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Volumn 50, Issue 4, 2004, Pages 225-238

Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)

Author keywords

Dms; DMSO reductase; Fdh; Formate dehydrogenase; Hya; Hyb; Hydrogenase; Nap; Nitrate reductase; Tat translocase; TMAO reductase; Tor; Twin arginine leader

Indexed keywords

BACTERIOLOGY; BIOSYNTHESIS; COMPETITION; COMPLEXATION; MICROBIOLOGY; NITRATES; REDOX REACTIONS; REDUCTION; SUBSTRATES; TRANSPORT PROPERTIES;

EID: 3142550604     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/w03-117     Document Type: Review
Times cited : (91)

References (101)
  • 1
    • 0028860781 scopus 로고
    • Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase
    • Abaibou, H., Pommier, J., Benoit, S., Giordano, G., and Mandrand-Berthelot, M.A. 1995. Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J. Bacteriol. 177: 7141-7149.
    • (1995) J. Bacteriol. , vol.177 , pp. 7141-7149
    • Abaibou, H.1    Pommier, J.2    Benoit, S.3    Giordano, G.4    Mandrand-Berthelot, M.A.5
  • 2
    • 0041656271 scopus 로고    scopus 로고
    • Energy use by biological protein transport pathways
    • Alder, N.N., and Theg, S.M. 2003. Energy use by biological protein transport pathways. Trends Biochem. Sci. 28: 442-451.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 442-451
    • Alder, N.N.1    Theg, S.M.2
  • 4
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Reading, UK
    • Andrews, S.C., Berks, B.C., McClay, J., Ambler, A., Quail, M.A., Golby, P., and Guest, J.R. 1997. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology (Reading, UK), 143: 3633-3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 5
    • 0027258545 scopus 로고
    • Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes
    • Augier, V., Asso, M., Guigliarelli, B., More, C., Bertrand, P., Santini, C.L., Blasco, F., Chippaux, M., and Giordano, G. 1993a. Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes. Biochemistry, 32: 5099-5108.
    • (1993) Biochemistry , vol.32 , pp. 5099-5108
    • Augier, V.1    Asso, M.2    Guigliarelli, B.3    More, C.4    Bertrand, P.5    Santini, C.L.6    Blasco, F.7    Chippaux, M.8    Giordano, G.9
  • 6
    • 0027406134 scopus 로고
    • Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes
    • Augier, V., Guigliarelli, B., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Chippaux, M., and Blasco, F. 1993b. Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes. Biochemistry, 32: 2013-2023.
    • (1993) Biochemistry , vol.32 , pp. 2013-2023
    • Augier, V.1    Guigliarelli, B.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Chippaux, M.7    Blasco, F.8
  • 7
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • Ballantine, S.P., and Boxer, D.H. 1985. Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J. Bacteriol. 163: 454-459.
    • (1985) J. Bacteriol. , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 8
    • 0023049446 scopus 로고
    • Isolation and characterization of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli
    • Ballantine, S.P., and Boxer, D.H. 1986. Isolation and characterization of a soluble active fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grown Escherichia coli. Eur. J. Biochem. 156: 277-284.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 277-284
    • Ballantine, S.P.1    Boxer, D.H.2
  • 9
    • 0025791979 scopus 로고
    • Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. II. Evidence that a mRNA stem-loop structure is essential for decoding opal (UGA) as selenocysteine
    • Berg, B.L., Baron, C., and Stewart, V. 1991. Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. II. Evidence that a mRNA stem-loop structure is essential for decoding opal (UGA) as selenocysteine. J. Biol. Chem. 266: 22 386-22 391.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22386-22391
    • Berg, B.L.1    Baron, C.2    Stewart, V.3
  • 10
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B.C. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22: 393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 11
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks, B.C., Ferguson, S.J., Moir, J.W., and Richardson, D.J. 1995a. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta, 1232: 97-173.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.3    Richardson, D.J.4
  • 12
    • 0028944291 scopus 로고
    • Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
    • Berks, B.C., Page, M.D., Richardson, D.J., Reilly, A., Cavill, A., Outen, F., and Ferguson, S.J. 1995b. Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop. Mol. Microbiol. 15: 319-331.
