA damage response plays a key role in spontaneous and induced-mutagenesis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 108, 19311-19316
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19311-19316
    • Gon, S.1    Napolitano, R.2    Rocha, W.3    Coulon, S.4    Fuchs, R.P.5
  • 3
    • 27844495735 scopus 로고    scopus 로고
    • Stimulation of mutagenesis by proportional deoxyribonucleoside triphosphate accumulation in Escherichia coli
    • DOI 10.1016/j.dnarep.2005.09.003, PII S1568786405002545
    • Wheeler, L.J., Rajagopal, I. and Mathews, C.K. (2005) Stimulation of mutagenesis by proportional deoxyribonucleoside triphosphate accumulation in Escherichia coli. DNA Repair 4, 1450-1456 (Pubitemid 41653306)
    • (2005) DNA Repair , vol.4 , Issue.12 , pp. 1450-1456
    • Wheeler, L.J.1    Rajagopal, I.2    Mathews, C.K.3
  • 4
    • 33749263031 scopus 로고    scopus 로고
    • Discovery and development of clofarabine: A nucleoside analogue for treating cancer
    • DOI 10.1038/nrd2055, PII NRD2055
    • Bonate, P.L., Arthaud, L., Cantrell, Jr, W.R., Stephenson, K., Secrist, 3rd, J.A. and Weitman, S. (2006) Discovery and development of clofarabine: a nucleoside analogue for treating cancer. Nat. Rev. Drug Discovery 5, 855-863 (Pubitemid 44480539)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.10 , pp. 855-863
    • Bonate, P.L.1    Arthaud, L.2    Cantrell, W.R.3    Stephenson, K.4    Secrist, J.A.5    Weitman, S.6
  • 5
    • 0025325071 scopus 로고
    • Evaluation of the antitumor activity of Gemcitabine (2',2'-difluoro-2'- deoxycytidine)
    • Hertel, L.W., Boder, G.B., Kroin, J.S., Rinzel, S.M., Poore, G.A., Todd, G.C. and Grindey, G.B. (1990) Evaluation of the antitumor activity of gemcitabine (2′,2′-difluoro-2′-deoxycytidine). Cancer Res. 50, 4417-4422 (Pubitemid 20225688)
    • (1990) Cancer Research , vol.50 , Issue.14 , pp. 4417-4422
    • Hertel, L.W.1    Boder, G.B.2    Kroin, J.S.3    Rinzel, S.M.4    Poore, G.A.5    Todd, G.C.6    Grindey, G.B.7
  • 6
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan, D.T., Andersson, J., Sjöberg, B.M. and Nordlund, P. (1999) A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science 283, 1499-1504
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1    Andersson, J.2    Sjöberg, B.M.3    Nordlund, P.4
  • 7
    • 0036219377 scopus 로고    scopus 로고
    • The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer
    • DOI 10.1038/nsb774
    • Sintchak, M.D., Arjara, G., Kellogg, B.A., Stubbe, J. and Drennan, C.L. (2002) The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Nat. Struct. Biol. 9, 293-300 (Pubitemid 34289903)
    • (2002) Nature Structural Biology , vol.9 , Issue.4 , pp. 293-300
    • Sintchak, M.D.1    Arjara, G.2    Kellogg, B.A.3    Stubbe, J.4    Drennan, C.L.5
  • 8
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • DOI 10.1038/370533a0
    • Uhlin, U. and Eklund, H. (1994) Structure of ribonucleotide reductase protein R1. Nature 370, 533-539 (Pubitemid 24264919)
    • (1994) Nature , vol.370 , Issue.6490 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 9
    • 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 (Pubitemid 26044465)
    • (1996) Science , vol.271 , Issue.5248 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 10
    • 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, Jr, J.M., 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
  • 11
    • 79953305717 scopus 로고    scopus 로고
    • Class I ribonucleotide reductases: Metallocofactor assembly and repair in vitro and in vivo
    • Cotruvo, J.A. and Stubbe, J. (2011) Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo. Annu. Rev. Biochem. 80, 733-767
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 733-767
    • Cotruvo, J.A.1    Stubbe, J.2
  • 13
    • 0021021913 scopus 로고
    • Characterization of the mRNA coding for ribonucleoside diphosphate reductase in Escherichia coli
    • Hanke, P.D. and Fuchs, J.A. (1983) Characterization of the mRNA coding for ribonucleoside diphosphate reductase in Escherichia coli. J. Bacteriol. 156, 1192-1197 (Pubitemid 14216345)
    • (1983) Journal of Bacteriology , vol.156 , Issue.3 , pp. 1192-1197
    • Hanke, P.D.1    Fuchs, J.A.2
  • 14
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • DOI 10.1016/S0968-0004(98)01296-1, PII S0968000498012961
    • Stubbe, J. and Riggs-Gelasco, P. (1998) Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase. Trends Biochem. Sci. 23, 438-443 (Pubitemid 28540745)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.11 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 15
    • 0018135309 scopus 로고
    • The tyrosine free radical in ribonucleotide reductase from Escherichia coli
    • Sjöberg, B.M., Reichard, P., Gräslund, A. and Ehrenberg, A. (1978) The tyrosine free radical in ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 253, 6863-6865 (Pubitemid 9068491)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.19 , pp. 6863-6865
    • Sjoberg, B.M.1    Reichard, P.2    Graslund, A.3    Ehrenberg, A.4
  • 16
    • 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
  • 17
    • 0038208381 scopus 로고    scopus 로고
    • Radical initiation in the class I ribonucleotide reductase: Long-range proton-coupled electron transfer?
