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Volumn 32, Issue 1, 1999, Pages 159-168

Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; MOLYBDENUM; OXIDOREDUCTASE; SODIUM CHLORIDE; SULFOXIDE; TRIMETHYLAMINE OXIDE; TUNGSTEN;

EID: 0032933144     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01340.x     Document Type: Article
Times cited : (87)

References (29)
  • 1
    • 0021778428 scopus 로고
    • Bacterial reduction of trimethylamine oxide
    • Barrett, E.L., and Kwan, H.S. (1985) Bacterial reduction of trimethylamine oxide. Annu Rev Microbiol 39: 131-149.
    • (1985) Annu Rev Microbiol , vol.39 , pp. 131-149
    • Barrett, E.L.1    Kwan, H.S.2
  • 2
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulfoxide 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 dimethylsulfoxide 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
  • 3
    • 0029612256 scopus 로고
    • Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta sub-units
    • Buc, J., Santini, C.L., Blasco, F., Giordani, R., Cardenas, M.L., Chippaux, M., et al. (1995) Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta sub-units. Eur J Biochem 234: 766-772.
    • (1995) Eur J Biochem , vol.234 , pp. 766-772
    • Buc, J.1    Santini, C.L.2    Blasco, F.3    Giordani, R.4    Cardenas, M.L.5    Chippaux, M.6
  • 5
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W., and Rees, D.C. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267: 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 6
    • 0014163158 scopus 로고
    • The statistical analysis of enzyme kinetic data
    • Cleland, W.W. (1967) The statistical analysis of enzyme kinetic data. Adv Enzymol 29: 1-32.
    • (1967) Adv Enzymol , vol.29 , pp. 1-32
    • Cleland, W.W.1
  • 7
    • 0032573427 scopus 로고    scopus 로고
    • Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 angstrom resolution
    • Czjzek, M., Dos Santos, J.-P., Pommier, J., Giordano, G., Méjean, V., and Haser, R. (1998) Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 angstrom resolution. J Mol Biol 284: 435-447.
    • (1998) J Mol Biol , vol.284 , pp. 435-447
    • Czjzek, M.1    Dos Santos, J.-P.2    Pommier, J.3    Giordano, G.4    Méjean, V.5    Haser, R.6
  • 8
    • 0032573575 scopus 로고    scopus 로고
    • Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species
    • Dos Santos, J.P., lobbi-Nivol, C., Couillault, C., Giordano, G., and Méjean, V. (1998) Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species. J Mol Biol 284: 421-433.
    • (1998) J Mol Biol , vol.284 , pp. 421-433
    • Dos Santos, J.P.1    Lobbi-Nivol, C.2    Couillault, C.3    Giordano, G.4    Méjean, V.5
  • 9
    • 0030014740 scopus 로고    scopus 로고
    • High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli
    • lobbi-Nivol, C., Pommier, J., Simala-Grant, J., Méjean, V., and Giordano, G. (1996) High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli. Biochim Biophys Acta 1294: 77-82.
    • (1996) Biochim Biophys Acta , vol.1294 , pp. 77-82
    • Lobbi-Nivol, C.1    Pommier, J.2    Simala-Grant, J.3    Méjean, V.4    Giordano, G.5
  • 11
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0031444936 scopus 로고    scopus 로고
    • Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: Crystal structure of the oxidised enzyme at 1.82 angstrom and the dithionite reduced enzyme at 2.8 angstrom resolution
    • McAlpine, A.S., McEwan, A.G., Shaw, A.L., and Bailey, S. (1997) Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82 angstrom and the dithionite reduced enzyme at 2.8 angstrom resolution. J Biol Inorg Chem 2: 690-701.
    • (1997) J Biol Inorg Chem 2 , pp. 690-701
    • McAlpine, A.S.1    McEwan, A.G.2    Shaw, A.L.3    Bailey, S.4
  • 15
    • 0032579202 scopus 로고    scopus 로고
    • The high resolution crystal structure of DMSO reductase in complex with DMSO
    • McAlpine, A.S., McEwan, A.G., and Bailey, S. (1998) The high resolution crystal structure of DMSO reductase in complex with DMSO. J Mol Biol 275: 613-623.