    • (1995) Mol. Microbiol. , vol.15 , pp. 319-331
    • Berks, B.C.1    Page, M.D.2    Richardson, D.J.3    Reilly, A.4    Cavill, A.5    Outen, F.6    Ferguson, S.J.7
  • 13
    • 0029160337 scopus 로고
    • The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
    • Berks, B.C., Richardson, D.J., Reilly, A., Willis, A.C., and Ferguson, S.J. 1995c. The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. Biochem. J. 309: 983-992.
    • (1995) Biochem. J. , vol.309 , pp. 983-992
    • Berks, B.C.1    Richardson, D.J.2    Reilly, A.3    Willis, A.C.4    Ferguson, S.J.5
  • 15
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks, B.C., Palmer, T., and Sargent, F. 2003. The Tat protein translocation pathway and its role in microbial physiology. Adv. Microb. Physiol. 47: 187-254.
    • (2003) Adv. Microb. Physiol. , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 16
    • 0021889335 scopus 로고
    • Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101
    • Bilous, P.T., and Weiner, J.H. 1985. Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101. J. Bacteriol. 163: 369-375.
    • (1985) J. Bacteriol. , vol.163 , pp. 369-375
    • Bilous, P.T.1    Weiner, J.H.2
  • 17
    • 0023988002 scopus 로고
    • Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon
    • Bilous, P.T., and Weiner, J.H. 1988. Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon. J. Bacteriol. 170: 1511-1518.
    • (1988) J. Bacteriol. , vol.170 , pp. 1511-1518
    • Bilous, P.T.1    Weiner, J.H.2
  • 18
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • Bilous, P.T., Cole, S.T., Anderson, W.F., and Weiner, J.H. 1988. Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2: 785-795.
    • (1988) Mol. Microbiol. , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 19
    • 0024713468 scopus 로고
    • Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer
    • Blasco, F., Iobbi, C., Giordano, G., Chippaux, M., and Bonnefoy, V. 1989. Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. Mol. Gen. Genet. 218: 249-256.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 249-256
    • Blasco, F.1    Iobbi, C.2    Giordano, G.3    Chippaux, M.4    Bonnefoy, V.5
  • 20
    • 0025368948 scopus 로고
    • Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon
    • Blasco, F., Iobbi, C., Ratouchniak, J., Bonnefoy, V., and Chippaux, M. 1990. Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol. Gen. Genet. 222: 104-111.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 104-111
    • Blasco, F.1    Iobbi, C.2    Ratouchniak, J.3    Bonnefoy, V.4    Chippaux, M.5
  • 21
    • 0026512058 scopus 로고
    • Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli
    • Blasco, F., Pommier, J., Augier, V., Chippaux, M., and Giordano, G. 1992. Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli. Mol. Microbiol. 6: 221-230.
    • (1992) Mol. Microbiol. , vol.6 , pp. 221-230
    • Blasco, F.1    Pommier, J.2    Augier, V.3    Chippaux, M.4    Giordano, G.5
  • 22
  • 23
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Bohm, R., Sauter, M., and Bock, A. 1990. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4: 231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Bohm, R.1    Sauter, M.2    Bock, A.3
  • 24
  • 25
    • 0036229614 scopus 로고    scopus 로고
    • Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation
    • Brondijk, T.H., Fiegen, D., Richardson, D.J., and Cole, J.A. 2003. Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation. Mol. Microbiol. 44: 245-255.
    • (2003) Mol. Microbiol. , vol.44 , pp. 245-255
    • Brondijk, T.H.1    Fiegen, D.2    Richardson, D.J.3    Cole, J.A.4
  • 26
    • 0025088388 scopus 로고
    • Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli
    • Cammack, R., and Weiner, J.H. 1990. Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli. Biochemistry, 29: 8410-8416.
    • (1990) Biochemistry , vol.29 , pp. 8410-8416
    • Cammack, R.1    Weiner, J.H.2
  • 27
    • 0035340936 scopus 로고    scopus 로고
    • Maturation of the [NiFe] hydrogenases
    • Casalot, L., and Rousset, M. 2001. Maturation of the [NiFe] hydrogenases. Trends Microbiol. 9: 228-237.
    • (2001) Trends Microbiol. , vol.9 , pp. 228-237
    • Casalot, L.1    Rousset, M.2
  • 28
    • 0001879359 scopus 로고    scopus 로고
    • Alternative gene for Biotin sulfoxide reduction in Escherichia coli K-12
    • del Campillo Campbell, A., and Cambell, A. 1996. Alternative gene for Biotin sulfoxide reduction in Escherichia coli K-12. J. Mol. Evol. 42: 85-90.
