메뉴 건너뛰기




Volumn 220, Issue 2, 2003, Pages 261-269

Properties of the periplasmic nitrate reductases from Paracoccus pantotrophus and Escherichia coli after growth in tungsten-supplemented media

Author keywords

Enzyme activity; Molybdenum; Nitrate reductase; Tungsten

Indexed keywords

MOLYBDENUM; MOLYBDIC ACID; NITRATE REDUCTASE; TUNGSTEN;

EID: 0037470970     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00122-8     Document Type: Article
Times cited : (46)

References (39)
  • 2
    • 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.B., Richardson D.J. Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta. 1232:1995;97-173.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 3
    • 0031056696 scopus 로고    scopus 로고
    • Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient on nitrate respiration
    • Sears H.J., Little P.J., Richardson D.J., Spiro S., Berks B.C., Ferguson S.J. Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient on nitrate respiration. Arch. Microbiol. 167:1997;61-66.
    • (1997) Arch. Microbiol. , vol.167 , pp. 61-66
    • Sears, H.J.1    Little, P.J.2    Richardson, D.J.3    Spiro, S.4    Berks, B.C.5    Ferguson, S.J.6
  • 6
    • 0035968094 scopus 로고    scopus 로고
    • Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus pantotrophus
    • Butler C.S., Ferguson S.J., Berks B.C., Thomson A.J., Cheesman M.R., Richardson D.J. Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus pantotrophus. FEBS Lett. 500:2001;71-74.
    • (2001) FEBS Lett. , vol.500 , pp. 71-74
    • Butler, C.S.1    Ferguson, S.J.2    Berks, B.C.3    Thomson, A.J.4    Cheesman, M.R.5    Richardson, D.J.6
  • 7
    • 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., Richardson D.J. Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport. J. Biol. Chem. 273:1998;28785-28790.
    • (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
  • 10
    • 0023665376 scopus 로고
    • Nitrogen fixation by Azotobacter vinelandii in tungsten-containing medium
    • Hales B.J., Case E.E. Nitrogen fixation by Azotobacter vinelandii in tungsten-containing medium. J. Biol. Chem. 262:1987;16205-16211.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16205-16211
    • Hales, B.J.1    Case, E.E.2
  • 11
    • 0000549163 scopus 로고
    • Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene
    • Deng M.D., Moureaux T., Caboche M. Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene. Plant Physiol. 91:1989;304-309.
    • (1989) Plant Physiol. , vol.91 , pp. 304-309
    • Deng, M.D.1    Moureaux, T.2    Caboche, M.3
  • 12
    • 0016212424 scopus 로고
    • Molecular basis of the biological function of molybdenum. Molybdenum-free sulfite oxidase from livers of tungsten-treated rats
    • Johnson J.L., Cohen H.J., Rajagopalan K.V. Molecular basis of the biological function of molybdenum. Molybdenum-free sulfite oxidase from livers of tungsten-treated rats. J. Biol. Chem. 249:1974;5046-5055.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5046-5055
    • Johnson, J.L.1    Cohen, H.J.2    Rajagopalan, K.V.3
  • 13
    • 0024059922 scopus 로고
    • Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum
    • May H.D., Patel P.S., Ferry J.G. Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum. J. Bacteriol. 170:1988;3384-3389.
    • (1988) J. Bacteriol. , vol.170 , pp. 3384-3389
    • May, H.D.1    Patel, P.S.2    Ferry, J.G.3
  • 14
    • 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., McAlpine A.S. Dimethylsulfoxide reductase: An enzyme capable of catalysis with either molybdenum or tungsten at the active site. J. Mol. Biol. 299:2000;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
  • 15
    • 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., Giordano G. Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli. Mol. Microbiol. 32:1999;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
  • 16
    • 0027787624 scopus 로고
    • Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity
    • Bell L.C., Page M.D., Berks B.C., Richardson D.J., Ferguson S.J. Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity. J. Gen. Microbiol. 139:1993;3205-3214.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 3205-3214
