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Volumn 68, Issue 2, 2004, Pages 263-279

RegB/RegA, a highly conserved redox-responding global two-component regulatory system

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; PROTEIN HISTIDINE KINASE;

EID: 2942558361     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.68.2.263-279.2004     Document Type: Review
Times cited : (165)

References (96)
  • 1
    • 0036242327 scopus 로고    scopus 로고
    • Bacteriochlorophyll-dependent expression of genes for pigment-binding proteins in Rhodobacter capsulatus involves the RegB/RegA two-component system
    • Abada, E. M., A. Balzer, A. Jager, and G. Klug. 2002. Bacteriochlorophyll-dependent expression of genes for pigment-binding proteins in Rhodobacter capsulatus involves the RegB/RegA two-component system. Mol. Genet. Genomics 267:202-209.
    • (2002) Mol. Genet. Genomics , vol.267 , pp. 202-209
    • Abada, E.M.1    Balzer, A.2    Jager, A.3    Klug, G.4
  • 2
    • 0032584767 scopus 로고    scopus 로고
    • Pathways for transcriptional activation of a glutathione-dependent formaldehyde dehydrogenase gene
    • Barber, D. R., and T. J. Donohue. 1998. Pathways for transcriptional activation of a glutathione-dependent formaldehyde dehydrogenase gene. J. Mol. Biol. 280:775-784.
    • (1998) J. Mol. Biol. , vol.280 , pp. 775-784
    • Barber, D.R.1    Donohue, T.J.2
  • 3
    • 0002702718 scopus 로고    scopus 로고
    • Regulating synthesis of the purple bacterial photosystem
    • E.-M. Aro and B. Andersson (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Bauer, C. E. 2001. Regulating synthesis of the purple bacterial photosystem, p. 67-83. In E.-M. Aro and B. Andersson (ed.), Regulation of photosynthesis. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2001) Regulation of Photosynthesis , pp. 67-83
    • Bauer, C.E.1
  • 4
    • 0029887594 scopus 로고    scopus 로고
    • Regulatory circuits controlling photosynthesis gene expression
    • Bauer, C. E., and T. H. Bird. 1996. Regulatory circuits controlling photosynthesis gene expression. Cell 85:5-8.
    • (1996) Cell , vol.85 , pp. 5-8
    • Bauer, C.E.1    Bird, T.H.2
  • 6
    • 0031858562 scopus 로고    scopus 로고
    • Expression of the fixR-nifA operon in Bradyrhizobium japonicum depends on a new response regulator
    • Bauer, E., T. Kaspar, H. M. Fischer, and H. Hennecke. 1998. Expression of the fixR-nifA operon in Bradyrhizobium japonicum depends on a new response regulator, RegR. J. Bacteriol. 180:3853-3863.
    • (1998) RegR. J. Bacteriol. , vol.180 , pp. 3853-3863
    • Bauer, E.1    Kaspar, T.2    Fischer, H.M.3    Hennecke, H.4
  • 7
    • 0033523121 scopus 로고    scopus 로고
    • Autophosphorylation, phosphotransfer and DNA-binding properties of the RegB/RegA two-component regulatory system in Rhodobacter capsulatus
    • Bird, T. H., S. Du, and C. E. Bauer. 1999. Autophosphorylation, phosphotransfer and DNA-binding properties of the RegB/RegA two-component regulatory system in Rhodobacter capsulatus. J. Biol. Chem. 274:16343-16348.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16343-16348
    • Bird, T.H.1    Du, S.2    Bauer, C.E.3
  • 8
    • 0033000075 scopus 로고    scopus 로고
    • In vitro activation and repression of photosynthesis gene transcription in Rhodobacter capsulatus
    • Bowman, W. C., S. Du, C. E. Bauer, and R. G. Kranz. 1999. In vitro activation and repression of photosynthesis gene transcription in Rhodobacter capsulatus. Mol. Microbiol. 33:429-437.
    • (1999) Mol. Microbiol. , vol.33 , pp. 429-437
    • Bowman, W.C.1    Du, S.2    Bauer, C.E.3    Kranz, R.G.4
  • 9
    • 0028825790 scopus 로고
    • Cloning and characterization of senC, a gene involved in both aerobic respiration and photosynthesis gene expression in Rhodobacter capsulatus
    • Buggy, J. J., and C. E. Bauer. 1995. Cloning and characterization of senC, a gene involved in both aerobic respiration and photosynthesis gene expression in Rhodobacter capsulatus. J. Bacteriol. 177:6958-6965.
    • (1995) J. Bacteriol. , vol.177 , pp. 6958-6965
    • Buggy, J.J.1    Bauer, C.E.2
  • 10
    • 0028151689 scopus 로고
    • Characterization of a light-responding trans-activator responsible for differentially controlling reaction center and light-harvesting I gene expression in Rhodobacter capsulatus
    • Buggy, J. J., M. W. Sganga, and C. E. Bauer. 1994. Characterization of a light-responding trans-activator responsible for differentially controlling reaction center and light-harvesting I gene expression in Rhodobacter capsulatus. J. Bacteriol. 176:6936-6943.
    • (1994) J. Bacteriol. , vol.176 , pp. 6936-6943
    • Buggy, J.J.1    Sganga, M.W.2    Bauer, C.E.3
  • 11
    • 0342948902 scopus 로고    scopus 로고
    • Correction of the DNA sequence of the regB gene of Rhodobacter capsulatus with implications for the membrane topology of the sensor kinase RegB
    • Chen, W., A. Jager, and G. Klug. 2000. Correction of the DNA sequence of the regB gene of Rhodobacter capsulatus with implications for the membrane topology of the sensor kinase RegB. J. Bacteriol. 182:818-820.
