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Volumn 37, Issue 3, 2009, Pages 479-486

The three-component signalling system HbpS-SenS-SenR as an example of a redox sensing pathway in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CATALASE PEROXIDASE; DITHIOTHREITOL; FERRIC ION; FERROUS CHLORIDE; HEME; HYDROGEN PEROXIDE; HYDROXYL RADICAL; MONOPHENOL MONOOXYGENASE; OXIDOREDUCTASE; PROTEIN HBPS; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 69249234639     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-009-0260-9     Document Type: Review
Times cited : (36)

References (66)
  • 1
    • 33751429178 scopus 로고    scopus 로고
    • The evolution of two-component systems in bacteria reveals different strategies for niche adaptation
    • E Alm K Huang A Arkin 2006 The evolution of two-component systems in bacteria reveals different strategies for niche adaptation PLoS Comput Biol 2 e143
    • (2006) PLoS Comput Biol , vol.2 , pp. 143
    • Alm, E.1    Huang, K.2    Arkin, A.3
  • 3
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: Common structural principles in proteins that transport iron and heme
    • HM Baker BF Anderson EN Baker 2003 Dealing with iron: common structural principles in proteins that transport iron and heme Proc Natl Acad Sci USA 100 3579 3583
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 4
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • P Baldrian V Valášková 2008 Degradation of cellulose by basidiomycetous fungi FEMS Microbiol Rev 32 501 521
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 501-521
    • Baldrian, P.1    Valášková, V.2
  • 5
    • 33845709126 scopus 로고    scopus 로고
    • Molecular engineering approaches to peptide, polyketide and other antibiotics
    • RH Baltz 2006 Molecular engineering approaches to peptide, polyketide and other antibiotics Nat Biotechnol 24 1533 1540
    • (2006) Nat Biotechnol , vol.24 , pp. 1533-1540
    • Baltz, R.H.1
  • 7
    • 34447632499 scopus 로고    scopus 로고
    • DNA-binding characteristics of the regulator SenR in response to phosphorylation by the sensor histidine autokinase SenS from Streptomyces reticuli
    • G Bogel H Schrempf D Ortiz de Orué Lucana 2007 DNA-binding characteristics of the regulator SenR in response to phosphorylation by the sensor histidine autokinase SenS from Streptomyces reticuli FEBS J 274 3900 3913
    • (2007) FEBS J , vol.274 , pp. 3900-3913
    • Bogel, G.1    Schrempf, H.2    Ortiz De Orué Lucana, D.3
  • 8
    • 70349584359 scopus 로고    scopus 로고
    • The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner
    • doi: 10.1007/s00726-008-0188-5
    • Bogel G, Schrempf H, Ortiz de Orué Lucana D (2008) The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner. Amino Acids. doi: 10.1007/s00726-008-0188-5
    • (2008) Amino Acids
    • Bogel, G.1
  • 9
    • 34548787792 scopus 로고    scopus 로고
    • Reactive oxygen species and cellular oxygen sensing
    • TP Cash Y Pan MC Simon 2007 Reactive oxygen species and cellular oxygen sensing Free Radic Biol Med 43 1219 1225
    • (2007) Free Radic Biol Med , vol.43 , pp. 1219-1225
    • Cash, T.P.1    Pan, Y.2    Simon, M.C.3
  • 10
    • 0345492332 scopus 로고    scopus 로고
    • Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species
    • GL Challis DA Hopwood 2003 Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species Proc Natl Acad Sci USA 100 14555 145561
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14555-145561
