메뉴 건너뛰기




Volumn 49, Issue 45, 2010, Pages 9911-9921

Adaptation to a high-tungsten environment: Pyrobaculum aerophilum contains an active tungsten nitrate reductase

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEON; BELONG TO; BIDENTATE LIGANDS; COFACTORS; DINUCLEOTIDES; ELECTRON DONORS; HYPERTHERMOPHILES; HYPERTHERMOPHILIC; MEMBRANE ANCHORS; MIDPOINT POTENTIALS; MOLYBDOENZYMES; MOLYBDOPTERIN; MONODENTATES; NITRATE REDUCTASE; PROTON-MOTIVE FORCES; PYROBACULUM AEROPHILUM; REDOX TITRATIONS; TURNOVER NUMBER;

EID: 78149435831     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100974v     Document Type: Article
Times cited : (28)

References (64)
  • 1
    • 0031018503 scopus 로고    scopus 로고
    • Enzyme diversity and mosaic gene organization in denitrification
    • Zumft, W. G. and Körner, H. (1997) Enzyme diversity and mosaic gene organization in denitrification Antonie van Leeuwenhoek 71, 43-58
    • (1997) Antonie Van Leeuwenhoek , vol.71 , pp. 43-58
    • Zumft, W.G.1    Körner, H.2
  • 2
    • 0036550077 scopus 로고    scopus 로고
    • Nitric oxide in biological denitrification: Fe/Cu metalloenzyme and metal complex NOx redox chemistry
    • Wasser, I. M., de Vries, S., Moenne-Loccoz, P., Schröder, I., and Karlin, K. D. (2002) Nitric oxide in biological denitrification: Fe/Cu metalloenzyme and metal complex NOx redox chemistry Chem. Rev. 102, 1201-1234
    • (2002) Chem. Rev. , vol.102 , pp. 1201-1234
    • Wasser, I.M.1    De Vries, S.2    Moenne-Loccoz, P.3    Schröder, I.4    Karlin, K.D.5
  • 6
    • 0031927321 scopus 로고    scopus 로고
    • Effect of tungstate on nitrate reduction by the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Afshar, S., Kim, C., Monbouquette, H. G., and Schröder, I. (1998) Effect of tungstate on nitrate reduction by the hyperthermophilic archaeon Pyrobaculum aerophilum Appl. Environ. Microbiol. 64, 3004-3008
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3004-3008
    • Afshar, S.1    Kim, C.2    Monbouquette, H.G.3    Schröder, I.4
  • 7
    • 0036670794 scopus 로고    scopus 로고
    • Comparison between the nitric oxide reductase family and its aerobic relatives, the cytochrome oxidases
    • de Vries, S. and Schröder, I. (2002) Comparison between the nitric oxide reductase family and its aerobic relatives, the cytochrome oxidases Biochem. Soc. Trans. 30, 662-667
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 662-667
    • De Vries, S.1    Schröder, I.2
  • 8
    • 0035957058 scopus 로고    scopus 로고
    • A novel copper A containing menaquinol NO reductase from Bacillus azotoformans
    • Suharti, Strampraad, M. J. F., Schröder, I., and de Vries, S. (2001) A novel copper A containing menaquinol NO reductase from Bacillus azotoformans Biochemistry 40, 2632-2639
    • (2001) Biochemistry , vol.40 , pp. 2632-2639
    • Suharti1    Strampraad, M.J.F.2    Schröder, I.3    De Vries, S.4
  • 9
    • 0037184270 scopus 로고    scopus 로고
    • Denitrifying genes in bacterial and archaeal genomes
    • Philippot, L. (2002) Denitrifying genes in bacterial and archaeal genomes Biochim. Biophys. Acta 1577, 355-376
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 355-376
    • Philippot, L.1
  • 10
  • 11
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. (1997) Cell biology and molecular basis of denitrification Microbiol. Mol. Biol. Rev. 61, 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 13
    • 1642370336 scopus 로고    scopus 로고
    • Architecture of NarGH reveals a structural classification of Mo-bis-MGD enzymes
    • Jormakka, M., Richardson, D., Byrne, B., and Iwata, S. (2004) Architecture of NarGH reveals a structural classification of Mo-bis-MGD enzymes Structure 12, 95-104