    • (2000) J. Bacteriol. , vol.182 , pp. 818-820
    • Chen, W.1    Jager, A.2    Klug, G.3
  • 12
    • 70449138041 scopus 로고
    • Kinetic studies of pigment synthesis by non-sulfur purple bacteria
    • Cohen-Bazire, G. W., W. R. Sistrom, and R. Y. Stanier. 1957. Kinetic studies of pigment synthesis by non-sulfur purple bacteria. J. Cell. Comp. Physiol. 49:25-68.
    • (1957) J. Cell. Comp. Physiol. , vol.49 , pp. 25-68
    • Cohen-Bazire, G.W.1    Sistrom, W.R.2    Stanier, R.Y.3
  • 15
    • 0036360123 scopus 로고    scopus 로고
    • Pseudomonas aeriginosa RoxR, a response regulator related to Rhodobacter sphaeroides PrrA, activates expression of the cyanide-insensitive terminal oxidase
    • Comolli, J. C., and T. J. Donohue. 2002. Pseudomonas aeriginosa RoxR, a response regulator related to Rhodobacter sphaeroides PrrA, activates expression of the cyanide-insensitive terminal oxidase. Mol. Microbiol. 45:755-768.
    • (2002) Mol. Microbiol. , vol.45 , pp. 755-768
    • Comolli, J.C.1    Donohue, T.J.2
  • 16
    • 0033456155 scopus 로고    scopus 로고
    • The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system
    • Dischert, W., P. M. Vignais, and A. Colbeau. 1999. The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system. Mol. Microbiol. 34:995-1006.
    • (1999) Mol. Microbiol. , vol.34 , pp. 995-1006
    • Dischert, W.1    Vignais, P.M.2    Colbeau, A.3
  • 17
    • 0036237131 scopus 로고    scopus 로고
    • AerR, a second aerobic repressor of photosynthesis geen expression in Rhodobacter capsulatus
    • Dong, C., S. Elsen, L. R. Swem, and C. E. Bauer. 2002. AerR, a second aerobic repressor of photosynthesis geen expression in Rhodobacter capsulatus. J. Bacteriol. 184:2805-2814.
    • (2002) J. Bacteriol. , vol.184 , pp. 2805-2814
    • Dong, C.1    Elsen, S.2    Swem, L.R.3    Bauer, C.E.4
  • 18
    • 0032541134 scopus 로고    scopus 로고
    • DNA binding characteristics of RegA*. A constitutively active anaerobic activator of photosynthesis gene expression in Rhodobacter capsulatus
    • Du, S., T. H. Bird, and C. E. Bauer. 1998. DNA binding characteristics of RegA*. A constitutively active anaerobic activator of photosynthesis gene expression in Rhodobacter capsulatus. J. Biol. Chem. 273:18509-18513.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18509-18513
    • Du, S.1    Bird, T.H.2    Bauer, C.E.3
  • 19
    • 0032807473 scopus 로고    scopus 로고
    • Regulated expression of a highly conserved regulatory gene cluster is necessary for controlling photosynthesis gene expression in response to anaerobiosis in Rhodobacter capsulatus
    • Du, S., J.-L. Kouadio, and C. E. Bauer. 1999. Regulated expression of a highly conserved regulatory gene cluster is necessary for controlling photosynthesis gene expression in response to anaerobiosis in Rhodobacter capsulatus. J. Bacteriol. 181:4334-4341.
    • (1999) J. Bacteriol. , vol.181 , pp. 4334-4341
    • Du, S.1    Kouadio, J.-L.2    Bauer, C.E.3
  • 21
    • 0031682152 scopus 로고    scopus 로고
    • 1 operon of Rhodobacter sphaeroides regulate gene expression
    • 1 operon of Rhodobacter sphaeroides regulate gene expression. J. Bacteriol. 180:4903-4911.
    • (1998) J. Bacteriol. , vol.180 , pp. 4903-4911
    • Dubbs, J.M.1    Tabita, F.R.2
  • 22
    • 0038182517 scopus 로고    scopus 로고
    • 11 promoter-operator region with CbbR and RegA (PrrA) regulators indicate distinct mechanisms to control expression of the two cbb operons of Rhodobacter sphaeroides
    • 11 promoter-operator region with CbbR and RegA (PrrA) regulators indicate distinct mechanisms to control expression of the two cbb operons of Rhodobacter sphaeroides. J. Biol. Chem. 278:16443-16450.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16443-16450
    • Dubbs, J.M.1    Tabita, F.R.2
  • 23
    • 0034055889 scopus 로고    scopus 로고
    • Expression of uptake hydrogenase and molybdenum nitrogenase in Rhodobacter capsulatus is coregulated by the RegB-RegA two-component regulatory system
    • Elsen, S., W. Dischert, A. Colbeau, and C. E. Bauer. 2000. Expression of uptake hydrogenase and molybdenum nitrogenase in Rhodobacter capsulatus is coregulated by the RegB-RegA two-component regulatory system. J. Bacteriol. 182:2831-2837.