    • Challis, G.L.1    Hopwood, D.A.2
  • 12
    • 20344374161 scopus 로고    scopus 로고
    • Conserved modular design of an oxygen sensory/signalling network with species-specific output
    • S Crosson PT McGrath C Stephens HH McAdams L Shapiro 2005 Conserved modular design of an oxygen sensory/signalling network with species-specific output Proc Natl Acad Sci USA 102 8018 8023
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8018-8023
    • Crosson, S.1    McGrath, P.T.2    Stephens, C.3    McAdams, H.H.4    Shapiro, L.5
  • 13
    • 34547151297 scopus 로고    scopus 로고
    • The VicRK system of Streptococcus mutans responds to oxidative stress
    • DM Deng MJ Liu JM ten Cate W Crielaard 2007 The VicRK system of Streptococcus mutans responds to oxidative stress J Dent Res 86 606 610
    • (2007) J Dent Res , vol.86 , pp. 606-610
    • Deng, D.M.1    Liu, M.J.2    Ten Cate, J.M.3    Crielaard, W.4
  • 14
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • PA DiGiuseppe TJ Silhavy 2003 Signal detection and target gene induction by the CpxRA two-component system J Bacteriol 185 2432 2440
    • (2003) J Bacteriol , vol.185 , pp. 2432-2440
    • Digiuseppe, P.A.1    Silhavy, T.J.2
  • 15
    • 0344666703 scopus 로고    scopus 로고
    • Interaction between the sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus
    • S Elsen O Dúche A Colbeau 2003 Interaction between the sensor HupUV and the histidine kinase HupT controls HupSL hydrogenase synthesis in Rhodobacter capsulatus J Bacteriol 185 7111 7119
    • (2003) J Bacteriol , vol.185 , pp. 7111-7119
    • Elsen, S.1    Dúche, O.2    Colbeau, A.3
  • 16
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: How one organism sees its world
    • C Fabret VA Feher JA Hoch 1999 Two-component signal transduction in Bacillus subtilis: how one organism sees its world J Bacteriol 181 1975 1983
    • (1999) J Bacteriol , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 17
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in the presence of iron
    • HJH Fenton 1986 Oxidation of tartaric acid in the presence of iron J Chem Soc 65 899 910
    • (1986) J Chem Soc , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 18
    • 0346734224 scopus 로고    scopus 로고
    • Growth polarity and cell division in Streptomyces
    • K Flardh 2003 Growth polarity and cell division in Streptomyces Curr Opin Microbiol 6 564 571
    • (2003) Curr Opin Microbiol , vol.6 , pp. 564-571
    • Flardh, K.1
  • 19
    • 0033527742 scopus 로고    scopus 로고
    • Inhibition of the FixL sensorkinase by the FixT protein in Sinorhizobium meliloti
    • AM Garnerone D Cabanes M Foussard P Boistard J Batut 1999 Inhibition of the FixL sensorkinase by the FixT protein in Sinorhizobium meliloti J Biol Chem 274 32500 32506
    • (1999) J Biol Chem , vol.274 , pp. 32500-32506
    • Garnerone, A.M.1    Cabanes, D.2    Foussard, M.3    Boistard, P.4    Batut, J.5
  • 20
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • K Hantke 2001 Iron and metal regulation in bacteria Curr Opin Microbiol 4 172 177
    • (2001) Curr Opin Microbiol , vol.4 , pp. 172-177
    • Hantke, K.1
  • 21
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • JA Hoch KI Varughese 2001 Keeping signals straight in phosphorelay signal transduction J Bacteriol 183 4941 4949
    • (2001) J Bacteriol , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 22
    • 33748520597 scopus 로고    scopus 로고
    • MtrAB-LpqB: A conserved three-component system in actinobacteria?