    • (1996) J. Mol. Evol. , vol.42 , pp. 85-90
    • Del Campillo Campbell, A.1    Cambell, A.2
  • 29
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M.P., Tullman, D., and Georgiou, G. 2003. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA. 100: 6115-6120.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 31
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: Identification of precursor-binding accessory proteins
    • Dubini, A., and Sargent, F. 2003. Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett. 549: 141-146.
    • (2003) FEBS Lett. , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 32
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • Dubini, A., Pye, R.L., Jack, R.L., Palmer, T., and Sargent, F. 2002. How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. Int. J. Hydrogen Energy, 27: 1413-1320.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1413-11320
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 33
    • 0016711942 scopus 로고
    • The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli
    • Enoch, H.G., and Lester, R.L. 1975. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J. Biol. Chem. 250: 6693-6705.
    • (1975) J. Biol. Chem. , vol.250 , pp. 6693-6705
    • Enoch, H.G.1    Lester, R.L.2
  • 35
    • 0033591263 scopus 로고    scopus 로고
    • Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli
    • Fritsche, E., Paschos, A., Beisel, H.G., Bock, A., and Huber, R. 1999. Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli. J. Mol. Biol. 288: 989-998.
    • (1999) J. Mol. Biol. , vol.288 , pp. 989-998
    • Fritsche, E.1    Paschos, A.2    Beisel, H.G.3    Bock, A.4    Huber, R.5
  • 36
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • Edited by F.C. Neidhardt, R. Curtis, III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, and H.E. Umbarger. American Society for Microbiology, Washington, D.C.
    • Gennis, R.B., and Stewart, V. 1996. Respiration. In Escherichia coli and Salmonella: cellular and molecular biology. 2nd ed. Edited by F.C. Neidhardt, R. Curtis, III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, and H.E. Umbarger. American Society for Microbiology, Washington, D.C. pp. 217-261.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology. 2nd Ed. , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 37
    • 0033814270 scopus 로고    scopus 로고
    • The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli
    • Gon, S., Patte, J.C., Mejean, V., and Iobbi-Nivol, C. 2000. The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli. J. Bacteriol. 182: 5779-5786.
    • (2000) J. Bacteriol. , vol.182 , pp. 5779-5786
    • Gon, S.1    Patte, J.C.2    Mejean, V.3    Iobbi-Nivol, C.4
  • 38
    • 0030033752 scopus 로고    scopus 로고
    • Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
    • Grove, J., Tanapongpipat, S., Thomas, G., Griffiths, L., Crooke, H., and Cole, J. 1996. Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm. Mol. Microbiol. 19: 467-481.
    • (1996) Mol. Microbiol. , vol.19 , pp. 467-481
    • Grove, J.1    Tanapongpipat, S.2    Thomas, G.3    Griffiths, L.4    Crooke, H.5    Cole, J.6
  • 39
    • 0026442487 scopus 로고
    • Oxygen-regulated gene expression in Escherichia coli. The 1992 Marjory Stephenson Prize Lecture
    • Guest, J.R. 1992. Oxygen-regulated gene expression in Escherichia coli. The 1992 Marjory Stephenson Prize Lecture. J. Gen. Microbiol. 138: 2253-2263.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2253-2263
    • Guest, J.R.1
  • 40
    • 0026741957 scopus 로고
    • EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism
    • Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G., and Bertrand, P. 1992. EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism. Eur. J. Biochem. 207: 61-68.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 61-68
    • Guigliarelli, B.1    Asso, M.2    More, C.3    Augier, V.4    Blasco, F.5    Pommier, J.6    Giordano, G.7    Bertrand, P.8
  • 41
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters
    • Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G., and Blasco, F. 1996. Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters. Biochemistry, 35: 4828-4836.
    • (1996) Biochemistry , vol.35 , pp. 4828-4836
    • Guigliarelli, B.1    Magalon, A.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Blasco, F.7
  • 42
    • 0036854448 scopus 로고    scopus 로고
    • Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica
    • Reading, UK
    • Hinsley, A.P., and Berks, B.C. 2002. Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica. Microbiology (Reading, UK), 148: 3631-3638.