    • (2000) J. Bacteriol. , vol.182 , pp. 2831-2837
    • Elsen, S.1    Dischert, W.2    Colbeau, A.3    Bauer, C.E.4
  • 24
    • 0032515071 scopus 로고    scopus 로고
    • CrtJ bound to distant binding sites interacts cooperatively to aerobically repress photopigment biosynthesis and light harvesting II gene expression in Rhodobacter capsulatus
    • Elsen, S., S. N. Ponnampalam, and C. E. Bauer. 1998. CrtJ bound to distant binding sites interacts cooperatively to aerobically repress photopigment biosynthesis and light harvesting II gene expression in Rhodobacter capsulatus. J. Biol. Chem. 273:30762-30769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30762-30769
    • Elsen, S.1    Ponnampalam, S.N.2    Bauer, C.E.3
  • 25
    • 0033697099 scopus 로고    scopus 로고
    • Evidence for a functional similarity between the two-component regulatory systems RegSR, ActSR, and RegBA (PrrBA) in α-Proteobacteria
    • Emmerich, R., H. Hennecke, and H. M. Fischer. 2000. Evidence for a functional similarity between the two-component regulatory systems RegSR, ActSR, and RegBA (PrrBA) in α-Proteobacteria. Arch. Microbiol. 174:307-313.
    • (2000) Arch. Microbiol. , vol.174 , pp. 307-313
    • Emmerich, R.1    Hennecke, H.2    Fischer, H.M.3
  • 26
    • 0033565695 scopus 로고    scopus 로고
    • Phosphorylation, dephosphorylation and DNA-binding of the Bradyrhizobium japonicum RegSR two-component regulatory proteins
    • Emmerich, R., K. Panglungtshang, P. Strehler, H. Hennecke, and H. M. Fischer. 1999. Phosphorylation, dephosphorylation and DNA-binding of the Bradyrhizobium japonicum RegSR two-component regulatory proteins. Eur. J. Biochem. 263:455-463.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 455-463
    • Emmerich, R.1    Panglungtshang, K.2    Strehler, P.3    Hennecke, H.4    Fischer, H.M.5
  • 27
    • 0009782977 scopus 로고    scopus 로고
    • Functional analysis of the Bradyrhizobium japonicum RegSR two-component regulatory system
    • F. O. Pedrosa, M. Hungria, G. Yates, and W. E. Newton (ed.). Kluwer, London, United Kingdom
    • Emmerich, R., P. Strehler, E. Bauer, H. M. Fischer, and H. Hennecke. 2000. Functional analysis of the Bradyrhizobium japonicum RegSR two-component regulatory system, p. 89-90. In F. O. Pedrosa, M. Hungria, G. Yates, and W. E. Newton (ed.), Nitrogen fixation: from molecules to crop productivity. Kluwer, London, United Kingdom.
    • (2000) Nitrogen Fixation: From Molecules to Crop Productivity , pp. 89-90
    • Emmerich, R.1    Strehler, P.2    Bauer, E.3    Fischer, H.M.4    Hennecke, H.5
  • 28
    • 0034327612 scopus 로고    scopus 로고
    • An imperfect inverted repeat is critical for DNA binding of the response regulator RegR of Bradyrhizobium japonicum
    • Emmerich, R., P. Strehler, H. Hennecke, and H. M. Fischer. 2000. An imperfect inverted repeat is critical for DNA binding of the response regulator RegR of Bradyrhizobium japonicum. Nucleic Acids Res. 28:4166-4171.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4166-4171
    • Emmerich, R.1    Strehler, P.2    Hennecke, H.3    Fischer, H.M.4
  • 29
    • 0027976503 scopus 로고
    • PrrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides
    • Eraso, J. M., and S. Kaplan. 1994. PrrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides. J. Bacteriol. 176:32-43.
    • (1994) J. Bacteriol. , vol.176 , pp. 32-43
    • Eraso, J.M.1    Kaplan, S.2
  • 30
    • 0029016713 scopus 로고
    • Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: A mutant histidine kinase
    • Eraso, J. M., and S. Kaplan. 1995. Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase. J. Bacteriol. 177:2695-2706.
    • (1995) J. Bacteriol. , vol.177 , pp. 2695-2706
    • Eraso, J.M.1    Kaplan, S.2
  • 31
    • 0034728367 scopus 로고    scopus 로고
    • From redox flow to gene regulation: Role of the PrrC protein of Rhodobacter sphaeroides 2.4.1
    • Eraso, J. M., and S. Kaplan. 2000. From redox flow to gene regulation: role of the PrrC protein of Rhodobacter sphaeroides 2.4.1. Biochemistry 39:2052-2062.
    • (2000) Biochemistry , vol.39 , pp. 2052-2062
    • Eraso, J.M.1    Kaplan, S.2
  • 32
    • 0007064908 scopus 로고    scopus 로고
    • ActR is a global genetic regulator in Sinorhizobium meliloti
    • F. O. Pedrosa, M. Hungria, G. Yates, and W. E. Newton (ed.). Kluwer Academic Publisher London, United Kingdom
    • Fenner, B. J., R. P. Tiwari, W. G. Reeve, M. J. Dilworth, and A. R. Glenn. 2000. ActR is a global genetic regulator in Sinorhizobium meliloti. p. 488. In F. O. Pedrosa, M. Hungria, G. Yates, and W. E. Newton (ed.), Nitrogen fixation: from molecules to crop productivity. Kluwer Academic Publisher London, United Kingdom.
    • (2000) Nitrogen Fixation: From Molecules to Crop Productivity , pp. 488
    • Fenner, B.J.1    Tiwari, R.P.2    Reeve, W.G.3    Dilworth, M.J.4    Glenn, A.R.5
  • 33
    • 0036882111 scopus 로고    scopus 로고
    • 2 fixation operons of Rhodobacter sphaeroides by the Prr/Reg two-component system during chemoautotrophic growth
    • 2 fixation operons of Rhodobacter sphaeroides by the Prr/Reg two-component system during chemoautotrophic growth. J. Bacteriol. 184:6654-6664.