    • PA Hoskisson MI Hutchings 2006 MtrAB-LpqB: a conserved three-component system in actinobacteria? Trends Microbiol 14 444 449
    • (2006) Trends Microbiol , vol.14 , pp. 444-449
    • Hoskisson, P.A.1    Hutchings, M.I.2
  • 23
    • 4844230017 scopus 로고    scopus 로고
    • Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2)
    • MI Hutchings PA Hoskisson G Chandra MJ Buttner 2004 Sensing and responding to diverse extracellular signals? Analysis of the sensor kinases and response regulators of Streptomyces coelicolor A3(2) Microbiology 150 2795 2806
    • (2004) Microbiology , vol.150 , pp. 2795-2806
    • Hutchings, M.I.1    Hoskisson, P.A.2    Chandra, G.3    Buttner, M.J.4
  • 24
    • 33749643123 scopus 로고    scopus 로고
    • The sigma(E) cell envelope stress response of Streptomyces coelicolor is influenced by a novel lipoprotein, CseA
    • MI Hutchings HJ Hong E Leibovitz IC Sutcliffe MJ Buttner 2006 The sigma(E) cell envelope stress response of Streptomyces coelicolor is influenced by a novel lipoprotein, CseA J Bacteriol 188 7222 7229
    • (2006) J Bacteriol , vol.188 , pp. 7222-7229
    • Hutchings, M.I.1    Hong, H.J.2    Leibovitz, E.3    Sutcliffe, I.C.4    Buttner, M.J.5
  • 27
    • 34548654789 scopus 로고    scopus 로고
    • Dimorphism and virulence in fungi
    • Klein BS, Tebbets (2007) Dimorphism and virulence in fungi. Curr Opin Microbiol 10:314-319
    • (2007) Curr Opin Microbiol , vol.10 , pp. 314-319
    • Klein, B.S.1    Tebbets2
  • 28
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • MA Kohanski DJ Dwyer B Hayete CA Lawrence JJ Collins 2007 A common mechanism of cellular death induced by bactericidal antibiotics Cell 130 797 810
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 29
    • 55449126342 scopus 로고    scopus 로고
    • Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death
    • MA Kohanski DJ Dwyer J Wierzbowski G Cottarel JJ Collins 2008 Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death Cell 135 679 690
    • (2008) Cell , vol.135 , pp. 679-690
    • Kohanski, M.A.1    Dwyer, D.J.2    Wierzbowski, J.3    Cottarel, G.4    Collins, J.J.5
  • 31
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two component signal transduction pathways
    • MT Laub M Goulian 2007 Specificity in two component signal transduction pathways Annu Rev Genet 41 121 145
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 32
    • 0032835113 scopus 로고    scopus 로고
    • Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: Nitrate elicits a superior anion ligand response compared to nitrite
    • AI Lee A Delgado RP Gunsalus 1999 Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: nitrate elicits a superior anion ligand response compared to nitrite J Bacteriol 181 5309 5316
    • (1999) J Bacteriol , vol.181 , pp. 5309-5316
    • Lee, A.I.1    Delgado, A.2    Gunsalus, R.P.3
  • 35
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • T Mascher JD Helmann G Unden 2006 Stimulus perception in bacterial signal-transducing histidine kinases Microbiol Mol Biol Rev 70 910 938
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 36
    • 0031589010 scopus 로고    scopus 로고
    • Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli
    • T Mizuno 1997 Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli DNA Res 4 161 168
    • (1997) DNA Res , vol.4 , pp. 161-168
    • Mizuno, T.1
  • 37
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • E Nagababu JM Rifkind 2004 Heme degradation by reactive oxygen species Antioxid Redox Signal 6 967 978
    • (2004) Antioxid Redox Signal , vol.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 38
    • 33646253928 scopus 로고    scopus 로고
    • Global control of dimorphism and virulence in fungi
    • JC Nemecek M Wüthrich BS Klein 2006 Global control of dimorphism and virulence in fungi Science 28 583 588
    • (2006) Science , vol.28 , pp. 583-588