    • (2002) Microbiology , vol.148 , pp. 3631-3638
    • Hinsley, A.P.1    Berks, B.C.2
  • 43
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli: Role of accessory proteins HypA and HybF
    • Hube, M., Blokesch, M., and Bock, A. 2002. Network of hydrogenase maturation in Escherichia coli: role of accessory proteins HypA and HybF. J. Bacteriol. 184: 3879-3885.
    • (2002) J. Bacteriol. , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Bock, A.3
  • 44
    • 0043209015 scopus 로고    scopus 로고
    • Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA
    • Ilbert, M., Méjean, V., Giudici-Orticoni, M.-T., Samama, J.-P., and Iobbi-Nivol, C. 2003. Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA. J. Biol. Chem. 278: 28 787-28 792,
    • (2003) J. Biol. Chem. , vol.278 , pp. 28787-28792
    • Ilbert, M.1    Méjean, V.2    Giudici-Orticoni, M.-T.3    Samama, J.-P.4    Iobbi-Nivol, C.5
  • 45
    • 0023656328 scopus 로고
    • Biochemical and immunological evidence for a second nitrate reductase in Escherichia coli K12
    • Iobbi, C., Santini, C.L., Bonnefoy, V., and Giordano, G. 1987. Biochemical and immunological evidence for a second nitrate reductase in Escherichia coli K12. Eur. J. Biochem. 168: 451-459.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 451-459
    • Iobbi, C.1    Santini, C.L.2    Bonnefoy, V.3    Giordano, G.4
  • 46
    • 0025355135 scopus 로고
    • Purification and further characterization of the second nitrate reductase of Escherichia coli K12
    • Iobbi-Nivol, C., Santini, C.L., Blasco, F., and Giordano, G. 1990. Purification and further characterization of the second nitrate reductase of Escherichia coli K12. Eur. J. Biochem. 188: 679-687.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 679-687
    • Iobbi-Nivol, C.1    Santini, C.L.2    Blasco, F.3    Giordano, G.4
  • 47
    • 0026446645 scopus 로고
    • The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli
    • Jacobi, A., Rossmann, R., and Bock, A. 1992. The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli. Arch. Microbiol. 158: 444-451.
    • (1992) Arch. Microbiol. , vol.158 , pp. 444-451
    • Jacobi, A.1    Rossmann, R.2    Bock, A.3
  • 49
  • 50
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Washington, D.C.
    • Jormakka, M., Tornroth, S., Byrne, B., and Iwata, S. 2002b. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science (Washington, D.C.), 295: 1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 51
    • 0141651638 scopus 로고    scopus 로고
    • The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC)
    • Lubitz, S.P., and Weiner, J.H. 2003. The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC). Arch. Biochem. Biophys. 418: 205-216.
    • (2003) Arch. Biochem. Biophys. , vol.418 , pp. 205-216
    • Lubitz, S.P.1    Weiner, J.H.2
  • 52
    • 0027142232 scopus 로고
    • Newly imported Rieske iron-sulfur protein associates with both Cpn60 and Hsp70 in the chloroplast stroma
    • Madueno, F., Napier, J.A., and Gray, J.C. 1993. Newly imported Rieske iron-sulfur protein associates with both Cpn60 and Hsp70 in the chloroplast stroma. Plant Cell, 5: 1865-1876.
    • (1993) Plant Cell , vol.5 , pp. 1865-1876
    • Madueno, F.1    Napier, J.A.2    Gray, J.C.3
  • 53
    • 0030845184 scopus 로고    scopus 로고
    • Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A
    • Magalon, A., Lemesle-Meunier, D., Rothery, R.A., Frixon, C., Weiner, J.H., and Blasco, F. 1997a. Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A. J. Biol. Chem. 272: 25 652-25 658.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25652-25658
    • Magalon, A.1    Lemesle-Meunier, D.2    Rothery, R.A.3    Frixon, C.4    Weiner, J.H.5    Blasco, F.6
  • 54
    • 0030742055 scopus 로고    scopus 로고
    • Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate
    • Magalon, A., Rothery, R.A., Giordano, G., Blasco, F., and Weiner, J.H. 1997b. Characterization by electron paramagnetic resonance of the role of the Escherichia coli nitrate reductase (NarGHI) iron-sulfur clusters in electron transfer to nitrate and identification of a semiquinone radical intermediate. J. Bacteriol. 179: 5037-5045.