    • (2004) Structure , vol.12 , pp. 95-104
    • Jormakka, M.1    Richardson, D.2    Byrne, B.3    Iwata, S.4
  • 14
    • 0034830306 scopus 로고    scopus 로고
    • Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Afshar, S., Johnson, E., de Vries, S., and Schröder, I. (2001) Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum J. Bacteriol. 183, 5491-5495
    • (2001) J. Bacteriol. , vol.183 , pp. 5491-5495
    • Afshar, S.1    Johnson, E.2    De Vries, S.3    Schröder, I.4
  • 15
    • 32544443991 scopus 로고    scopus 로고
    • Respiratory nitrate and nitrite pathway in the denitrifier haloarchaeon Haloferax mediterranei
    • Martinez-Espinosa, R. M., Richardson, D. J., Butt, J. N., and Bonete, M. J. (2006) Respiratory nitrate and nitrite pathway in the denitrifier haloarchaeon Haloferax mediterranei Biochem. Soc. Trans. 34, 115-117
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 115-117
    • Martinez-Espinosa, R.M.1    Richardson, D.J.2    Butt, J.N.3    Bonete, M.J.4
  • 16
    • 0037051993 scopus 로고    scopus 로고
    • Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui
    • Yoshimatsu, K., Iwasaki, T., and Fujiwara, T. (2002) Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui FEBS Lett. 516, 145-150
    • (2002) FEBS Lett. , vol.516 , pp. 145-150
    • Yoshimatsu, K.1    Iwasaki, T.2    Fujiwara, T.3
  • 17
    • 0034708409 scopus 로고    scopus 로고
    • Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui
    • Yoshimatsu, K., Sakurai, T., and Fujiwara, T. (2000) Purification and characterization of dissimilatory nitrate reductase from a denitrifying halophilic archaeon, Haloarcula marismortui FEBS Lett. 470, 216-220
    • (2000) FEBS Lett. , vol.470 , pp. 216-220
    • Yoshimatsu, K.1    Sakurai, T.2    Fujiwara, T.3
  • 19
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. (2000) Bacterial respiration: A flexible process for a changing environment Microbiology 146, 551-571
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 20
    • 33846174685 scopus 로고    scopus 로고
    • 561 is encoded by the narC gene in the dissimilatory nitrate reductase operon
    • 561 is encoded by the narC gene in the dissimilatory nitrate reductase operon Extremophiles 11, 41-47
    • (2007) Extremophiles , vol.11 , pp. 41-47
    • Yoshimatsu, K.1    Araya, O.2    Fujiwara, T.3
  • 23
    • 8644286154 scopus 로고    scopus 로고
    • Mo and W bis-MGD enzymes: Nitrate reductases and formate dehydrogenases
    • Moura, J. J., Brondino, C. D., Trincao, J., and Romao, M. J. (2004) Mo and W bis-MGD enzymes: Nitrate reductases and formate dehydrogenases J. Biol. Inorg. Chem. 9, 791-799
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 791-799
    • Moura, J.J.1    Brondino, C.D.2    Trincao, J.3    Romao, M.J.4
  • 25
    • 0030061270 scopus 로고    scopus 로고
    • Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum
    • Hilton, J. C. and Rajagopalan, K. V. (1996) Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum Arch. Biochem. Biophys. 325, 139-143
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 139-143
    • Hilton, J.C.1    Rajagopalan, K.V.2
  • 26
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 27
    • 0027933876 scopus 로고
    • Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O
    • Lübben, M. and Morand, K. (1994) Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O J. Biol. Chem. 269, 21473-21479
    • (1994) J. Biol. Chem. , vol.269 , pp. 21473-21479
    • Lübben, M.1    Morand, K.2
  • 29
    • 0028174266 scopus 로고
    • The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre
    • von Wachenfeldt, C., de Vries, S., and van der Oost, J. (1994) The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre FEBS Lett. 340, 109-113