    • Nemecek, J.C.1    Wüthrich, M.2    Klein, B.S.3
  • 39
    • 33748294219 scopus 로고    scopus 로고
    • Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
    • K Nishino FF Hsu J Turk MJ Cromie MMSM Wösten EA Groisman 2006 Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III) Mol Microbiol 61 645 654
    • (2006) Mol Microbiol , vol.61 , pp. 645-654
    • Nishino, K.1    Hsu, F.F.2    Turk, J.3    Cromie, M.J.4    Wösten, M.5    Groisman, E.A.6
  • 40
    • 58549096736 scopus 로고    scopus 로고
    • Quorum sensing in staphylococci
    • RP Novick E Geisinger 2008 Quorum sensing in staphylococci Annu Rev Genet 42 541 564
    • (2008) Annu Rev Genet , vol.42 , pp. 541-564
    • Novick, R.P.1    Geisinger, E.2
  • 41
    • 0037292954 scopus 로고    scopus 로고
    • Amino acid residues involved in reversible thiol formation and zinc ion binding in the Streptomyces reticuli redox regulator FurS
    • D Ortiz de Orué Lucana M Troller H Schrempf 2003 Amino acid residues involved in reversible thiol formation and zinc ion binding in the Streptomyces reticuli redox regulator FurS Mol Genet Genomics 268 618 627
    • (2003) Mol Genet Genomics , vol.268 , pp. 618-627
    • Ortiz De Orué Lucana, D.1    Troller, M.2    Schrempf, H.3
  • 42
    • 4444235114 scopus 로고    scopus 로고
    • The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB
    • D Ortiz de Orué Lucana T Schaa H Schrempf 2004 The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB Microbiology 150 2575 2585
    • (2004) Microbiology , vol.150 , pp. 2575-2585
    • Ortiz De Orué Lucana, D.1    Schaa, T.2    Schrempf, H.3
  • 43
    • 27844486088 scopus 로고    scopus 로고
    • Identification of a novel two-component system SenS/SenR modulating the production of the catalase-peroxidase CpeB and the haem-binding protein HbpS in Streptomyces reticuli
    • D Ortiz de Orué Lucana P Zou M Nierhaus H Schrempf 2005 Identification of a novel two-component system SenS/SenR modulating the production of the catalase-peroxidase CpeB and the haem-binding protein HbpS in Streptomyces reticuli Microbiology 151 3603 3614
    • (2005) Microbiology , vol.151 , pp. 3603-3614
    • Ortiz De Orué Lucana, D.1    Zou, P.2    Nierhaus, M.3    Schrempf, H.4
  • 44
    • 60349105581 scopus 로고    scopus 로고
    • The oligomeric assembly of the novel haem degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase
    • D Ortiz de Orué Lucana G Bogel P Zou MR Groves 2009 The oligomeric assembly of the novel haem degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase J Mol Biol 386 1108 1122
    • (2009) J Mol Biol , vol.386 , pp. 1108-1122
    • Ortiz De Orué Lucana, D.1    Bogel, G.2    Zou, P.3    Groves, M.R.4
  • 45
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • H Panek MR O'Brian 2002 A whole genome view of prokaryotic haem biosynthesis Microbiology 148 2273 2282
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 48
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • A Rietsch J Beckwith 1998 The genetics of disulfide bond metabolism Annu Rev Genet 32 163 184
    • (1998) Annu Rev Genet , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 49
    • 33744979998 scopus 로고    scopus 로고
    • Beyond the fur paradigm: Iron-controlled gene expression in rhizobia
    • G Rudolph H Hennecke HM Fischer 2006 Beyond the Fur paradigm: iron-controlled gene expression in rhizobia FEMS Microbiol Rev 30 631 648
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 631-648
    • Rudolph, G.1    Hennecke, H.2    Fischer, H.M.3
  • 52
    • 0026745984 scopus 로고
    • The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains
    • A Schlochtermeier S Walter J Schröder M Moormann H Schrempf 1992 The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains Mol Microbiol 6 3611 3621
    • (1992) Mol Microbiol , vol.6 , pp. 3611-3621
    • Schlochtermeier, A.1    Walter, S.2    Schröder, J.3    Moormann, M.4    Schrempf, H.5
  • 53