    • (1997) J. Bacteriol. , vol.179 , pp. 5037-5045
    • Magalon, A.1    Rothery, R.A.2    Giordano, G.3    Blasco, F.4    Weiner, J.H.5
  • 55
    • 0024146809 scopus 로고
    • Mutants of Escherichia coli specifically deficient in respiratory formate dehydrogenase activity
    • Mandrand-Berthelot, M.A., Couchoux-Luthaud, G., Santini, C.L., and Giordano, G. 1988. Mutants of Escherichia coli specifically deficient in respiratory formate dehydrogenase activity. J. Gen. Microbiol. 134(Pt 12): 3129-3139.
    • (1988) J. Gen. Microbiol. , vol.134 , Issue.12 PART , pp. 3129-3139
    • Mandrand-Berthelot, M.A.1    Couchoux-Luthaud, G.2    Santini, C.L.3    Giordano, G.4
  • 56
    • 0036016822 scopus 로고    scopus 로고
    • Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethly sulphoxide reductase family of microbial molybdopterin-containing enzymes
    • McDevitt, C.A., Hugenholtz, P., Hanson, G.R., and McEwan, A.G. 2002. Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethly sulphoxide reductase family of microbial molybdopterin-containing enzymes. Mol. Microbiol. 44: 1575-1587.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1575-1587
    • McDevitt, C.A.1    Hugenholtz, P.2    Hanson, G.R.3    McEwan, A.G.4
  • 57
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K., and Jones, D.T. 2000. The PSIPRED protein structure prediction server. Bioinformatics, 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 59
    • 0025366313 scopus 로고
    • Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames
    • Menon, N.K., Robbins, J., Peck, H.D.J., Chatelus, C.Y., Choi, E.S., and Przybyla, A.E. 1990. Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames. J. Bacteriol. 172: 1969-1977.
    • (1990) J. Bacteriol. , vol.172 , pp. 1969-1977
    • Menon, N.K.1    Robbins, J.2    Peck, H.D.J.3    Chatelus, C.Y.4    Choi, E.S.5    Przybyla, A.E.6
  • 60
    • 0025914936 scopus 로고
    • Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1
    • Menon, N.K., Robbins, J., Wendt, J.C., Shanmugam, K.T., and Przybyla, A.E. 1991. Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1. J. Bacteriol. 173: 4851-4861.
    • (1991) J. Bacteriol. , vol.173 , pp. 4851-4861
    • Menon, N.K.1    Robbins, J.2    Wendt, J.C.3    Shanmugam, K.T.4    Przybyla, A.E.5
  • 62
    • 0026646678 scopus 로고
    • Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein
    • Niviere, V., Wong, S.L., and Voordouw, G. 1992. Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein. J. Gen. Microbiol. 138: 2173-2183.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2173-2183
    • Niviere, V.1    Wong, S.L.2    Voordouw, G.3
  • 63
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader binding for the Sec-independent translocase
    • Oresnik, I., Ladner, C.L., and Turner, R.J. 2001. Identification of a twin-arginine leader binding for the Sec-independent translocase. Mol. Microbiol. 40: 323-331.
    • (2001) Mol. Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.1    Ladner, C.L.2    Turner, R.J.3
  • 64
    • 0037352234 scopus 로고    scopus 로고
    • Moving folded proteins across the bacterial cell membrane
    • Reading, UK
    • Palmer, T., and Berks, B.C. 2003. Moving folded proteins across the bacterial cell membrane. Microbiology (Reading, UK), 149: 547-556.
    • (2003) Microbiology , vol.149 , pp. 547-556
    • Palmer, T.1    Berks, B.C.2
  • 65
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • Palmer, T., Santini, C.L., Iobbi-Nivol, C., Eaves, D.J., Boxer, D.H., and Giordano, G. 1996. Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol. Microbiol. 20: 875-884.
    • (1996) Mol. Microbiol. , vol.20 , pp. 875-884
    • Palmer, T.1    Santini, C.L.2    Iobbi-Nivol, C.3    Eaves, D.J.4    Boxer, D.H.5    Giordano, G.6
  • 66
    • 0027219606 scopus 로고
    • Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 min
    • Plunkett, G.R., Burland, V., Daniels, D.L., and Blattner, F.R. 1993. Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 min. Nucleic Acids Res. 21: 3391-3398.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3391-3398
    • Plunkett, G.R.1    Burland, V.2    Daniels, D.L.3    Blattner, F.R.4
  • 67
    • 0031022332 scopus 로고    scopus 로고
    • Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme
    • Pollock, V.V., and Barber, M.J. 1997. Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme. J. Biol. Chem. 272: 3355-3362.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3355-3362
    • Pollock, V.V.1    Barber, M.J.2
  • 68
    • 0026683497 scopus 로고
    • A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichla coli
    • Pommier, J., Mandrand, M.A., Holt, S.E., Boxer, D.H., and Giordano, G. 1992. A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichla coli. Biochim. Biophys. Acta, 1107: 305-313.