    • (1994) FEBS Lett. , vol.340 , pp. 109-113
    • Von Wachenfeldt, C.1    De Vries, S.2    Van Der Oost, J.3
  • 30
    • 33748296263 scopus 로고    scopus 로고
    • Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum
    • Kloer, D. P., Hagel, C., Heider, J., and Schulz, G. E. (2006) Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum Structure 14, 1377-1388
    • (2006) Structure , vol.14 , pp. 1377-1388
    • Kloer, D.P.1    Hagel, C.2    Heider, J.3    Schulz, G.E.4
  • 31
    • 0035877588 scopus 로고    scopus 로고
    • Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme
    • Kniemeyer, O. and Heider, J. (2001) Ethylbenzene dehydrogenase, a novel hydrocarbon-oxidizing molybdenum/iron-sulfur/heme enzyme J. Biol. Chem. 276, 21381-21386
    • (2001) J. Biol. Chem. , vol.276 , pp. 21381-21386
    • Kniemeyer, O.1    Heider, J.2
  • 32
    • 0034064383 scopus 로고    scopus 로고
    • Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis
    • Krafft, T., Bowen, A., Theis, F., and Macy, J. M. (2000) Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis DNA Sequence 10, 365-377
    • (2000) DNA Sequence , vol.10 , pp. 365-377
    • Krafft, T.1    Bowen, A.2    Theis, F.3    MacY, J.M.4
  • 33
    • 34547114026 scopus 로고    scopus 로고
    • Biogenesis of a respiratory complex is orchestrated by a single accessory protein
    • Lanciano, P., Vergnes, A., Grimaldi, S., Guigliarelli, B., and Magalon, A. (2007) Biogenesis of a respiratory complex is orchestrated by a single accessory protein J. Biol. Chem. 282, 17468-17474
    • (2007) J. Biol. Chem. , vol.282 , pp. 17468-17474
    • Lanciano, P.1    Vergnes, A.2    Grimaldi, S.3    Guigliarelli, B.4    Magalon, A.5
  • 34
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • Turner, R. J., Papish, A. L., and Sargent, F. (2004) Sequence analysis of bacterial redox enzyme maturation proteins (REMPs) Can. J. Microbiol. 50, 225-238
    • (2004) Can. J. Microbiol. , vol.50 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 35
    • 33644872480 scopus 로고    scopus 로고
    • NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly
    • Vergnes, A., Pommier, J., Toci, R., Blasco, F., Giordano, G., and Magalon, A. (2006) NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly J. Biol. Chem. 281, 2170-2176
    • (2006) J. Biol. Chem. , vol.281 , pp. 2170-2176
    • Vergnes, A.1    Pommier, J.2    Toci, R.3    Blasco, F.4    Giordano, G.5    Magalon, A.6
  • 36
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and tungsten in biology
    • Hille, R. (2002) Molybdenum and tungsten in biology Trends Biochem. Sci. 27, 360
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 360
    • Hille, R.1
  • 37
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • Schwarz, G., Mendel, R. R., and Ribbe, M. W. (2009) Molybdenum cofactors, enzymes and pathways Nature 460, 839-847
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3
  • 38
    • 0019316208 scopus 로고
    • The orientation of the substrate sites of formate dehydrogenase and fumarate reductase in the membrane of Vibrio succinogenes
    • Kroger, A., Dorrer, E., and Winkler, E. (1980) The orientation of the substrate sites of formate dehydrogenase and fumarate reductase in the membrane of Vibrio succinogenes Biochim. Biophys. Acta 589, 118-136
    • (1980) Biochim. Biophys. Acta , vol.589 , pp. 118-136
    • Kroger, A.1    Dorrer, E.2    Winkler, E.3
  • 39
    • 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. (1997) 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, 25652-25658
    • (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
  • 40
  • 42
    • 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
  • 43
    • 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