    • Bell, L.C.1    Page, M.D.2    Berks, B.C.3    Richardson, D.J.4    Ferguson, S.J.5
  • 17
    • 0001328962 scopus 로고
    • Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulphur bacterium
    • Robertson L.A., Kuenen J.G. Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulphur bacterium. J. Gen. Miocrobiol. 129:1983;2847-2855.
    • (1983) J. Gen. Miocrobiol. , vol.129 , pp. 2847-2855
    • Robertson, L.A.1    Kuenen, J.G.2
  • 18
    • 0026575047 scopus 로고
    • Involvement of the narJ or narW gene production formation of active nitrate reductase in Escherichia coli
    • Blasco F., Nunzi F., Pommier J., Brasseur R., Chipaux M., Giordano G. Involvement of the narJ or narW gene production formation of active nitrate reductase in Escherichia coli. Mol. Microbiol. 6:1992;209-219.
    • (1992) Mol. Microbiol. , vol.6 , pp. 209-219
    • Blasco, F.1    Nunzi, F.2    Pommier, J.3    Brasseur, R.4    Chipaux, M.5    Giordano, G.6
  • 19
    • 0034175841 scopus 로고    scopus 로고
    • Novel growth characteristics and high rates of nitrate reduction of an Escherichia coli strain, LCB2048, that expresses only a periplasmic nitrate reductase
    • Potter L.C., Millington P.D., Thomas G.H., Rothery R.A., Giordano G., Cole J.A. Novel growth characteristics and high rates of nitrate reduction of an Escherichia coli strain, LCB2048, that expresses only a periplasmic nitrate reductase. FEMS Microbiol. Lett. 185:2000;51-57.
    • (2000) FEMS Microbiol. Lett. , vol.185 , pp. 51-57
    • Potter, L.C.1    Millington, P.D.2    Thomas, G.H.3    Rothery, R.A.4    Giordano, G.5    Cole, J.A.6
  • 20
    • 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., Millington P., Thomas G., Cole J. 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. 344:1999;77-84.
    • (1999) Biochem. J. , vol.344 , pp. 77-84
    • Potter, L.1    Millington, P.2    Thomas, G.3    Cole, J.4
  • 21
    • 0028098074 scopus 로고
    • Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha
    • Berks B.C., Richardson D.J., Robinson C., Reilly A., Aplin R.T., Ferguson S.J. Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha. Eur. J. Biochem. 220:1994;117-124.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 117-124
    • Berks, B.C.1    Richardson, D.J.2    Robinson, C.3    Reilly, A.4    Aplin, R.T.5    Ferguson, S.J.6
  • 22
    • 0000150675 scopus 로고
    • Cleavage of structural head proteins during assembly of the head bacteriophage T4
    • Laemmli U.K. Cleavage of structural head proteins during assembly of the head bacteriophage T4. Nature. 227:1970;280-285.
    • (1970) Nature , vol.227 , pp. 280-285
    • Laemmli, U.K.1
  • 23
    • 0015878020 scopus 로고
    • Immunisation, Isolation of immunoglobulins and estimation of antibody titre
    • Harboe N., Ingild A. Immunisation, Isolation of immunoglobulins and estimation of antibody titre. Scand. J. Immunol. 2:(Suppl. 1):1973;161-164.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.SUPPL. 1 , pp. 161-164
    • Harboe, N.1    Ingild, A.2
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4357.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4357
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 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.C., Fiegen D., Richardson D.J., Cole J.A. Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation. Mol. Microbiol. 44:2002;245-255.
    • (2002) Mol. Microbiol. , vol.44 , pp. 245-255
    • Brondijk, T.H.C.1    Fiegen, D.2    Richardson, D.J.3    Cole, J.A.4
  • 26
    • 0022541702 scopus 로고
    • The respiratory nitrate reductase from Paracoccus denitrificans. Molecular characterisation and kinetic properties
    • Craske A.L., Ferguson S.J. The respiratory nitrate reductase from Paracoccus denitrificans. Molecular characterisation and kinetic properties. Eur. J. Biochem. 158:1986;429-436.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 429-436
    • Craske, A.L.1    Ferguson, S.J.2
  • 27
    • 0014275624 scopus 로고
    • Localisation of synthesis of of nitrate reductase in Escherichia coli
    • Showe M.K., DeMoss J.A. Localisation of synthesis of of nitrate reductase in Escherichia coli. J. Bacteriol. 95:1968;1305-1313.
    • (1968) J. Bacteriol. , vol.95 , pp. 1305-1313