    • (1992) Biochim. Biophys. Acta , vol.1107 , pp. 305-313
    • Pommier, J.1    Mandrand, M.A.2    Holt, S.E.3    Boxer, D.H.4    Giordano, G.5
  • 69
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethlyamine N-oxide reductase enzyme (TorA) in Escherichia coli
    • Pommier, J., Mejean, V., Giordano, G., and Iobbi-Nivol, C. 1998. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethlyamine N-oxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273: 16 615-16 620.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16615-16620
    • Pommier, J.1    Mejean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 70
    • 0033571287 scopus 로고    scopus 로고
    • Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
    • Potter, L.C., and Cole, J.A. 1999. Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12. Biochem. J. 344(Pt 1): 69-76.
    • (1999) Biochem. J. , vol.344 , Issue.1 PART , pp. 69-76
    • Potter, L.C.1    Cole, J.A.2
  • 71
    • 0033571051 scopus 로고    scopus 로고
    • Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: Does Nap confer a selective advantage during nitrate-limited growth?
    • Potter, L.C., Millington, P., Griffiths, L., Thomas, G.H., and Cole, J.A. 1999. Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth? Biochem. J. 344(Pt 1): 77-84.
    • (1999) Biochem. J. , vol.344 , Issue.1 PART , pp. 77-84
    • Potter, L.C.1    Millington, P.2    Griffiths, L.3    Thomas, G.H.4    Cole, J.A.5
  • 72
    • 0032079782 scopus 로고    scopus 로고
    • Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: Transcriptional and mutational analysis of the napKEFDABC gene cluster
    • Reyes, F., Gavira, M., Castillo, F., and Moreno-Vivian, C. 1998. Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: transcriptional and mutational analysis of the napKEFDABC gene cluster. Biochem. J. 331: 897-904.
    • (1998) Biochem. J. , vol.331 , pp. 897-904
    • Reyes, F.1    Gavira, M.2    Castillo, F.3    Moreno-Vivian, C.4
  • 74
    • 0034012712 scopus 로고    scopus 로고
    • The twin-arginine translocation system: A novel means of transporting folded proteins in chloroplasts and bacteria
    • Robinson, C. 2000. The twin-arginine translocation system: a novel means of transporting folded proteins in chloroplasts and bacteria. Biol. Chem. 381: 89-93.
    • (2000) Biol. Chem. , vol.381 , pp. 89-93
    • Robinson, C.1
  • 75
    • 0030603123 scopus 로고    scopus 로고
    • Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli
    • Rodrigue, A., Boxer, D.H., Mandrand-Berthelot, M.A., and Wu, L.F. 1996. Requirement for nickel of the transmembrane translocation of NiFe-hydrogenase 2 in Escherichia coli. FEBS Lett. 392: 81-86.
    • (1996) FEBS Lett. , vol.392 , pp. 81-86
    • Rodrigue, A.1    Boxer, D.H.2    Mandrand-Berthelot, M.A.3    Wu, L.F.4
  • 76
    • 0032582701 scopus 로고    scopus 로고
    • Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport
    • Roldan, M.D., Sears, H.J., Cheesman, M.R., Ferguson, S.J., Thomson, A.J., Berks, B.C., and Richardson, D.J. 1998. Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport. J. Biol. Chem. 273: 28 785-28 790.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28785-28790
    • Roldan, M.D.1    Sears, H.J.2    Cheesman, M.R.3    Ferguson, S.J.4    Thomson, A.J.5    Berks, B.C.6    Richardson, D.J.7
  • 77
    • 0028936979 scopus 로고
    • Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: Effect of tungstate and a mob mutation
    • Rothery, R.A., Grant, J.L., Johnson, J.L., Rajagopalan, K.V., and Weiner, J.H. 1995. Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation. J. Bacteriol. 177: 2057-2063.