    • Stubbe, J., Nocera, D.G., Yee, C.S. and Chang, M.C. (2003) Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer? Chem. Rev. 103, 2167-2201
    • (2003) Chem. Rev. , vol.103 , pp. 2167-2201
    • Stubbe, J.1    Nocera, D.G.2    Yee, C.S.3    Chang, M.C.4
  • 18
    • 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
  • 20
    • 79959241252 scopus 로고    scopus 로고
    • Kinetics of radical intermediate formation and deoxynucleotide production in 3-aminotyrosine-substituted Escherichia coli ribonucleotide reductases
    • Minnihan, E.C., Seyedsayamdost, M.R., Uhlin, U. and Stubbe, J. (2011) Kinetics of radical intermediate formation and deoxynucleotide production in 3-aminotyrosine-substituted Escherichia coli ribonucleotide reductases. J. Am. Chem. Soc. 133, 9430-9440
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 9430-9440
    • Minnihan, E.C.1    Seyedsayamdost, M.R.2    Uhlin, U.3    Stubbe, J.4
  • 21
    • 36849004028 scopus 로고    scopus 로고
    • 731 in radical propagation
    • DOI 10.1021/ja076043y
    • Seyedsayamdost, M.R., Xie, J., Chan, C.T., Schultz, P.G. and Stubbe, J. (2007) Site-specific insertion of 3-aminotyrosine into subunit α2 of E. coli ribonucleotide reductase: direct evidence for involvement of Y730 and Y731 in radical propagation. J. Am. Chem. Soc. 129, 15060-15071 (Pubitemid 350230727)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.48 , pp. 15060-15071
    • Seyedsayamdost, M.R.1    Xie, J.2    Chan, C.T.Y.3    Schultz, P.G.4    Stubbe, J.5
  • 22
    • 0023655427 scopus 로고
    • Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli
    • Sjöberg, B.M., Karlsson, M. and Jörnvall, H. (1987) Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 262, 9736-9743
    • (1987) J. Biol. Chem. , vol.262 , pp. 9736-9743
    • Sjöberg, B.M.1    Karlsson, M.2    Jörnvall, H.3
  • 23
    • 0025851264 scopus 로고
    • Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: Kinetic analysis of inhibition studies
    • Climent, I., Sjöberg, B.M. and Huang, C.Y. (1991) Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: kinetic analysis of inhibition studies. Biochemistry 30, 5164-5171
    • (1991) Biochemistry , vol.30 , pp. 5164-5171
    • Climent, I.1    Sjöberg, B.M.2    Huang, C.Y.3
  • 24
    • 32244433011 scopus 로고    scopus 로고
    • 356 is a redox-active amino acid along the radical propagation pathway
    • DOI 10.1021/ja055927j
    • Seyedsayamdost, M.R., Yee, C.S., Reece, S.Y., Nocera, D.G. and Stubbe, J. (2006) pH rate profiles of FnY356-R2s (n = 2, 3, 4) in Escherichia coli ribonucleotide reductase: evidence that Y356 is a redox-active amino acid along the radical propagation pathway. J. Am. Chem. Soc. 128, 1562-1568 (Pubitemid 43214868)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.5 , pp. 1562-1568
    • Seyedsayamdost, M.R.1    Yee, C.S.2    Reece, S.Y.3    Nocera, D.G.4    Stubbe, J.5
  • 25
    • 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
  • 26
    • 0016257826 scopus 로고
    • Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli: Oxidation-reduction-active disulfides in the B1 subunit
    • Thelander, L. (1974) Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli: oxidation-reduction-active disulfides in the B1 subunit. J. Biol. Chem. 249, 4858-4862
    • (1974) J. Biol. Chem. , vol.249 , pp. 4858-4862
    • Thelander, L.1
  • 27
    • 0014694297 scopus 로고
    • Role of effector binding in allosteric control of ribonucleoside diphosphate reductase
    • Brown, N.C. and Reichard, P. (1969) Role of effector binding in allosteric control of ribonucleoside diphosphate reductase. J. Mol. Biol. 46, 39-55
    • (1969) J. Mol. Biol. , vol.46 , pp. 39-55
    • Brown, N.C.1    Reichard, P.2
  • 28
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • Eriksson, M., Uhlin, U., Ramaswamy, S., Ekberg, M., Regnström, K., Sjöberg, B.M. and Eklund, H. (1997) Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 5, 1077-1092 (Pubitemid 27393092)
    • (1997) Structure , vol.5 , Issue.8 , pp. 1077-1092