    • Showe, M.K.1    DeMoss, J.A.2
  • 28
    • 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., Cole J.A. Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12. Biochem. J. 344:1999;69-76.
    • (1999) Biochem. J. , vol.344 , pp. 69-76
    • Potter, L.C.1    Cole, J.A.2
  • 29
    • 0030023719 scopus 로고    scopus 로고
    • Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli
    • Rech S., Wolin C., Gunsalus R.P. Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli. J. Biol. Chem. 271:1996;2557-2562.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2557-2562
    • Rech, S.1    Wolin, C.2    Gunsalus, R.P.3
  • 30
    • 0031056696 scopus 로고    scopus 로고
    • Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient on nitrate respiration
    • Sears H.J., Little P.J., Richardson D.J., Spiro S., Berks B.C., Ferguson S.J. Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient on nitrate respiration. Arch. Microbiol. 167:1997;61-66.
    • (1997) Arch. Microbiol. , vol.167 , pp. 61-66
    • Sears, H.J.1    Little, P.J.2    Richardson, D.J.3    Spiro, S.4    Berks, B.C.5    Ferguson, S.J.6
  • 31
    • 0032957729 scopus 로고    scopus 로고
    • The periplasmic nitrate reductase from Escherichia coli: A heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site
    • Thomas G., Potter L., Cole J.A. The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site. FEMS Microbiol. Lett. 174:1999;167-171.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 167-171
    • Thomas, G.1    Potter, L.2    Cole, J.A.3
  • 32
    • 0033588028 scopus 로고    scopus 로고
    • An analysis of the binding repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli
    • Grunden A.M., Self W.T., Villain M., Blalock J.E., Shanmugam K.T. An analysis of the binding repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli. J. Biol. Chem. 274:1999;24308-24315.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24308-24315
    • Grunden, A.M.1    Self, W.T.2    Villain, M.3    Blalock, J.E.4    Shanmugam, K.T.5
  • 33
    • 0032513256 scopus 로고    scopus 로고
    • Molybdate binding by ModA, the periplasmic componente of the Escherichia coli mod molybdate transport system
    • Imperial J., Hadi M., Amy N.K. Molybdate binding by ModA, the periplasmic componente of the Escherichia coli mod molybdate transport system. Biochim. Biophys. Acta. 1370:1998;337-346.
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 337-346
    • Imperial, J.1    Hadi, M.2    Amy, N.K.3
  • 34
    • 0026508528 scopus 로고
    • The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha
    • Richardson D.J., Ferguson S.J. The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha. Arch. Microbiol. 157:1992;535-537.
    • (1992) Arch. Microbiol. , vol.157 , pp. 535-537
    • Richardson, D.J.1    Ferguson, S.J.2
  • 35
    • 0027787624 scopus 로고
    • Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity
    • Bell L.C., Page M.D., Berks B.C., Richardson D.J., Ferguson S.J. Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity. J. Gen. Microbiol. 139:1993;3205-3214.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 3205-3214
    • Bell, L.C.1    Page, M.D.2    Berks, B.C.3    Richardson, D.J.4    Ferguson, S.J.5
  • 38
    • 0015351383 scopus 로고
    • Effects of molybdate, tungstate, and selenium compounds on formate dehydrogenase and other enzymes systems in Escherichia coli
    • Enoch H.G., Lester R.L. Effects of molybdate, tungstate, and selenium compounds on formate dehydrogenase and other enzymes systems in Escherichia coli. J. Bacteriol. 110:1972;1032-1040.
    • (1972) J. Bacteriol. , vol.110 , pp. 1032-1040
    • Enoch, H.G.1    Lester, R.L.2
  • 39
    • 0034830306 scopus 로고    scopus 로고
    • Properties of a thermostable nitrate reductase from the hyperthermophilic Archaeon Pyrobaculum aerophilium
    • Afshar S., Johnson E., De Vries S., Schröder I. Properties of a thermostable nitrate reductase from the hyperthermophilic Archaeon Pyrobaculum aerophilium. J. Bacteriol. 183:2001;5491-5495.
    • (2001) J. Bacteriol. , vol.183 , pp. 5491-5495
    • Afshar, S.1    Johnson, E.2    De Vries, S.3    Schröder, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.