    • (1995) J. Bacteriol. , vol.177 , pp. 2057-2063
    • Rothery, R.A.1    Grant, J.L.2    Johnson, J.L.3    Rajagopalan, K.V.4    Weiner, J.H.5
  • 78
    • 0032571394 scopus 로고    scopus 로고
    • The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters
    • Rothery, R.A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., and Weiner, J.H. 1998. The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters. J. Biol. Chem. 273: 7462-7469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7462-7469
    • Rothery, R.A.1    Magalon, A.2    Giordano, G.3    Guigliarelli, B.4    Blasco, F.5    Weiner, J.H.6
  • 79
    • 0036320337 scopus 로고    scopus 로고
    • Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase
    • Rubio, L.M., Flores, E., and Herrero, A. 2002. Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase. Photosynth. Res. 72: 13-26.
    • (2002) Photosynth. Res. , vol.72 , pp. 13-26
    • Rubio, L.M.1    Flores, E.2    Herrero, A.3
  • 80
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C.L., Ize, B., Chanal, A., Muller, M., Giordano, G., and Wu, L.-F. 1998. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17: 101-112.
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.-F.6
  • 81
    • 3142604150 scopus 로고    scopus 로고
    • (University of Calgary.) Unpublished data
    • Sarfo, K., and Turner, R.J. 2003. (University of Calgary.) Unpublished data.
    • (2003)
    • Sarfo, K.1    Turner, R.J.2
  • 82
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., Bogsch, E.G., Stanley, N.R., Wexler, M., Robinson, C., Berks, B.C., and Palmer, T. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17: 3640-3650.
    • (1998) EMBO J. , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 83
    • 0032146314 scopus 로고    scopus 로고
    • Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit - Identification of a soluble precursor of the small subunit in a hypB mutant
    • Sargent, P., Ballantine, S.P., Rugman, P.A., Palmer, T., and Boxer, D.H. 1998. Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit - identification of a soluble precursor of the small subunit in a hypB mutant. Eur. J. Biochem. 255: 746-754.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 746-754
    • Sargent, P.1    Ballantine, S.P.2    Rugman, P.A.3    Palmer, T.4    Boxer, D.H.5
  • 84
    • 0036311769 scopus 로고    scopus 로고
    • Assembly of membrane-bound respiratory complexes by the Tat protein-transport system
    • Sargent, F., Berks, B.C., and Palmer, T. 2002. Assembly of membrane-bound respiratory complexes by the Tat protein-transport system. Arch. Microbiol. 178: 77-84.
    • (2002) Arch. Microbiol. , vol.178 , pp. 77-84
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 85
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • Sauter, M., Bohm, R., and Bock, A. 1992. Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol. Microbiol. 6: 1523-1532.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1523-1532
    • Sauter, M.1    Bohm, R.2    Bock, A.3
  • 86
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R.G., Ballantine, S.P., and Boxer, D.H. 1985. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacteriol. 164: 1324-1331.
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 87
    • 0025074128 scopus 로고
    • Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase
    • Schlindwein, C., Giordano, G., Santini, C.L., and Mandrand, M.A. 1990. Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase. J. Bacteriol. 172: 6112-6121.
    • (1990) J. Bacteriol. , vol.172 , pp. 6112-6121
    • Schlindwein, C.1    Giordano, G.2    Santini, C.L.3    Mandrand, M.A.4
  • 88
    • 0030722626 scopus 로고    scopus 로고
    • Sec-independent protein translocation by the maize Hcf106 protein
    • Washington, D.C.
    • Settles, A.M., Yonetani, A., Baron, A., Bush, D.R., Cline, K., and Martienssen, R. 1997. Sec-independent protein translocation by the maize Hcf106 protein. Science (Washington, D.C.), 278: 1467-1470.
    • (1997) Science , vol.278 , pp. 1467-1470
    • Settles, A.M.1    Yonetani, A.2    Baron, A.3    Bush, D.R.4    Cline, K.5    Martienssen, R.6
  • 89
    • 0023988313 scopus 로고
    • narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes
    • Sodergren, E.J., and DeMoss, J.A. 1988. narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J. Bacteriol. 170: 1721-1729.
    • (1988) J. Bacteriol. , vol.170 , pp. 1721-1729
    • Sodergren, E.J.1    DeMoss, J.A.2
  • 90
    • 0027321764 scopus 로고
    • Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli
    • Stewart, V. 1993. Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli. Mol. Microbiol. 9: 425-434.