    • Eriksson, M.1    Uhlin, U.2    Ramaswamy, S.3    Ekberg, M.4    Regnstrom, K.5    Sjoberg, B.-M.6    Eklund, H.7
  • 30
    • 0034886973 scopus 로고    scopus 로고
    • Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases
    • DOI 10.1016/S0969-2126(01)00627-X, PII S096921260100627X
    • Larsson, K.M., Andersson, J., Sjöberg, B.M., Nordlund, P. and Logan, D.T. (2001) Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases. Structure 9, 739-750 (Pubitemid 32772896)
    • (2001) Structure , vol.9 , Issue.8 , pp. 739-750
    • Larsson, K.-M.1    Andersson, J.2    Sjoberg, B.-M.3    Nordlund, P.4    Logan, D.T.5
  • 32
    • 0015850211 scopus 로고
    • Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli
    • Thelander, L. (1973) Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli. J. Biol. Chem. 248, 4591-4601
    • (1973) J. Biol. Chem. , vol.248 , pp. 4591-4601
    • Thelander, L.1
  • 33
    • 0014694233 scopus 로고
    • Ribonucleoside diphosphate reductase: Formation of active and inactive complexes of proteins B1 and B2
    • Brown, N.C. and Reichard, P. (1969) Ribonucleoside diphosphate reductase: formation of active and inactive complexes of proteins B1 and B2. J. Mol. Biol. 46, 25-38
    • (1969) J. Mol. Biol. , vol.46 , pp. 25-38
    • Brown, N.C.1    Reichard, P.2
  • 34
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase
    • DOI 10.1074/jbc.271.34.20655
    • 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 (Pubitemid 26281846)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20655-20659
    • Ekberg, M.1    Sahlin, M.2    Eriksson, M.3    Sjoberg, B.-M.4
  • 35
    • 0028963767 scopus 로고
    • Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase
    • Rova, U., Goodtzova, K., Ingemarson, R., Behravan, G., 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, G.4    Gräslund, A.5    Thelander, L.6
  • 36
    • 0022763898 scopus 로고
    • Identification of the stable free radical tyrosine residue in ribonucleotide reductase
    • Larsson, A. and Sjöberg, B.M. (1986) Identification of the stable free radical tyrosine residue in ribonucleotide reductase. EMBO J. 5, 2037-2040
    • (1986) EMBO J. , vol.5 , pp. 2037-2040
    • Larsson, A.1    Sjöberg, B.M.2
  • 37
    • 37549042071 scopus 로고    scopus 로고
    • PELDOR spectroscopy with DOPA-β2 and NH2Y-α2s: Distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase
    • Seyedsayamdost, M.R., Chan, C.T., Mugnaini, V., Stubbe, J. and Bennati, M. (2007) PELDOR spectroscopy with DOPA-β2 and NH2Y-α2s: distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 129, 15748-15749
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15748-15749
    • Seyedsayamdost, M.R.1    Chan, C.T.2    Mugnaini, V.3    Stubbe, J.4    Bennati, M.5
  • 39
    • 58149091633 scopus 로고    scopus 로고
    • Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase
    • Rofougaran, R., Crona, M., Vodnala, M., Sjöberg, B.M. and Hofer, A. (2008) Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase. J. Biol. Chem. 283, 35310-35318
    • (2008) J. Biol. Chem. , vol.283 , pp. 35310-35318
    • Rofougaran, R.1    Crona, M.2    Vodnala, M.3    Sjöberg, B.M.4    Hofer, A.5
  • 40
    • 52449131059 scopus 로고    scopus 로고
    • Electron transfer and electronic conduction through an intervening medium
    • Edwards, P.P., Gray, H.B., Lodge, M.T. and Williams, R.J. (2008) Electron transfer and electronic conduction through an intervening medium. Angew. Chem. Int. Ed. 47, 6758-6765
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 6758-6765
    • Edwards, P.P.1    Gray, H.B.2    Lodge, M.T.3    Williams, R.J.4
  • 41
    • 33645239831 scopus 로고    scopus 로고
    • Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation
    • Xu, H., Faber, C., Uchiki, T., Fairman, J.W., Racca, J. and Dealwis, C. (2006) Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation. Proc. Natl. Acad. Sci. U.S.A. 103, 4022-4027
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4022-4027
    • Xu, H.1    Faber, C.2    Uchiki, T.3    Fairman, J.W.4    Racca, J.5    Dealwis, C.6
  • 43