    • (2002) J. Bacteriol. , vol.184 , pp. 6654-6664
    • Gibson, J.L.1    Dubbs, J.M.2    Tabita, F.R.3
  • 34
    • 0027165454 scopus 로고
    • Nucleotide sequence and functional analysis of CbbR, a positive regulator of the calvin cycle operons of Rhodobacter sphaeroides
    • Gibson, J. L., and F. R. Tabita. 1993. Nucleotide sequence and functional analysis of CbbR, a positive regulator of the calvin cycle operons of Rhodobacter sphaeroides. J. Bacteriol. 175:5778-5784.
    • (1993) J. Bacteriol. , vol.175 , pp. 5778-5784
    • Gibson, J.L.1    Tabita, F.R.2
  • 35
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum, D. M., and A. Shtanko, and A. Tzagoloff. 1996. SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271:20531-20535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 36
    • 0029111464 scopus 로고
    • Isolation of regulatory mutants in photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1 and partial complementation of a PrrB mutant by the HupT histidine-kinase
    • Gomelsky, M., and S. Kaplan. 1995. Isolation of regulatory mutants in photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1 and partial complementation of a PrrB mutant by the HupT histidine-kinase. Microbiology 141:1805-1819.
    • (1995) Microbiology , vol.141 , pp. 1805-1819
    • Gomelsky, M.1    Kaplan, S.2
  • 37
    • 0003146605 scopus 로고
    • 1 complexes
    • R. E. Blankenship, M. T. Madigan and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 1 complexes, p. 747-774. In R. E. Blankenship, M. T. Madigan and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 747-774
    • Gray, K.A.1    Daldal, F.2
  • 39
    • 0008632136 scopus 로고    scopus 로고
    • Transcriptional regulation of puf and puc operon expression in Rhodobacter capsulatus by the DNA binding protein RegA
    • G. A. Peschek, W. Löffelhardt, and G. Schmetterer (ed.). Kluwer Academic, Plenum Publishers, New York
    • Hemschemeier, S. K., M. Kirndörfer, U. Ebel, and G. Klug. 1999. Transcriptional regulation of puf and puc operon expression in Rhodobacter capsulatus by the DNA binding protein RegA, p. 127-130. In G. A. Peschek, W. Löffelhardt, and G. Schmetterer (ed.), The phototrophic prokaryotes. Kluwer Academic, Plenum Publishers, New York.
    • (1999) The Phototrophic Prokaryotes , pp. 127-130
    • Hemschemeier, S.K.1    Kirndörfer, M.2    Ebel, U.3    Klug, G.4
  • 40
    • 0343130515 scopus 로고    scopus 로고
    • DNA binding of wild-type RegA protein and its differential effect on the expression of pigment binding proteins in Rhodobacter capsulatus
    • Hemsehemeier, S. K., M. Kirndörfer, M. Hebermchl, and G. Klug. 2000. DNA binding of wild-type RegA protein and its differential effect on the expression of pigment binding proteins in Rhodobacter capsulatus. J. Mol. Microbiol. Biotechnol. 2:235-243.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 235-243
    • Hemsehemeier, S.K.1    Kirndörfer, M.2    Hebermchl, M.3    Klug, G.4
  • 41
    • 0028924678 scopus 로고
    • Isolation and in vitro phosphorylation of sensory transduction components controlling anaerobic induction of light harvesting and reaction center gene expression in Rhodobacter capsulatus
    • Inoue, K., J.-L. Kouadio, C. S. Mosley, and C. E. Bauer. 1995. Isolation and in vitro phosphorylation of sensory transduction components controlling anaerobic induction of light harvesting and reaction center gene expression in Rhodobacter capsulatus. Biochemistry 34:391-396.
    • (1995) Biochemistry , vol.34 , pp. 391-396
    • Inoue, K.1    Kouadio, J.-L.2    Mosley, C.S.3    Bauer, C.E.4
  • 42
    • 84902405976 scopus 로고    scopus 로고
    • Regulation of porins in Escherichia coli by the osmosensing histidine kinase/phosphatase EnvZ
    • M. Inouye and R. Dutta (ed.). Academic Press, Inc., San Diego, Calif.
    • Inouye, M., R. Dutta, and Y. Zhu. 2003. Regulation of porins in Escherichia coli by the osmosensing histidine kinase/phosphatase EnvZ, p. 25-46. In M. Inouye and R. Dutta (ed.), Histidine kinases in signal transduction. Academic Press, Inc., San Diego, Calif.
    • (2003) Histidine Kinases in Signal Transduction , pp. 25-46
    • Inouye, M.1    Dutta, R.2    Zhu, Y.3
  • 43
    • 0029855868 scopus 로고    scopus 로고
    • A global two-component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation
    • Joshi, H. M., and F. R. Tabita. 1996. A global two-component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation. Proc. Natl. Acad. Sci. USA 93:14515-14520.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14515-14520
    • Joshi, H.M.1    Tabita, F.R.2
  • 44
    • 0036181755 scopus 로고    scopus 로고
    • Control of dimethyl-sulfoxide reductase expression in Rhodobacter capsulatus: The role of carbon metabolites and the response regulators DorR and RegA
    • Kappler, U., W. M. Huston, and A. G. McEwan. 2002. Control of dimethyl-sulfoxide reductase expression in Rhodobacter capsulatus: the role of carbon metabolites and the response regulators DorR and RegA. Microbiology 148:605-614.