  • 44
    • 2442546646 scopus 로고    scopus 로고
    • The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state
    • Rothery, R. A., Bertero, M. G., Cammack, R., Palak, M., Blasco, F., Strynadka, N. C., and Weiner, J. H. (2004) The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state Biochemistry 43, 5324-5333
    • (2004) Biochemistry , vol.43 , pp. 5324-5333
    • Rothery, R.A.1    Bertero, M.G.2    Cammack, R.3    Palak, M.4    Blasco, F.5    Strynadka, N.C.6    Weiner, J.H.7
  • 45
    • 0032546574 scopus 로고    scopus 로고
    • Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit
    • Magalon, A., Asso, M., Guigliarelli, B., Rothery, R. A., Bertrand, P., Giordano, G., and Blasco, F. (1998) Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit Biochemistry 37, 7363-7370
    • (1998) Biochemistry , vol.37 , pp. 7363-7370
    • Magalon, A.1    Asso, M.2    Guigliarelli, B.3    Rothery, R.A.4    Bertrand, P.5    Giordano, G.6    Blasco, F.7
  • 46
    • 0026611768 scopus 로고
    • A tungsten-containing active formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
    • Schmitz, R. A., Richter, M., Linder, D., and Thauer, R. K. (1992) A tungsten-containing active formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei Eur. J. Biochem. 207, 559-565
    • (1992) Eur. J. Biochem. , vol.207 , pp. 559-565
    • Schmitz, R.A.1    Richter, M.2    Linder, D.3    Thauer, R.K.4
  • 47
    • 0028265243 scopus 로고
    • Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase
    • Bertram, P. A., Schmitz, R. A., Linder, D., and Thauer, R. K. (1994) Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase Arch. Microbiol. 161, 220-228
    • (1994) Arch. Microbiol. , vol.161 , pp. 220-228
    • Bertram, P.A.1    Schmitz, R.A.2    Linder, D.3    Thauer, R.K.4
  • 48
    • 0031664705 scopus 로고    scopus 로고
    • The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: Induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
    • Hochheimer, A., Hedderich, R., and Thauer, R. K. (1998) The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: Induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme Arch. Microbiol. 170, 389-393
    • (1998) Arch. Microbiol. , vol.170 , pp. 389-393
    • Hochheimer, A.1    Hedderich, R.2    Thauer, R.K.3
  • 49
    • 1542268267 scopus 로고    scopus 로고
    • Incorporation of either molybdenum or tungsten into from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria
    • Brondino, C. D., Passeggi, M. C., Caldeira, J., Almendra, M. J., Feio, M. J., Moura, J. J., and Moura, I. (2004) Incorporation of either molybdenum or tungsten into from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria J. Biol. Inorg. Chem. 9, 145-151
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 145-151
    • Brondino, C.D.1    Passeggi, M.C.2    Caldeira, J.3    Almendra, M.J.4    Feio, M.J.5    Moura, J.J.6    Moura, I.7
  • 50
    • 0032933144 scopus 로고    scopus 로고
    • Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli
    • Buc, J., Santini, C. L., Giordani, R., Czjzek, M., Wu, L. F., and Giordano, G. (1999) Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli Mol. Microbiol. 32, 159-168
    • (1999) Mol. Microbiol. , vol.32 , pp. 159-168
    • Buc, J.1    Santini, C.L.2    Giordani, R.3    Czjzek, M.4    Wu, L.F.5    Giordano, G.6
  • 51
    • 0034625310 scopus 로고    scopus 로고
    • Dimethylsulfoxide reductase: An enzyme capable of catalysis with either molybdenum or tungsten at the active site
    • Stewart, L. J., Bailey, S., Bennett, B., Charnock, J. M., Garner, C. D., and McAlpine, A. S. (2000) Dimethylsulfoxide reductase: An enzyme capable of catalysis with either molybdenum or tungsten at the active site J. Mol. Biol. 299, 593-600
