메뉴 건너뛰기




Volumn 287, Issue 47, 2012, Pages 39686-39697

Bacillus anthracis thioredoxin systems, characterization and role as electron donors for ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRACIS; ANTIMICROBIAL THERAPY; BACILLUS ANTHRACIS; CATALYTIC EFFICIENCIES; CAUSATIVE AGENTS; DISULFIDE REDUCTASE; DITHIOTHREITOL; ELECTRON DONORS; GLUTATHIONES; MONOTHIOL; MORTALITY RATE; NITROBENZOIC ACIDS; REDUCTANTS; RIBONUCLEOTIDE REDUCTASE; THIOREDOXIN REDUCTASE; THIOREDOXINS; WESTERN BLOTS;

EID: 84869211845     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.413427     Document Type: Article
Times cited : (30)

References (63)
  • 1
    • 0037341503 scopus 로고    scopus 로고
    • Bacillus anthracis
    • Spencer, R. C. (2003) Bacillus anthracis. J. Clin. Pathol. 56, 182-187
    • (2003) J. Clin. Pathol. , vol.56 , pp. 182-187
    • Spencer, R.C.1
  • 2
    • 70349559190 scopus 로고    scopus 로고
    • What sets Bacillus anthracis apart from other Bacillus species?
    • Kolstø, A. B., Tourasse, N. J., and Økstad, O. A. (2009) What sets Bacillus anthracis apart from other Bacillus species? Annu. Rev. Microbiol. 63, 451-476
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 451-476
    • Kolstø, A.B.1    Tourasse, N.J.2    Økstad, O.A.3
  • 4
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent, T. C., Moore, E. C., and Reichard, P. (1964) Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J. Biol. Chem. 239, 3436-3444
    • (1964) J. Biol. Chem. , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 5
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér, E. S., and Holmgren, A. (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.1    Holmgren, A.2
  • 6
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren, A. (2000) Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid. Redox Signal 2, 811-820
    • (2000) Antioxid. Redox Signal , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 7
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules - From biology to health and disease
    • DOI 10.1089/ars.2007.9.25
    • Lillig, C. H., and Holmgren, A. (2007) Thioredoxin and related molecules-from biology to health and disease. Antioxid. Redox Signal. 9, 25-47 (Pubitemid 44901873)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.1 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 8
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren, A. (1976) Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. U.S.A. 73, 2275-2279
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 9
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System
    • Fernandes, A. P., and Holmgren, A. (2004) Glutaredoxins. Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6, 63-74 (Pubitemid 38063976)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.1 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 11
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • DOI 10.1074/jbc.272.25.15661
    • Prinz, W. A., Aslund, F., Holmgren, A., and Beckwith, J. (1997) The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272, 15661-15667 (Pubitemid 27265536)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 12
    • 33745807629 scopus 로고    scopus 로고
    • In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli
    • DOI 10.1089/ars.2006.8.735
    • Gon, S., Faulkner, M. J., and Beckwith, J. (2006) In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli . Antioxid. Redox Signal. 8, 735-742 (Pubitemid 44036492)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.5-6 , pp. 735-742
    • Gon, S.1    Faulkner, M.J.2    Beckwith, J.3
  • 13
    • 0031940127 scopus 로고    scopus 로고
    • Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis
    • Scharf, C., Riethdorf, S., Ernst, H., Engelmann, S., Völker, U., and Hecker, M. (1998) Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis. J. Bacteriol. 180, 1869-1877 (Pubitemid 28173069)
    • (1998) Journal of Bacteriology , vol.180 , Issue.7 , pp. 1869-1877
    • Scharf, C.1    Riethdorf, S.2    Ernst, H.3    Engelmann, S.4    Volker, U.5    Hecker, M.6
  • 15
    • 46049117838 scopus 로고    scopus 로고
    • Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis
    • DOI 10.1128/JB.00252-08
    • Möller, M. C., and Hederstedt, L. (2008) Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis. J. Bacteriol. 190, 4660-4665 (Pubitemid 351898983)
    • (2008) Journal of Bacteriology , vol.190 , Issue.13 , pp. 4660-4665
    • Moller, M.C.1    Hederstedt, L.2
  • 16
    • 20444479468 scopus 로고    scopus 로고
    • Tricksy business: Transcriptome analysis reveals the involvement of thioredoxin A in redox homeostasis, oxidative stress, sulfur metabolism, and cellular differentiation in Bacillus subtilis