    • (2002) Microbiology , vol.148 , pp. 605-614
    • Kappler, U.1    Huston, W.M.2    McEwan, A.G.3
  • 46
    • 0031841913 scopus 로고    scopus 로고
    • Integration host factor affects the oxygen-regulated expression of photosynthesis gene in Rhodobacter capsulatus
    • Kirndörfer, M., A. Jäger, and G. Klug. 1998. Integration host factor affects the oxygen-regulated expression of photosynthesis gene in Rhodobacter capsulatus. Mol. Gen. Genet. 258:297-305.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 297-305
    • Kirndörfer, M.1    Jäger, A.2    Klug, G.3
  • 47
    • 0034677662 scopus 로고    scopus 로고
    • Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase
    • Koch H. G., C. Winterstein, A. S. Saribas, J. O. Alben, and F. Daldal. 2000. Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase. J. Mol. Biol. 297:49-65.
    • (2000) J. Mol. Biol. , vol.297 , pp. 49-65
    • Koch, H.G.1    Winterstein, C.2    Saribas, A.S.3    Alben, J.O.4    Daldal, F.5
  • 49
    • 0344237366 scopus 로고    scopus 로고
    • Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: Insights into DNA binding specificity
    • Laguri, C., M. K. Phillips-Jones, and M. P. Williamson. 2003. Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity. Nucleic Acids Res. 31:6778-6787.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6778-6787
    • Laguri, C.1    Phillips-Jones, M.K.2    Williamson, M.P.3
  • 50
    • 0036279617 scopus 로고    scopus 로고
    • Involvement of the PrrB/PrrA two-component system in nitrite respiration in Rhodobacter sphaeroides 2.4.3: Evidence for transcriptional regulation
    • Laratta, W. P., P. S. Choi, I. E. Tosques, and J. P. Shapleigh. 2002. Involvement of the PrrB/PrrA two-component system in nitrite respiration in Rhodobacter sphaeroides 2.4.3: evidence for transcriptional regulation. J. Bacteriol. 184:3521-3529.
    • (2002) J. Bacteriol. , vol.184 , pp. 3521-3529
    • Laratta, W.P.1    Choi, P.S.2    Tosques, I.E.3    Shapleigh, J.P.4
  • 52
    • 0029881337 scopus 로고    scopus 로고
    • Organization and regulation of genes encoding the molybdenum nitrogenase and the alternative nitrogenase in Rhodobacter capsulatus
    • Masepohl, B., and W. Klipp. 1996. Organization and regulation of genes encoding the molybdenum nitrogenase and the alternative nitrogenase in Rhodobacter capsulatus. Arch. Microbiol. 165:80-90.
    • (1996) Arch. Microbiol. , vol.165 , pp. 80-90
    • Masepohl, B.1    Klipp, W.2
  • 53
    • 0032814544 scopus 로고    scopus 로고
    • Structural and functional analyses of photosynthetic regulatory genes regA and regB from Rhodovulum sulfidophilum, Roseobacter denitrificans and Rhodobacter capsulatus
    • Masuda, S., Y. Matsumoto, K. V. P. Nagashima, K. Shimada, K. Inoue, C. E. Bauer, and K. Matsuura. 1999. Structural and functional analyses of photosynthetic regulatory genes regA and regB from Rhodovulum sulfidophilum, Roseobacter denitrificans and Rhodobacter capsulatus. J. Bacteriol. 181:4205-4215.
    • (1999) J. Bacteriol. , vol.181 , pp. 4205-4215
    • Masuda, S.1    Matsumoto, Y.2    Nagashima, K.V.P.3    Shimada, K.4    Inoue, K.5    Bauer, C.E.6    Matsuura, K.7
  • 54
    • 0037042213 scopus 로고    scopus 로고
    • PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity
    • McEwan, A. G., A. Lewin, S. L. Davy, R. Boetzel, A. Leech, D. Walker, T. Wood, and G. R. Moore. 2002. PrrC from Rhodobacter sphaeroides, a homologue of eukaryotic Sco proteins, is a copper-binding protein and may have a thiol-disulfide oxidoreductase activity. FEBS Lett. 518:10-16.
    • (2002) FEBS Lett. , vol.518 , pp. 10-16
    • McEwan, A.G.1    Lewin, A.2    Davy, S.L.3    Boetzel, R.4    Leech, A.5    Walker, D.6    Wood, T.7    Moore, G.R.8
  • 55
    • 0028019047 scopus 로고
    • Identification and molecular genetic characterization of a sensor kinase responsible for coordinately regulating light harvesting and reaction center gene expression in response to anaerobiosis
    • Mosley, C. S., J. Y. Suzuki, and C. E. Bauer. 1994. Identification and molecular genetic characterization of a sensor kinase responsible for coordinately regulating light harvesting and reaction center gene expression in response to anaerobiosis. J. Bacteriol. 176:7566-7573.
    • (1994) J. Bacteriol. , vol.176 , pp. 7566-7573
    • Mosley, C.S.1    Suzuki, J.Y.2    Bauer, C.E.3
  • 56
    • 0031774285 scopus 로고    scopus 로고
    • Redox-dependent gene regulation in Rhodobacter sphaeroides 2.4.1: Effects on dimethylsulfoxide reductase (dor) gene expression
    • Mouncey, N. J., and S. Kaplan. 1998. Redox-dependent gene regulation in Rhodobacter sphaeroides 2.4.1: effects on dimethylsulfoxide reductase (dor) gene expression. J. Bacteriol. 180:5612-5618.
    • (1998) J. Bacteriol. , vol.180 , pp. 5612-5618
    • Mouncey, N.J.1    Kaplan, S.2
  • 57
    • 0030835030 scopus 로고    scopus 로고
    • Characterization of the genes encoding dimethylsufoxide reductase of Rhodobacter sphaeroides 2.4.1: An essential metabolic gene function encoded by chromosome II
    • Mouncey, N. J., M. Choudhary, and S. Kaplan. 1997. Characterization of the genes encoding dimethylsufoxide reductase of Rhodobacter sphaeroides 2.4.1: an essential metabolic gene function encoded by chromosome II. J. Bacteriol. 179:7617-7624.