    • (1993) Mol. Microbiol. , vol.9 , pp. 425-434
    • Stewart, V.1
  • 91
    • 0028575650 scopus 로고
    • Regulation of nitrate and nitrite reductase synthesis in enterobacteria
    • Stewart, V. 1994. Regulation of nitrate and nitrite reductase synthesis in enterobacteria. Antonie Van Leeuwenhoek, 66: 37-45.
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 37-45
    • Stewart, V.1
  • 92
    • 0025856933 scopus 로고
    • Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12
    • Stewart, V., Lin, J.T., and Berg, B.L. 1991. Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12. J. Bacteriol. 173: 4417-4423.
    • (1991) J. Bacteriol. , vol.173 , pp. 4417-4423
    • Stewart, V.1    Lin, J.T.2    Berg, B.L.3
  • 93
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., and Higgins, D.G. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25: 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 94
    • 0036707997 scopus 로고    scopus 로고
    • Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA
    • Tranier, S., Mortier-Barriere, I., Ilbert, M., Birck, C., Iobbi-Nivol, C., Mejean, V., and Samama, J. 2002. Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA. Protein Sci. 11: 2148-2157.
    • (2002) Protein Sci. , vol.11 , pp. 2148-2157
    • Tranier, S.1    Mortier-Barriere, I.2    Ilbert, M.3    Birck, C.4    Iobbi-Nivol, C.5    Mejean, V.6    Samama, J.7
  • 95
    • 0037317075 scopus 로고    scopus 로고
    • A novel protein fold and extreme domain swapping in the dimeric TorD chaperon from Shewanella massilia
    • London
    • Tranier, S., Iobbi-Nivol, C., Birck, C., Ilbert, M., Mortier-Barriere, I., Méjean, V., and Samama, J.-P. 2003. A novel protein fold and extreme domain swapping in the dimeric TorD chaperon from Shewanella massilia. Structure (London), 11: 165-174.
    • (2003) Structure , vol.11 , pp. 165-174
    • Tranier, S.1    Iobbi-Nivol, C.2    Birck, C.3    Ilbert, M.4    Mortier-Barriere, I.5    Méjean, V.6    Samama, J.-P.7
  • 96
    • 0036601150 scopus 로고    scopus 로고
    • Computational methods for the prediction of protein interactions
    • Valencia, A., and Pazos, F. 2002. Computational methods for the prediction of protein interactions. Curr. Opin. Struct. Biol. 12: 368-373.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 368-373
    • Valencia, A.1    Pazos, F.2
  • 97
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P.M., Billoud, B., and Meyer, J. 2001. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25: 455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 98
    • 0032835980 scopus 로고    scopus 로고
    • The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite
    • Wang, H., Tseng, C.P., and Gunsalus, R.P. 1999. The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite. J. Bacteriol. 181: 5303-5308.
    • (1999) J. Bacteriol. , vol.181 , pp. 5303-5308
    • Wang, H.1    Tseng, C.P.2    Gunsalus, R.P.3
  • 99
    • 0027460079 scopus 로고
    • The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli
    • Weiner, J.H., Shaw, G., Turner, R.J., and Trieber, C.A. 1993. The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 268: 3238-3244.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3238-3244
    • Weiner, J.H.1    Shaw, G.2    Turner, R.J.3    Trieber, C.A.4
  • 100
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of proteins in the folded state
    • Weiner, J.H., Bilous, P.T., Shaw, G.M., Lubitz, S.P., Frost, L., Thomas, G.H., Cole, J.A., and Turner, R.J. 1998. A novel and ubiquitous system for membrane targeting and secretion of proteins in the folded state. Cell, 93: 93-101.
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6    Cole, J.A.7    Turner, R.J.8
  • 101
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analysis of the twin-arginine targeting (Tat) protein export system
    • Yen, M.-R., Tseng, Y.-H., Nguyen, E.H., Wu, L.-F., and Saier, M.H. 2002. Sequence and phylogenetic analysis of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177: 441-450.
    • (2002) Arch. Microbiol. , vol.177 , pp. 441-450
    • Yen, M.-R.1    Tseng, Y.-H.2    Nguyen, E.H.3    Wu, L.-F.4    Saier, M.H.5


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