    • DOI 10.1128/JB.187.12.3921-3930.2005
    • Smits, W. K., Dubois, J. Y., Bron, S., van Dijl, J. M., and Kuipers, O. P. (2005) Tricksy business. Transcriptome analysis reveals the involvement of thioredoxin A in redox homeostasis, oxidative stress, sulfur metabolism, and cellular differentiation in Bacillus subtilis. J. Bacteriol. 187, 3921-3930 (Pubitemid 40827775)
    • (2005) Journal of Bacteriology , vol.187 , Issue.12 , pp. 3921-3930
    • Smits, W.K.1    Dubois, J.-Y.F.2    Bron, S.3    Van Dijl, J.M.4    Kuipers, O.P.5
  • 17
    • 47249112231 scopus 로고    scopus 로고
    • The role of thioredoxin TrxA in Bacillus subtilis: A proteomics and transcriptomics approach
    • DOI 10.1002/pmic.200701015
    • Mostertz, J., Hochgräfe, F., Jürgen, B., Schweder, T., and Hecker, M. (2008) The role of thioredoxin TrxA in Bacillus subtilis: a proteomics and transcriptomics approach. Proteomics 8, 2676-2690 (Pubitemid 351988572)
    • (2008) Proteomics , vol.8 , Issue.13 , pp. 2676-2690
    • Mostertz, J.1    Hochgrafe, F.2    Jurgen, B.3    Schweder, T.4    Hecker, M.5
  • 18
    • 0347915666 scopus 로고    scopus 로고
    • Transcriptional Regulation of the Staphylococcus aureus Thioredoxin and Thioredoxin Reductase Genes in Response to Oxygen and Disulfide Stress
    • DOI 10.1128/JB.186.2.326-334.2004
    • Uziel, O., Borovok, I., Schreiber, R., Cohen, G., and Aharonowitz, Y. (2004) Transcriptional regulation of the Staphylococcus aureus thioredoxin and thioredoxin reductase genes in response to oxygen and disulfide stress. J. Bacteriol. 186, 326-334 (Pubitemid 38076421)
    • (2004) Journal of Bacteriology , vol.186 , Issue.2 , pp. 326-334
    • Uziel, O.1    Borovok, I.2    Schreiber, R.3    Cohen, G.4    Aharonowitz, Y.5
  • 24
    • 73149106387 scopus 로고    scopus 로고
    • RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to GenBank
    • Lundin, D., Torrents, E., Poole, A. M., and Sjöberg, B. M. (2009) RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to GenBank. BMC Genomics 10, 589
    • (2009) BMC Genomics , vol.10 , pp. 589
    • Lundin, D.1    Torrents, E.2    Poole, A.M.3    Sjöberg, B.M.4
  • 25
    • 0028557349 scopus 로고
    • A second class I ribonucleotide reductase in Enterobacteriaceae. Characterization of the Salmonella typhimurium enzyme
    • Jordan, A., Pontis, E., Atta, M., Krook, M., Gibert, I., Barbé, J., and Reichard, P. (1994) A second class I ribonucleotide reductase in Enterobacteriaceae. Characterization of the Salmonella typhimurium enzyme. Proc. Natl. Acad. Sci. U.S.A. 91, 12892-12896
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12892-12896
    • Jordan, A.1    Pontis, E.2    Atta, M.3    Krook, M.4    Gibert, I.5    Barbé, J.6    Reichard, P.7
  • 26
    • 76749163991 scopus 로고    scopus 로고
    • An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
    • Cotruvo, J. A., Jr., and Stubbe, J. (2010) An active dimanganese(III)- tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Biochemistry 49, 1297-1309
    • (2010) Biochemistry , vol.49 , pp. 1297-1309
    • Cotruvo Jr., J.A.1    Stubbe, J.2
  • 27
    • 77957270576 scopus 로고    scopus 로고
    • High resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states-an unusual flavodoxin. Structural biology
    • Johansson, R., Torrents, E., Lundin, D., Sprenger, J., Sahlin, M., Sjöberg, B. M., and Logan, D. T. (2010) High resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states-an unusual flavodoxin. Structural biology. FEBS J. 277, 4265-4277
    • (2010) FEBS J. , vol.277 , pp. 4265-4277
    • Johansson, R.1    Torrents, E.2    Lundin, D.3    Sprenger, J.4    Sahlin, M.5    Sjöberg, B.M.6    Logan, D.T.7
  • 28
    • 0030829520 scopus 로고    scopus 로고
    • Characterization of Escherichia coli NrdH: A glutaredoxin-like protein with a thioredoxin-like activity profile
    • DOI 10.1074/jbc.272.29.18044
    • Jordan, A., Aslund, F., Pontis, E., Reichard, P., and Holmgren, A. (1997) Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile. J. Biol. Chem. 272, 18044-18050 (Pubitemid 27306385)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18044-18050
    • Jordan, A.1    Aslund, F.2    Pontis, E.3    Reichard, P.4    Holmgren, A.5
  • 29
    • 80052993543 scopus 로고    scopus 로고
    • NrdH-redoxin protein mediates high enzyme activity in manganese-reconstituted ribonucleotide reductase from Bacillus anthracis
    • Crona, M., Torrents, E., Røhr, A. K., Hofer, A., Furrer, E., Tomter, A. B., Andersson, K. K., Sahlin, M., and Sjöberg, B. M. (2011) NrdH-redoxin protein mediates high enzyme activity in manganese-reconstituted ribonucleotide reductase from Bacillus anthracis. J. Biol. Chem. 286, 33053-33060
