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Volumn 358, Issue 2, 2006, Pages 289-294

Development of a viologen-based microtiter plate assay for the analysis of oxyanion reductase activity: Application to the membrane-bound selenate reductase from Enterobacter cloacae SLD1a-1

Author keywords

Enterobacter cloacae; Methyl viologen; Microtiter plate; Oxyanion reductase activity; Selenate

Indexed keywords

MEMBRANES; POSITIVE IONS;

EID: 33749991611     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.08.028     Document Type: Article
Times cited : (6)

References (16)
  • 1
    • 0017616853 scopus 로고
    • Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli
    • Jones R.W., and Garland P.B. Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Biochem. J. 164 (1977) 199-211
    • (1977) Biochem. J. , vol.164 , pp. 199-211
    • Jones, R.W.1    Garland, P.B.2
  • 2
    • 0022541702 scopus 로고
    • The respiratory nitrate reductase from Paracoccus denitrificans Molecular characterisation and kinetic properties
    • Crask A., and 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
    • Crask, A.1    Ferguson, S.J.2
  • 5
    • 0026526443 scopus 로고
    • The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes
    • Rech S.A., and Macy J.M. The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes. J. Bacteriol. 174 (1992) 7316-7320
    • (1992) J. Bacteriol. , vol.174 , pp. 7316-7320
    • Rech, S.A.1    Macy, J.M.2
  • 6
    • 0242696464 scopus 로고    scopus 로고
    • Purification and characterisation of the selenate reductase from Thauera selenatis
    • Schroder I., Rech S., Krafft T., and Macy J.M. Purification and characterisation of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272 (1997) 23765-23768
    • (1997) J. Biol. Chem. , vol.272 , pp. 23765-23768
    • Schroder, I.1    Rech, S.2    Krafft, T.3    Macy, J.M.4
  • 7
    • 0032729246 scopus 로고    scopus 로고
    • Purification and characterization of (per) chlorate reductase from the chlorate-respiring strain GR-1
    • Kengen S.W., Rikken G.B., Hagen W.R., Van Ginkel C.G., and Stams A.J.M. Purification and characterization of (per) chlorate reductase from the chlorate-respiring strain GR-1. J. Bacteriol. 181 (1999) 6706-6711
    • (1999) J. Bacteriol. , vol.181 , pp. 6706-6711
    • Kengen, S.W.1    Rikken, G.B.2    Hagen, W.R.3    Van Ginkel, C.G.4    Stams, A.J.M.5
  • 8
    • 0035514940 scopus 로고    scopus 로고
    • Characterisation of the reduction of selenate and tellurite by nitrate reductases
    • Sabaty M., Avazeri C., Pignol D., and Vermeglio A. Characterisation of the reduction of selenate and tellurite by nitrate reductases. Appl. Environ. Microbiol. 67 (2001) 5122-5126
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5122-5126
    • Sabaty, M.1    Avazeri, C.2    Pignol, D.3    Vermeglio, A.4
  • 9
    • 33747372448 scopus 로고    scopus 로고
    • Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 responsible for the selective reduction of nitrate and selenate
    • Ridley H., Watts C.A., Richardson D.J., and Butler C.S. Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 responsible for the selective reduction of nitrate and selenate. Appl. Environ. Microbiol. 72 (2006) 5173-5180
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5173-5180
    • Ridley, H.1    Watts, C.A.2    Richardson, D.J.3    Butler, C.S.4
  • 10
    • 0002245717 scopus 로고
    • Kesterson Reservoir- past, present and future: an ecological risk assessment
    • Frankenberger J.R., and Benson S. (Eds), Marcel Dekker, New York
    • Ohlendorf H.M., and Santolo G.M. Kesterson Reservoir- past, present and future: an ecological risk assessment. In: Frankenberger J.R., and Benson S. (Eds). Selenium in the Environment (1994), Marcel Dekker, New York 69-117
    • (1994) Selenium in the Environment , pp. 69-117
    • Ohlendorf, H.M.1    Santolo, G.M.2
  • 11
    • 0023457307 scopus 로고
    • Biogeochemical cycling of selenium in the San Joaquin Valley, California, USA
    • Presser T.S., and Ohlendorf H.M. Biogeochemical cycling of selenium in the San Joaquin Valley, California, USA. Environ. Manage. 11 (1987) 805-821
    • (1987) Environ. Manage. , vol.11 , pp. 805-821
    • Presser, T.S.1    Ohlendorf, H.M.2
  • 12
    • 0344585331 scopus 로고    scopus 로고
    • Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase
    • Watts C.A., Ridley H., Condie K.L., Leaver J.T., Richardson D.J., and Butler C.S. Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase. FEMS Microbiol. Lett. 228 (2003) 273-279
    • (2003) FEMS Microbiol. Lett. , vol.228 , pp. 273-279
    • Watts, C.A.1    Ridley, H.2    Condie, K.L.3    Leaver, J.T.4    Richardson, D.J.5    Butler, C.S.6
  • 13
    • 0030876819 scopus 로고    scopus 로고
    • Reduction of selenium oxyanions by Enterobacter cloacae SLD1a-1: Isolation and growth of the bacterium and its expulsion of selenium particles
    • Losi M.E., and Frankenberger W.T. Reduction of selenium oxyanions by Enterobacter cloacae SLD1a-1: Isolation and growth of the bacterium and its expulsion of selenium particles. Appl. Environ. Microbiol. 63 (1997) 3079-3084
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3079-3084
    • Losi, M.E.1    Frankenberger, W.T.2
  • 15
    • 1642370336 scopus 로고    scopus 로고
    • Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes
    • Jormakka M., Richardson D., Byrne B., and Iwata S. Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes. Structure 12 (2004) 95-104
    • (2004) Structure , vol.12 , pp. 95-104
    • Jormakka, M.1    Richardson, D.2    Byrne, B.3    Iwata, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.