    • (1997) J. Bacteriol. , vol.179 , pp. 7617-7624
    • Mouncey, N.J.1    Choudhary, M.2    Kaplan, S.3
  • 58
    • 0031876196 scopus 로고    scopus 로고
    • Analysis of the puc operon promoter from Rhodobacter capsulatus
    • Nickens, D. G., and C. E. Bauer. 1998. Analysis of the puc operon promoter from Rhodobacter capsulatus. J. Bacteriol. 180:4270-4277.
    • (1998) J. Bacteriol. , vol.180 , pp. 4270-4277
    • Nickens, D.G.1    Bauer, C.E.2
  • 59
    • 0032054815 scopus 로고    scopus 로고
    • Growth, pigmentation, and expression of the puf and puc operons in a light-responding-repressor (SPB)-disrupted Rhodobacter sphaeroides
    • Nishimura K., H. Shimada, S. Hatanaka, H. Mizoguchi, H. Ohta, T. Masuda, and K. Takamiya. 1998. Growth, pigmentation, and expression of the puf and puc operons in a light-responding-repressor (SPB)-disrupted Rhodobacter sphaeroides. Plant Cell Physiol. 39:411-417.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 411-417
    • Nishimura, K.1    Shimada, H.2    Hatanaka, S.3    Mizoguchi, H.4    Ohta, H.5    Masuda, T.6    Takamiya, K.7
  • 60
    • 0030897418 scopus 로고    scopus 로고
    • Evidence for the role of redox carriers in photosynthesis gene expression and carotenoid biosynthesis in Rhodobacter sphaeroides. 2.4.1
    • O'Gara, J. P., J. M. Eraso, and S. Kaplan. 1998. Evidence for the role of redox carriers in photosynthesis gene expression and carotenoid biosynthesis in Rhodobacter sphaeroides. 2.4.1. J. Bacteriol. 179:1951-1961.
    • (1998) J. Bacteriol. , vol.179 , pp. 1951-1961
    • O'Gara, J.P.1    Eraso, J.M.2    Kaplan, S.3
  • 61
    • 0031829887 scopus 로고    scopus 로고
    • A redox-responsive pathway for aerobic regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1
    • O'Gara, J. P., and S. Kaplan. 1997. A redox-responsive pathway for aerobic regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 180:4044-4050.
    • (1997) J. Bacteriol. , vol.180 , pp. 4044-4050
    • O'Gara, J.P.1    Kaplan, S.2
  • 62
    • 0034034325 scopus 로고    scopus 로고
    • Interacting regulatory circuits involved in orderly control of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1
    • Oh, J.-I., J. M. Eraso, and S. Kaplan. 2000. Interacting regulatory circuits involved in orderly control of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 182:3081-3087.
    • (2000) J. Bacteriol. , vol.182 , pp. 3081-3087
    • Oh, J.-I.1    Eraso, J.M.2    Kaplan, S.3
  • 63
    • 0033514508 scopus 로고    scopus 로고
    • 3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: Structural and functional implications for the regulation of spectral complex formation
    • 3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation. Biochemistry 38:2688-2696.
    • (1999) Biochemistry , vol.38 , pp. 2688-2696
    • Oh, J.-I.1    Kaplan, S.2
  • 64
    • 0034664042 scopus 로고    scopus 로고
    • Redox signaling: Globalization of gene expression
    • Oh, J.-I., and S. Kaplan. 2000. Redox signaling: globalization of gene expression. EMBO J. 19:4237-4247.
    • (2000) EMBO J. , vol.19 , pp. 4237-4247
    • Oh, J.-I.1    Kaplan, S.2
  • 65
    • 0035107555 scopus 로고    scopus 로고
    • Generalized approach to the regulation and integration of gene expression
    • Oh, J.-I., and S. Kaplan. 2001. Generalized approach to the regulation and integration of gene expression. Mol. Microbiol. 39:1116-1123.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1116-1123
    • Oh, J.-I.1    Kaplan, S.2
  • 66
    • 0037013310 scopus 로고    scopus 로고
    • 3 cytochrome c oxidase of Rhodobacter sphaeroides 2.4.1
    • 3 cytochrome c oxidase of Rhodobacter sphaeroides 2.4.1. J. Biol. Chem. 277:16220-16228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16220-16228
    • Oh, J.I.1    Kaplan, S.2
  • 67
    • 0035164698 scopus 로고    scopus 로고
    • The default state of the membrane-localized histidine kinase PrrB of Rhodobacter sphaeroides 2.4.1 is in the kinase-positive mode
    • Oh, J. I., I. J. Ko, and S. Kaplan. 2001 The default state of the membrane-localized histidine kinase PrrB of Rhodobacter sphaeroides 2.4.1 is in the kinase-positive mode. J. Bacteriol. 183:6807-6814.
    • (2001) J. Bacteriol. , vol.183 , pp. 6807-6814
    • Oh, J.I.1    Ko, I.J.2    Kaplan, S.3
  • 68
    • 0033546279 scopus 로고    scopus 로고
    • Topological analysis of the membrane-localized redox-responsive sensor kinase PrrB from Rhodobacter sphaeroides 2.4.1
    • Ouchane, S., and S. Kaplan. 1999. Topological analysis of the membrane-localized redox-responsive sensor kinase PrrB from Rhodobacter sphaeroides 2.4.1. J. Biol. Chem. 274:17290-17296.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17290-17296
    • Ouchane, S.1    Kaplan, S.2
  • 69
    • 0031876149 scopus 로고    scopus 로고
    • Physiological control and regulation of the Rhodobacter capsulatus cbb operons
    • Paoli, G. C., P. Vichivanives, and F. R. Tabita. 1998. Physiological control and regulation of the Rhodobacter capsulatus cbb operons. J. Bacteriol. 180:4258-4269.