    • (2000) J. Mol. Biol. , vol.299 , pp. 593-600
    • Stewart, L.J.1    Bailey, S.2    Bennett, B.3    Charnock, J.M.4    Garner, C.D.5    McAlpine, A.S.6
  • 52
    • 0018734798 scopus 로고
    • Characterization of molybdenum cofactor from Escherichia coli
    • Amy, N. K. and Rajagopalan, K. V. (1979) Characterization of molybdenum cofactor from Escherichia coli J. Bacteriol. 140, 114-124
    • (1979) J. Bacteriol. , vol.140 , pp. 114-124
    • Amy, N.K.1    Rajagopalan, K.V.2
  • 54
    • 0346366817 scopus 로고    scopus 로고
    • Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus
    • Hagedoorn, P. L., Hagen, W. R., Stewart, L. J., Docrat, A., Bailey, S., and Garner, C. D. (2003) Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus FEBS Lett. 555, 606-610
    • (2003) FEBS Lett. , vol.555 , pp. 606-610
    • Hagedoorn, P.L.1    Hagen, W.R.2    Stewart, L.J.3    Docrat, A.4    Bailey, S.5    Garner, C.D.6
  • 55
    • 4744362799 scopus 로고    scopus 로고
    • Involvement of the molybdenum cofactor biosynthetic machinery in the maturation of the Escherichia coli nitrate reductase A
    • Vergnes, A., Gouffi-Belhabich, K., Blasco, F., Giordano, G., and Magalon, A. (2004) Involvement of the molybdenum cofactor biosynthetic machinery in the maturation of the Escherichia coli nitrate reductase A J. Biol. Chem. 279, 41398-41403
    • (2004) J. Biol. Chem. , vol.279 , pp. 41398-41403
    • Vergnes, A.1    Gouffi-Belhabich, K.2    Blasco, F.3    Giordano, G.4    Magalon, A.5
  • 56
    • 0141704413 scopus 로고    scopus 로고
    • Purification and characterization of the MQH2: NO oxidoreductase (qNOR) from the hyperthermophilic Archaeon Pyrobaculum aerophilum
    • de Vries, S., Strampraad, M. J., Lu, S., Moenne-Loccoz, P., and Schröder, I. (2003) Purification and characterization of the MQH2: NO oxidoreductase (qNOR) from the hyperthermophilic Archaeon Pyrobaculum aerophilum J. Biol. Chem. 278, 35861-35868
    • (2003) J. Biol. Chem. , vol.278 , pp. 35861-35868
    • De Vries, S.1    Strampraad, M.J.2    Lu, S.3    Moenne-Loccoz, P.4    Schröder, I.5
  • 57
    • 36348986643 scopus 로고    scopus 로고
    • Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy
    • Dridge, E. J., Watts, C. A., Jepson, B. J., Line, K., Santini, J. M., Richardson, D. J., and Butler, C. S. (2007) Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy Biochem. J. 408, 19-28
    • (2007) Biochem. J. , vol.408 , pp. 19-28
    • Dridge, E.J.1    Watts, C.A.2    Jepson, B.J.3    Line, K.4    Santini, J.M.5    Richardson, D.J.6    Butler, C.S.7
  • 59
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • Palmer, T., Sargent, F., and Berks, B. C. (2005) Export of complex cofactor-containing proteins by the bacterial Tat pathway Trends Microbiol. 13, 175-180
    • (2005) Trends Microbiol. , vol.13 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 60
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • Sargent, F. (2007) The twin-arginine transport system: Moving folded proteins across membranes Biochem. Soc. Trans. 35, 835-847
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 835-847
    • Sargent, F.1
  • 63
    • 0033613194 scopus 로고    scopus 로고
    • The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to narI
    • Rothery, R. A., Blasco, F., Magalon, A., Asso, M., and Weiner, J. H. (1999) The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to narI Biochemistry 38, 12747-12757
    • (1999) Biochemistry , vol.38 , pp. 12747-12757
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Asso, M.4    Weiner, J.H.5
  • 64
    • 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. (1997) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.