    • (2011) J. Biol. Chem. , vol.286 , pp. 33053-33060
    • Crona, M.1    Torrents, E.2    Røhr, A.K.3    Hofer, A.4    Furrer, E.5    Tomter, A.B.6    Andersson, K.K.7    Sahlin, M.8    Sjöberg, B.M.9
  • 31
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • DOI 10.1016/j.pep.2007.04.013, PII S1046592807001143
    • Blommel, P. G., and Fox, B. G. (2007) A combined approach to improving large scale production of tobacco etch virus protease. Protein Expr. Purif. 55, 53-68 (Pubitemid 47259692)
    • (2007) Protein Expression and Purification , vol.55 , Issue.1 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 32
    • 33846057724 scopus 로고    scopus 로고
    • NCBI reference sequences (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins
    • DOI 10.1093/nar/gkl842
    • Pruitt, K. D., Tatusova, T., and Maglott, D. R. (2007) NCBI reference sequences (RefSeq). A curated nonredundant sequence database of genomes, transcripts, and proteins. Nucleic Acids Res. 35, D61-D65 (Pubitemid 46056171)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL. 1
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 33
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0. Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu, N. Y., Wagner, J. R., Laird, M. R., Melli, G., Rey, S., Lo, R., Dao, P., Sahinalp, S. C., Ester, M., Foster, L. J., and Brinkman, F. S. (2010) PSORTb 3.0. Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26, 1608-1615
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6    Dao, P.7    Sahinalp, S.C.8    Ester, M.9    Foster, L.J.10    Brinkman, F.S.11
  • 35
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • Geiser, M., Cèbe, R., Drewello, D., and Schmitz, R. (2001) Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase. BioTechniques 31, 88-90
    • (2001) BioTechniques , vol.31 , pp. 88-90
    • Geiser, M.1    Cèbe, R.2    Drewello, D.3    Schmitz, R.4
  • 36
    • 33645021327 scopus 로고    scopus 로고
    • RF cloning. A restriction-free method for inserting target genes into plasmids
    • van den Ent, F., and Löwe, J. (2006) RF cloning. A restriction-free method for inserting target genes into plasmids. J. Biochem. Biophys. Methods 67, 67-74
    • (2006) J. Biochem. Biophys. Methods , vol.67 , pp. 67-74
    • Van Den Ent, F.1    Löwe, J.2
  • 37
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., Nojima, H., and Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96, 23-28
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 38
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 42
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren, A., and Björnstedt, M. (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol. 252, 199-208
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 43
    • 0024545809 scopus 로고
    • Characterization of two active site mutations of thioredoxin reductase from Escherichia coli
    • Prongay, A. J., Engelke, D. R., and Williams, C. H., Jr. (1989) Characterization of two active site mutations of thioredoxin reductase from Escherichia coli. J. Biol. Chem. 264, 2656-2664 (Pubitemid 19057758)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.5 , pp. 2656-2664
    • Prongay, A.J.1    Engelke, D.R.2    Williams Jr., C.H.3
  • 44
    • 0032545258 scopus 로고    scopus 로고
    • Allosteric regulation of Trypanosoma brucei ribonucleotide reductase studied in vitro and in vivo
    • DOI 10.1074/jbc.273.51.34098
    • Hofer, A., Ekanem, J. T., and Thelander, L. (1998) Allosteric regulation of Trypanosoma brucei ribonucleotide reductase studied in vitro and in vivo. J. Biol. Chem. 273, 34098-34104 (Pubitemid 29008879)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.51 , pp. 34098-34104
    • Hofer, A.1    Ekanem, J.T.2    Thelander, L.3
  • 45
    • 0023147728 scopus 로고
    • A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid
    • DOI 10.1016/0022-1759(87)90324-3
    • McKinney, M. M., and Parkinson, A. (1987) A simple, nonchromatographic procedure to purify immunoglobulins from serum and ascites fluid. J. Immunol. Methods 96, 271-278 (Pubitemid 17022661)
    • (1987) Journal of Immunological Methods , vol.96 , Issue.2 , pp. 271-278
    • McKinney, M.M.1    Parkinson, A.2
  • 47
    • 84868007353 scopus 로고    scopus 로고
    • Dendroscope 3. An interactive tool for rooted phylogenetic trees and networks
    • Huson, D. H., and Scornavacca, C. (2012) Dendroscope 3. An interactive tool for rooted phylogenetic trees and networks. Systematic Biol.,
    • (2012) Systematic Biol.