    • (1998) J. Bacteriol. , vol.180 , pp. 4258-4269
    • Paoli, G.C.1    Vichivanives, P.2    Tabita, F.R.3
  • 70
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 71
    • 0028353302 scopus 로고
    • Cloning and nucleotide sequence of regA, a putative response regulator gene of Rhodobacter sphaeroides
    • Phillips-Jones, M. K., and C. N. Hunter. 1994. Cloning and nucleotide sequence of regA, a putative response regulator gene of Rhodobacter sphaeroides. FEMS Microbiol. Lett. 116:269-275.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 269-275
    • Phillips-Jones, M.K.1    Hunter, C.N.2
  • 72
    • 0028999161 scopus 로고
    • Characterization of an aerobic repressor that coordinately regulates bacteriochlorophyll, carotenoid, and light harvesting-II expression in Rhodobacter capsulatus
    • Ponnampalam, S. N., J. J. Buggy, and C. E. Bauer. 1995. Characterization of an aerobic repressor that coordinately regulates bacteriochlorophyll, carotenoid, and light harvesting-II expression in Rhodobacter capsulatus. J. Bacteriol. 177:2990-2997.
    • (1995) J. Bacteriol. , vol.177 , pp. 2990-2997
    • Ponnampalam, S.N.1    Buggy, J.J.2    Bauer, C.E.3
  • 73
    • 0030747910 scopus 로고    scopus 로고
    • DNA Binding characteristics of CrtJ: A redox-responding repressor of bacteriochlorophyll, carotenoid and light harvesting-II gene expression in Rhodobacter capsulatus
    • Ponnampalam, S. N., and C. E. Bauer. 1997. DNA Binding characteristics of CrtJ: a redox-responding repressor of bacteriochlorophyll, carotenoid and light harvesting-II gene expression in Rhodobacter capsulatus. J. Biol. Chem. 272:9671-9676.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9671-9676
    • Ponnampalam, S.N.1    Bauer, C.E.2
  • 74
    • 0036296323 scopus 로고    scopus 로고
    • Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides
    • Potter, C. A., A. Ward, C. Laguri, M. P. Williamson, P. J. Henderson, and M. K. Phillips-Jones. 2002. Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides. J. Mol. Biol. 320:201-213.
    • (2002) J. Mol. Biol. , vol.320 , pp. 201-213
    • Potter, C.A.1    Ward, A.2    Laguri, C.3    Williamson, M.P.4    Henderson, P.J.5    Phillips-Jones, M.K.6
  • 75
    • 0030046502 scopus 로고    scopus 로고
    • 2 fixation in Rhodobacter sphaeroides
    • 2 fixation in Rhodobacter sphaeroides. J. Bacteriol. 178:12-18.
    • (1996) J. Bacteriol. , vol.178 , pp. 12-18
    • Qian, Y.1    Tabita, F.R.2
  • 76
    • 0034039548 scopus 로고    scopus 로고
    • Genetic and phenotypic analyses of the rdx locus of Rhodobacter sphaeroides 2.4.1
    • Roh, J. H., and S. Kaplan. 2000. Genetic and phenotypic analyses of the rdx locus of Rhodobacter sphaeroides 2.4.1. J. Bacteriol. 182:3475-3481.
    • (2000) J. Bacteriol. , vol.182 , pp. 3475-3481
    • Roh, J.H.1    Kaplan, S.2
  • 77
    • 0036786855 scopus 로고    scopus 로고
    • Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N
    • Romagnoli, S., H. L. Packer, and J. P. Armitage. 2002. Tactic responses to oxygen in the phototrophic bacterium Rhodobacter sphaeroides WS8N. J. Bacteriol. 184:5590-5598.
    • (2002) J. Bacteriol. , vol.184 , pp. 5590-5598
    • Romagnoli, S.1    Packer, H.L.2    Armitage, J.P.3
  • 78
    • 0026585783 scopus 로고
    • Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expression in Rhodobacter capsulatus
    • Sganga, M. W., and C. E. Bauer. 1992. Regulatory factors controlling photosynthetic reaction center and light-harvesting gene expression in Rhodobacter capsulatus. Cell 68:945-954.
    • (1992) Cell , vol.68 , pp. 945-954
    • Sganga, M.W.1    Bauer, C.E.2
  • 79
    • 0033049616 scopus 로고    scopus 로고
    • Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus
    • Shaw, A. L., S. Leimkuhler, W. Klipp, G. R. Hanson, and A. G. McEwan. 1999. Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus. Microbiology 145:1409-1420.
    • (1999) Microbiology , vol.145 , pp. 1409-1420
    • Shaw, A.L.1    Leimkuhler, S.2    Klipp, W.3    Hanson, G.R.4    McEwan, A.G.5
  • 80
    • 0030174976 scopus 로고    scopus 로고
    • A transcription factor with a leucine-zipper motif involved in light-dependent inhibition of expression of the puf operon in the photosynthetic bacterium Rhodobacter sphaeroides
    • Shimada, H., T. Wada, H. Handa, H. Ohta, H. Mizoguchi, K. Nishimura, T. Masuda, Y. Shioi, and K. Takamiya. 1996. A transcription factor with a leucine-zipper motif involved in light-dependent inhibition of expression of the puf operon in the photosynthetic bacterium Rhodobacter sphaeroides. Plant Cell Physiol. 37:515-521.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 515-521
    • Shimada, H.1    Wada, T.2    Handa, H.3    Ohta, H.4    Mizoguchi, H.5    Nishimura, K.6    Masuda, T.7    Shioi, Y.8    Takamiya, K.9
  • 81
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., A. J. Ninfa, and A. M. Stock. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53:450-490.