    • (1998) J Mol Biol , vol.275 , pp. 613-623
    • McAlpine, A.S.1    McEwan, A.G.2    Bailey, S.3
  • 18
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H, (1972). Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 19
    • 0030064820 scopus 로고    scopus 로고
    • Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund, S., and Adams, M.W.W. (1996) Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 178: 163-167.
    • (1996) J Bacteriol , vol.178 , pp. 163-167
    • Mukund, S.1    Adams, M.W.W.2
  • 20
    • 0029117622 scopus 로고
    • Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli
    • Rosentel, J.K., Healy, F., Maupin-Furlow, J.A., Lee, J.H., and Shanmugam, K.T. (1995) Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli. J Bacteriol 177: 4857-4864.
    • (1995) J Bacteriol , vol.177 , pp. 4857-4864
    • Rosentel, J.K.1    Healy, F.2    Maupin-Furlow, J.A.3    Lee, J.H.4    Shanmugam, K.T.5
  • 21
    • 0028936979 scopus 로고
    • Association of molybdopterin gua-nine 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 gua-nine 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
  • 22
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C.L., Ize, B., Chanal, A., Müller, 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    Müller, M.4    Giordano, G.5    Wu, L.-F.6
  • 23
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K.V., and Rees, D.C. (1996) Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science 272: 1615-1621.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 24
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution
    • Schneider, F., Lowe, J., Huber, R., Schindelin, H., Kisker, C., and Knablein, J. (1996) Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution. J Mol Biol 263: 53-69.
    • (1996) J Mol Biol , vol.263 , pp. 53-69
    • Schneider, F.1    Lowe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knablein, J.6
  • 25
    • 0024554106 scopus 로고
    • Molybdenum accumulation in chlD mutant of Escherichia coli
    • Scott, D., and Amy, N.K. (1989) Molybdenum accumulation in chlD mutant of Escherichia coli. J Bacteriol 171: 1284-1287.
    • (1989) J Bacteriol , vol.171 , pp. 1284-1287
    • Scott, D.1    Amy, N.K.2
  • 26
    • 0024388691 scopus 로고
    • The inducible trimethylamine N-oxide reductase of Escherichia coli K-12: Its localization and inducers
    • Silvestro, A., Pommier, J., Pascal, M.C., and Giordano, G. (1989) The inducible trimethylamine N-oxide reductase of Escherichia coli K-12: its localization and inducers. Biochim Biophys Acta 994: 208-216.
    • (1989) Biochim Biophys Acta , vol.994 , pp. 208-216
    • Silvestro, A.1    Pommier, J.2    Pascal, M.C.3    Giordano, G.4
  • 27
    • 0029854878 scopus 로고    scopus 로고
    • Kinetic analysis and substrate specificity of Escherichia coli dimethylsulfoxide reductase
    • Simala-Grant, J.L., and Weiner, J.H. (1996) Kinetic analysis and substrate specificity of Escherichia coli dimethylsulfoxide reductase. Microbiology 142: 3231-3239.
    • (1996) Microbiology , vol.142 , pp. 3231-3239
    • Simala-Grant, J.L.1    Weiner, J.H.2
  • 28
    • 0020429524 scopus 로고
    • Nitrate reductase in Escherichia coli K-12; involvement of chlC, chlE, and chlG loci
    • Stewart, V., and MacGregor, C.H. (1982) Nitrate reductase in Escherichia coli K-12; involvement of chlC, chlE, and chlG loci. J Bacteriol 151: 788-799.
    • (1982) J Bacteriol , vol.151 , pp. 788-799
    • Stewart, V.1    MacGregor, C.H.2
  • 29
    • 0031017621 scopus 로고    scopus 로고
    • A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
    • Vorholt, J.A., Vaupel, M., and Thauer, R.K. (1997) A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri. Mol Microbiol 23: 1033-1042.
    • (1997) Mol Microbiol , vol.23 , pp. 1033-1042
    • Vorholt, J.A.1    Vaupel, M.2    Thauer, R.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.