    • 0037452529 scopus 로고    scopus 로고
    • Comprehensive model for allosteric regulation of mammalian ribonucleotide reductase: Refinements and consequences
    • DOI 10.1021/bi020634d
    • Kashlan, O.B. and Cooperman, B.S. (2003) Comprehensive model for allosteric regulation of mammalian ribonucleotide reductase: refinements and consequences. Biochemistry 42, 1696-1706 (Pubitemid 36205978)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1696-1706
    • Kashlan, O.B.1    Cooperman, B.S.2
  • 44
    • 0034693148 scopus 로고    scopus 로고
    • Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase
    • Reichard, P., Eliasson, R., Ingemarson, R. and Thelander, L. (2000) Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase. J. Biol. Chem. 275, 33021-33026
    • (2000) J. Biol. Chem. , vol.275 , pp. 33021-33026
    • Reichard, P.1    Eliasson, R.2    Ingemarson, R.3    Thelander, L.4
  • 45
    • 0018786927 scopus 로고
    • Allosteric regulation of calf thymus ribonucleoside diphosphate reductase
    • Eriksson, S., Thelander, L. and Akerman, M. (1979) Allosteric regulation of calf thymus ribonucleoside diphosphate reductase. Biochemistry 18, 2948-2952 (Pubitemid 9245448)
    • (1979) Modern Medicine of New Zealand , vol.12 , Issue.6 , pp. 2948-2952
    • Eriksson, S.1    Thelander, L.2    Akerman, M.3
  • 46
    • 79959966626 scopus 로고    scopus 로고
    • Clofarabine 5′-di and -triphosphates inhibit human ribonucleotide reductase by altering the quaternary structure of its large subunit
    • Aye, Y. and Stubbe, J. (2011) Clofarabine 5′-di and -triphosphates inhibit human ribonucleotide reductase by altering the quaternary structure of its large subunit. Proc. Natl. Acad. Sci. U.S.A. 108, 9815-9820
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9815-9820
    • Aye, Y.1    Stubbe, J.2
  • 47
    • 33748785426 scopus 로고    scopus 로고
    • 2 octamer
    • DOI 10.1074/jbc.M605573200
    • Rofougaran, R., Vodnala, M. and Hofer, A. (2006) Enzymatically active mammalian ribonucleotide reductase exists primarily as an α6β2 octamer. J. Biol. Chem. 281, 27705-27711 (Pubitemid 44414484)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 27705-27711
    • Rofougaran, R.1    Vodnala, M.2    Hofer, A.3
  • 48
    • 0019321430 scopus 로고
    • Ribonucleotide reductase from calf thymus: Separation of the enzyme into two nonidentical subunits, proteins M1 and M2
    • Thelander, L., Eriksson, S. and Akerman, M. (1980) Ribonucleotide reductase from calf thymus: separation of the enzyme into two nonidentical subunits, proteins M1 and M2. J. Biol. Chem. 255, 7426-7432
    • (1980) J. Biol. Chem. , vol.255 , pp. 7426-7432
    • Thelander, L.1    Eriksson, S.2    Akerman, M.3
  • 50
    • 27544491667 scopus 로고    scopus 로고
    • EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase
    • DOI 10.1021/ja054991y
    • 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 (Pubitemid 41547354)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.43 , pp. 15014-15015
    • Bennati, M.1    Robblee, J.H.2    Mugnaini, V.3    Stubbe, J.4    Freed, J.H.5    Borbat, P.6
  • 51
    • 0041823734 scopus 로고    scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of E. coli class I ribonucleotide reductase
    • DOI 10.1021/bi034374r
    • 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, 10071-10083 (Pubitemid 37052027)
    • (2003) Biochemistry , vol.42 , Issue.34 , pp. 10071-10083
    • Ge, J.1    Yu, G.2    Ator, M.A.3    Stubbe, J.4
  • 52
    • 0035859842 scopus 로고    scopus 로고
    • Kinetics in the pre-steady state of the formation of cystines in ribonucleoside diphosphate reductase: Evidence for an asymmetric complex
    • Erickson, H.K. (2001) Kinetics in the pre-steady state of the formation of cystines in ribonucleoside diphosphate reductase: evidence for an asymmetric complex. Biochemistry 40, 9631-9637
    • (2001) Biochemistry , vol.40 , pp. 9631-9637
    • Erickson, H.K.1
  • 53
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D. and Svergun, D.I. (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.