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 83
    • 0035946912 scopus 로고    scopus 로고
    • The RegB/RegA two-component regulatory system controls synthesis of photosynthetic and respiratory electron transfer components in Rhodobacter capsulatus
    • Swem, L., S. Elsen, T. H. Bird, H.-G. Koch, H. Myllykallio, F. Daldal, and C. E. Bauer. 2001. The RegB/RegA two-component regulatory system controls synthesis of photosynthetic and respiratory electron transfer components in Rhodobacter capsulatus. J. Mol. Biol. 309:121-138.
    • (2001) J. Mol. Biol. , vol.309 , pp. 121-138
    • Swem, L.1    Elsen, S.2    Bird, T.H.3    Koch, H.-G.4    Myllykallio, H.5    Daldal, F.6    Bauer, C.E.7
  • 85
    • 0036233407 scopus 로고    scopus 로고
    • 3 oxidase expression by multiple regulators in Rhodobacter-capsulatus
    • 3 oxidase expression by multiple regulators in Rhodobacter-capsulatus. J. Bacteriol. 184:2815-2820.
    • (2002) J. Bacteriol. , vol.184 , pp. 2815-2820
    • Swem, D.L.1    Bauer, C.E.2
  • 86
    • 0000947778 scopus 로고
    • 2 fixation in purple bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 2 fixation in purple bacteria, p. 885-914. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 885-914
    • Tabita, F.R.1
  • 87
    • 0027969974 scopus 로고
    • The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus
    • Thöny-Meyer, L., C. Beck, O. Preisig, and H. Hennecke. 1994. The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus. Mol. Microbiol. 174:705-716.
    • (1994) Mol. Microbiol. , vol.174 , pp. 705-716
    • Thöny-Meyer, L.1    Beck, C.2    Preisig, O.3    Hennecke, H.4
  • 88
    • 0035688827 scopus 로고    scopus 로고
    • Interactive control of Rhodobacter capsulatus redox-balancing systems during phototrophic metabolism
    • Tichi, M. A., and F. R. Tabita. 2001. Interactive control of Rhodobacter capsulatus redox-balancing systems during phototrophic metabolism. J. Bacteriol. 183:6344-6354.
    • (2001) J. Bacteriol. , vol.183 , pp. 6344-6354
    • Tichi, M.A.1    Tabita, F.R.2
  • 89
    • 0033712708 scopus 로고    scopus 로고
    • Maintenance and control of redox poise in Rhodobacter capsulatus strains deficient in the Calvin-Benson-Bassham pathway
    • Tichi, M. A., and F. R. Tabita. 2000. Maintenance and control of redox poise in Rhodobacter capsulatus strains deficient in the Calvin-Benson-Bassham pathway. Arch. Microbiol. 174:322-333.
    • (2000) Arch. Microbiol. , vol.174 , pp. 322-333
    • Tichi, M.A.1    Tabita, F.R.2
  • 90
    • 0029977023 scopus 로고    scopus 로고
    • Acid tolerance in Rhizobium meliloti strain WSM419 involves a two-component sensor-regulator system
    • Tiwari, R. P., W. G. Reeve, M. J. Dilworth, and A. R. Glenn. 1996. Acid tolerance in Rhizobium meliloti strain WSM419 involves a two-component sensor-regulator system. Microbiology 142:1693-1704.
    • (1996) Microbiology , vol.142 , pp. 1693-1704
    • Tiwari, R.P.1    Reeve, W.G.2    Dilworth, M.J.3    Glenn, A.R.4
  • 91
    • 0026764408 scopus 로고
    • 1 complex, is homologous to bacterial response regulators and necessary for photosynthetic and respiratory growth of Rhodobacter capsulatus
    • 1 complex, is homologous to bacterial response regulators and necessary for photosynthetic and respiratory growth of Rhodobacter capsulatus. Mol. Microbiol. 6:1645-1654.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1645-1654
    • Tokito, M.K.1    Daldal, F.2
  • 93
    • 0034725524 scopus 로고    scopus 로고
    • Multiple regulators and their interactions in vivo and in vitro with the cbb regulons of Rhodobacter capsulatus
    • Vichivanives, P., T. H. Bird, C. E. Bauer, and F. R. Tabita. 2000. Multiple regulators and their interactions in vivo and in vitro with the cbb regulons of Rhodobacter capsulatus. J. Mol. Biol. 300:1079-1099.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1079-1099
    • Vichivanives, P.1    Bird, T.H.2    Bauer, C.E.3    Tabita, F.R.4
  • 94
    • 0002226012 scopus 로고
    • Regulation of hydrogenase gene expression
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Vignais, P. M., B. Toussaint, and A. Colbeau. 1995. Regulation of hydrogenase gene expression, p. 1175-1190. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1175-1190
    • Vignais, P.M.1    Toussaint, B.2    Colbeau, A.3
  • 95
    • 0001888153 scopus 로고
    • Aerobic and anaerobic transport chains in anoxygenic phototrophic bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Zannoni, D. 1995. Aerobic and anaerobic transport chains in anoxygenic phototrophic bacteria, p. 949-971. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 949-971
    • Zannoni, D.1


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