    • 0032833084 scopus 로고    scopus 로고
    • Identification of a two-component signal transduction system from Corynebacterium diphteriae that activates gene expression in response to the presence of heme and hemoglobin
    • MP Schmitt 1999 Identification of a two-component signal transduction system from Corynebacterium diphteriae that activates gene expression in response to the presence of heme and hemoglobin J Bacteriol 181 5330 5340
    • (1999) J Bacteriol , vol.181 , pp. 5330-5340
    • Schmitt, M.P.1
  • 55
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein families based on seed alignments
    • ELL Sonnhammer SR Eddy R Durbin 1997 Pfam: a comprehensive database of protein families based on seed alignments Proteins 28 405 420
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.L.1    Eddy, S.R.2    Durbin, R.3
  • 56
    • 34548857623 scopus 로고    scopus 로고
    • Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing
    • DL Stauff VJ Torres EP Skaar 2007 Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing J Biol Chem 282 36 26111 26121
    • (2007) J Biol Chem , vol.282 , Issue.36 , pp. 26111-26121
    • Stauff, D.L.1    Torres, V.J.2    Skaar, E.P.3
  • 57
    • 22544460491 scopus 로고    scopus 로고
    • YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis
    • H Szurmant K Nelson EJ Kim M Perego JA Hoch 2005 YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis J Bacteriol 187 5419 5426
    • (2005) J Bacteriol , vol.187 , pp. 5419-5426
    • Szurmant, H.1    Nelson, K.2    Kim, E.J.3    Perego, M.4    Hoch, J.A.5
  • 58
    • 44449149782 scopus 로고    scopus 로고
    • An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins
    • H Szurmant L Bu CL Brooks III JA Hoch 2008 An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins Proc Natl Acad Sci USA 105 5891 5896
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5891-5896
    • Szurmant, H.1    Bu, L.2    Brooks Iii, C.L.3    Hoch, J.A.4
  • 59
    • 33747658416 scopus 로고    scopus 로고
    • AI-1 influences the kinase activity but not the phosphatase activity of LuxN of Vibrio harveyi
    • M Timmen BL Bassler K Jung 2006 AI-1 influences the kinase activity but not the phosphatase activity of LuxN of Vibrio harveyi J Biol Chem 281 24398 24404
    • (2006) J Biol Chem , vol.281 , pp. 24398-24404
    • Timmen, M.1    Bassler, B.L.2    Jung, K.3
  • 60
    • 39749178251 scopus 로고    scopus 로고
    • Cytokinin signaling: Two-components and more
    • JP To JJ Kieber 2008 Cytokinin signaling: two-components and more Trends Plant Sci 13 85 92
    • (2008) Trends Plant Sci , vol.13 , pp. 85-92
    • To, J.P.1    Kieber, J.J.2
  • 63
    • 0036886272 scopus 로고    scopus 로고
    • Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator
    • DOI 10.1046/j.1365-2958.2002.03240.x
    • T Yoshida S Cai M Inouye 2002 Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator Mol Microbiol 46 1283 1294 (Pubitemid 36961263)
    • (2002) Molecular Microbiology , vol.46 , Issue.5 , pp. 1283-1294
    • Yoshida, T.1    Cai, S.J.2    Inouye, M.3
  • 64
    • 0034662751 scopus 로고    scopus 로고
    • A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction
    • J Zapf U Sen HochJA Madhusudan KI Varughese 2000 A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction Structure 15 851 862
    • (2000) Structure , vol.15 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Hochja, M.3    Varughese, K.I.4
  • 65
    • 0034033246 scopus 로고    scopus 로고
    • The heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase-peroxidase CpeB
    • P Zou H Schrempf 2000 The heme-independent manganese-peroxidase activity depends on the presence of the C-terminal domain within the Streptomyces reticuli catalase-peroxidase CpeB Eur J Biochem 267 2840 2849
    • (2000) Eur J Biochem , vol.267 , pp. 2840-2849
    • Zou, P.1    Schrempf, H.2


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