    • Huson, D.H.1    Scornavacca, C.2
  • 49
    • 0014404185 scopus 로고
    • Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B
    • Holmgren, A. (1968) Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B. Eur. J. Biochem. 6, 475-484
    • (1968) Eur. J. Biochem. , vol.6 , pp. 475-484
    • Holmgren, A.1
  • 51
    • 77957363373 scopus 로고    scopus 로고
    • Staphylococcus aureus NrdH redoxin is a reductant of the class Ib ribonucleotide reductase
    • Rabinovitch, I., Yanku, M., Yeheskel, A., Cohen, G., Borovok, I., and Aharonowitz, Y. (2010) Staphylococcus aureus NrdH redoxin is a reductant of the class Ib ribonucleotide reductase. J. Bacteriol. 192, 4963-4972
    • (2010) J. Bacteriol. , vol.192 , pp. 4963-4972
    • Rabinovitch, I.1    Yanku, M.2    Yeheskel, A.3    Cohen, G.4    Borovok, I.5    Aharonowitz, Y.6
  • 52
    • 33747357184 scopus 로고    scopus 로고
    • Arsenate reduction. Thiol cascade chemistry with convergent evolution
    • Messens, J., and Silver, S. (2006) Arsenate reduction. Thiol cascade chemistry with convergent evolution. J. Mol. Biol. 362, 1-17
    • (2006) J. Mol. Biol. , vol.362 , pp. 1-17
    • Messens, J.1    Silver, S.2
  • 53
    • 0031127895 scopus 로고    scopus 로고
    • Application of a single-plasmid vector for mutagenesis and high level expression of thioredoxin reductase and its use to examine flavin cofactor incorporation
    • Mulrooney, S. B. (1997) Application of a single-plasmid vector for mutagenesis and high level expression of thioredoxin reductase and its use to examine flavin cofactor incorporation. Protein Expr. Purif. 9, 372-378
    • (1997) Protein Expr. Purif. , vol.9 , pp. 372-378
    • Mulrooney, S.B.1
  • 55
    • 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
  • 56
    • 0018786716 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin
    • Holmgren, A. (1979) Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. J. Biol. Chem. 254, 3672-3678
    • (1979) J. Biol. Chem. , vol.254 , pp. 3672-3678
    • Holmgren, A.1
  • 59
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • DOI 10.1128/JB.183.6.1961-1973.2001
    • Baker, L. M., Raudonikiene, A., Hoffman, P. S., and Poole, L. B. (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori. Genetic and kinetic characterization. J. Bacteriol. 183, 1961-1973 (Pubitemid 32225991)
    • (2001) Journal of Bacteriology , vol.183 , Issue.6 , pp. 1961-1973
    • Baker, L.M.S.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 60
    • 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 (Pubitemid 18031680)
    • (1988) European Journal of Biochemistry , vol.170 , Issue.3 , pp. 603-611
    • Willing, A.1    Follmann, H.2    Auling, G.3
  • 62
    • 0031776932 scopus 로고    scopus 로고
    • Ribonucleotide reductase in Bacillus subtilis - Evidence for a Mn- dependent enzyme
    • Mohamed, S. F., Gvozdiak, O. R., Stallmann, D., Griepenburg, U., Follmann, H., and Auling, G. (1998) Ribonucleotide reductase in Bacillus subtilis - evidence for a Mn-dependent enzyme. Biofactors 7, 337-344 (Pubitemid 28305026)
    • (1998) BioFactors , vol.7 , Issue.4 , pp. 337-344
    • Mohamed, S.F.1    Gvozdiak, O.R.2    Stallmann, D.3    Griepenburg, U.4    Follmann, H.5    Auling, G.6
  • 63
    • 79952401377 scopus 로고    scopus 로고
    • Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo
    • Cotruvo, J. A., and Stubbe, J. (2011) Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo. Biochemistry 50, 1672-1681
    • (2011) Biochemistry , vol.50 , pp. 1672-1681
    • Cotruvo, J.A.1    Stubbe, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.