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Volumn , Issue , 2007, Pages 21-35

The Prokaryotic Nitrate Reductases

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Indexed keywords


EID: 84857544811     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-044452857-5.50003-5     Document Type: Chapter
Times cited : (14)

References (15)
  • 3
    • 1642370336 scopus 로고    scopus 로고
    • The architecture of NarGH reveals a structural classification of MGD enzymes
    • Jormakka M., Richardson D.J., Byrne B., Iwata S. The architecture of NarGH reveals a structural classification of MGD enzymes. Structure 2004, 12:95-104.
    • (2004) Structure , vol.12 , pp. 95-104
    • Jormakka, M.1    Richardson, D.J.2    Byrne, B.3    Iwata, S.4
  • 4
    • 0035949638 scopus 로고    scopus 로고
    • Protein film electrochemistry of the membrane-bound nitrate reductase
    • Anderson L., Richardson D.J., Butt J.N. Protein film electrochemistry of the membrane-bound nitrate reductase. Biochemistry 2001, 40:11294-11307.
    • (2001) Biochemistry , vol.40 , pp. 11294-11307
    • Anderson, L.1    Richardson, D.J.2    Butt, J.N.3
  • 5
    • 0036225747 scopus 로고    scopus 로고
    • Two domains of a dual function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus
    • Wood N., Alizadeh T., Richardson D.J., Ferguson S.J., Moir J.W.B. Two domains of a dual function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus. Mol. Microbiol. 2002, 44:157-170.
    • (2002) Mol. Microbiol. , vol.44 , pp. 157-170
    • Wood, N.1    Alizadeh, T.2    Richardson, D.J.3    Ferguson, S.J.4    Moir, J.W.B.5
  • 6
    • 4444281824 scopus 로고    scopus 로고
    • Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei: biochemcial and genetic analysis
    • Lledo B., Martinez-Espinosa R.M., Marhuenda-Egea F.C., Bonete M.J. Respiratory nitrate reductase from haloarchaeon Haloferax mediterranei: biochemcial and genetic analysis. Biochim. Biophys. Acta 2004, 1674:50-59.
    • (2004) Biochim. Biophys. Acta , vol.1674 , pp. 50-59
    • Lledo, B.1    Martinez-Espinosa, R.M.2    Marhuenda-Egea, F.C.3    Bonete, M.J.4
  • 7
    • 0034015380 scopus 로고    scopus 로고
    • The 1999 Fleming Lecture. Bacterial respiration: a flexible process for a changing environment
    • Richardson D.J. The 1999 Fleming Lecture. Bacterial respiration: a flexible process for a changing environment. Microbiology 2000, 146:551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 10
    • 0032582701 scopus 로고    scopus 로고
    • Spectroscopic characterization of a novel tetra-heme c-type cytochrome widely implicated in bacterial electron transport
    • Roldan M.D., Sears H.J., Ferguson S.J., Cheesman M.R., Thomson A.J., Berks B.C., Richardson D.J. Spectroscopic characterization of a novel tetra-heme c-type cytochrome widely implicated in bacterial electron transport. J. Biol. Chem. 1998, 273:28785-28790.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28785-28790
    • Roldan, M.D.1    Sears, H.J.2    Ferguson, S.J.3    Cheesman, M.R.4    Thomson, A.J.5    Berks, B.C.6    Richardson, D.J.7
  • 11
    • 0036717906 scopus 로고    scopus 로고
    • Hierarchy of carbon source selection in Paracoccus pantotrophus: Strict correlation between reduction state of the carbon substrate and aerobic expression of the nap operon
    • Ellington M.J.K., Bhakoo K.K., Sawers G., Richardson D.J., Ferguson S.J. Hierarchy of carbon source selection in Paracoccus pantotrophus: Strict correlation between reduction state of the carbon substrate and aerobic expression of the nap operon. J. Bact. 2002, 184:4767-4774.
    • (2002) J. Bact. , vol.184 , pp. 4767-4774
    • Ellington, M.J.K.1    Bhakoo, K.K.2    Sawers, G.3    Richardson, D.J.4    Ferguson, S.J.5
  • 12
  • 13
    • 0036229614 scopus 로고    scopus 로고
    • The roles of NapF, NapG and NapH gene products in electron transfer from ubiquinol to the periplasmic nitrate reductase of Escherichia coli
    • Brondijk T.H.C., Fiegen D., Richardson D.J., Cole J.A. The roles of NapF, NapG and NapH gene products in electron transfer from ubiquinol to the periplasmic nitrate reductase of Escherichia coli. Mol. Microb. 2002, 44:245-255.
    • (2002) Mol. Microb. , vol.44 , pp. 245-255
    • Brondijk, T.H.C.1    Fiegen, D.2    Richardson, D.J.3    Cole, J.A.4
  • 14
    • 3543029827 scopus 로고    scopus 로고
    • Tuning a nitrate reductase for function: the first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties
    • Jepson B.N., Anderson L., Rubio L., Taylor C., Butler C., Herrero A., Flores E., Butt J.N., Richardson D.J. Tuning a nitrate reductase for function: the first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties. J. Biol. Chem. 2004, 279:32212-32218.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32212-32218
    • Jepson, B.N.1    Anderson, L.2    Rubio, L.3    Taylor, C.4    Butler, C.5    Herrero, A.6    Flores, E.7    Butt, J.N.8    Richardson, D.J.9
  • 15
    • 22544435739 scopus 로고    scopus 로고
    • Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site
    • Fischer K., Barbeir G.G., Hecht H.J., Mendel R.R., Campbell W.H., Schwarz G. Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site. Plant Cell 2005, 17:1167-1179.
    • (2005) Plant Cell , vol.17 , pp. 1167-1179
    • Fischer, K.1    Barbeir, G.G.2    Hecht, H.J.3    Mendel, R.R.4    Campbell, W.H.5    Schwarz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.