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Volumn 20, Issue 5, 2003, Pages 686-693

Arsenite oxidase, an ancient bioenergetic enzyme

Author keywords

Arsenite; Bioenergetics; Evolution; Molybdopterin protein; Phylogeny; Rieske protein

Indexed keywords

ARSENITE OXIDASE; DIMETHYL SULFOXIDE REDUCTASE; FORMATE DEHYDROGENASE; NITRATE REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0013139343     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/molbev/msg071     Document Type: Article
Times cited : (150)

References (30)
  • 1
    • 0030669387 scopus 로고    scopus 로고
    • Electron transfer towards the RCI-type photosystem in the green sulphur bacterium Chlorobium limicola forma thiosulfatophilum studied by time-resolved optical spectroscopy in-vivo
    • Albouy, D., P. Joliot, B. Robert, and W. Nitschke. 1997. Electron transfer towards the RCI-type photosystem in the green sulphur bacterium Chlorobium limicola forma thiosulfatophilum studied by time-resolved optical spectroscopy in-vivo. Eur. J. Biochem. 249:630-636.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 630-636
    • Albouy, D.1    Joliot, P.2    Robert, B.3    Nitschke, W.4
  • 3
    • 0027104536 scopus 로고
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
    • Anderson, G. L., J. Williams, and R. Hille. 1992. The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase. J. Biol.-Chem. 267:23674-23682.
    • (1992) J. Biol.-Chem. , vol.267 , pp. 23674-23682
    • Anderson, G.L.1    Williams, J.2    Hille, R.3
  • 5
    • 12444340545 scopus 로고    scopus 로고
    • Evolution du complexe bc: Etude de cette enzyme chez la bactérie primitive Chloroflexus aurantiacus
    • Université d'Aix-Marseille I, France
    • Brugna, M. 1997. Evolution du complexe bc: Etude de cette enzyme chez la bactérie primitive Chloroflexus aurantiacus. Diplome d'Etudes Approfondies, Université d'Aix-Marseille I, France.
    • (1997) Diplome d'Etudes Approfondies
    • Brugna, M.1
  • 6
    • 0032457470 scopus 로고    scopus 로고
    • Diversity of cytochrome bc-complexes: Example of the Rieske protein in green sulfur bacteria
    • Brugna, M., D. Albouy, and W. Nitschke. 1998. Diversity of cytochrome bc-complexes: example of the Rieske protein in green sulfur bacteria. J. Bacteriol. 180:3719-3723.
    • (1998) J. Bacteriol. , vol.180 , pp. 3719-3723
    • Brugna, M.1    Albouy, D.2    Nitschke, W.3
  • 7
    • 0033546142 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms
    • Brugna, M., W. Nitschke, M. Asso, B. Guigliarelli, D. Lemesle-Meunier, and C. Schmidt. 1999. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms. J. Biol. Chem. 274:16766-16772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16766-16772
    • Brugna, M.1    Nitschke, W.2    Asso, M.3    Guigliarelli, B.4    Lemesle-Meunier, D.5    Schmidt, C.6
  • 9
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein
    • Carrell, C. J., H. Zhang, W. A. Cramer, and J. L. Smith. 1997. Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5:1613-1625.
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 10
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å
    • Ellis, P. J., T. Conrads, R. Hille, and P. Kuhn. 2001. Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å. Structure 9:125-132.
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 11
    • 0035907063 scopus 로고    scopus 로고
    • A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif
    • Hinsley, A. P., N. R. Stanley, T. Palmer, and B. C. Berks. 2001. A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif. FEBS Lett. 497:45-49.
    • (2001) FEBS Lett. , vol.497 , pp. 45-49
    • Hinsley, A.P.1    Stanley, N.R.2    Palmer, T.3    Berks, B.C.4
  • 13
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka, M., S. Toernroth, B. Byrne, and S. Iwata. 2002. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Toernroth, S.2    Byrne, B.3    Iwata, S.4
  • 14
    • 0030899010 scopus 로고    scopus 로고
    • Cyclic electron transfer in Heliobacillus mobilis involving a menaquinol oxidizing cytochrome bc complex and an RCI-type reaction center
    • Kramer, D. M., B. Schoepp, U. Liebl, and W. Nitschke. 1997. Cyclic electron transfer in Heliobacillus mobilis involving a menaquinol oxidizing cytochrome bc complex and an RCI-type reaction center. Biochemistry 36:4203-4211.
    • (1997) Biochemistry , vol.36 , pp. 4203-4211
    • Kramer, D.M.1    Schoepp, B.2    Liebl, U.3    Nitschke, W.4
  • 15
    • 0037471691 scopus 로고    scopus 로고
    • On the origin of cells: A hypothesis for the evolutionary transitions from prebiotic geochemistry to membrane-bounded chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells
    • Martin, W., and M. J. Russell. 2003. On the origin of cells: a hypothesis for the evolutionary transitions from prebiotic geochemistry to membrane-bounded chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells. Phil. Trans. R. Soc. Lond. B 358:59-85.
    • (2003) Phil. Trans. R. Soc. Lond. B , vol.358 , pp. 59-85
    • Martin, W.1    Russell, M.J.2
  • 17
  • 18
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: Breathing new life into microbiology
    • Olsen, G. J., C. R. Woese, and R. Overbeek. 1994. The winds of (evolutionary) change: breathing new life into microbiology. J. Bacteriol. 176:1-6.
    • (1994) J. Bacteriol. , vol.176 , pp. 1-6
    • Olsen, G.J.1    Woese, C.R.2    Overbeek, R.3
  • 19
    • 0030875872 scopus 로고    scopus 로고
    • The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front
    • Russell, M. J., and A. J. Hall. 1997. The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front. J. Geol. Soc. Lond. 154:377-402.
    • (1997) J. Geol. Soc. Lond. , vol.154 , pp. 377-402
    • Russell, M.J.1    Hall, A.J.2
  • 20
    • 1542339055 scopus 로고    scopus 로고
    • On the dissipation of thermal and chemical energies on the early Earth: The onsets of hydrothermal convection, chemiosmosis, genetically regulated metabolism and oxygenic photosynthesis
    • in press
    • Russell, M. J., A. J. Hall, and A. R. Mellersh. 2003. On the dissipation of thermal and chemical energies on the early Earth: the onsets of hydrothermal convection, chemiosmosis, genetically regulated metabolism and oxygenic photosynthesis. Natural and laboratory simulated thermal chemical processes. (in press).
    • (2003) Natural and Laboratory Simulated Thermal Chemical Processes
    • Russell, M.J.1    Hall, A.J.2    Mellersh, A.R.3
  • 21
    • 0025163688 scopus 로고
    • Orientation of P700, the primary electron donor of photosystem I
    • Rutherford, A. W., and P. Sétif. 1990. Orientation of P700, the primary electron donor of photosystem I. Biochim. Biophys. Acta 1100:128-132.
    • (1990) Biochim. Biophys. Acta , vol.1100 , pp. 128-132
    • Rutherford, A.W.1    Sétif, P.2
  • 22
    • 0035067599 scopus 로고    scopus 로고
    • A comprehensive phylogenetic analysis of Rieske and Rieske-type iron-sulphur proteins
    • Schmidt, C., and L. Shaw. 2001. A comprehensive phylogenetic analysis of Rieske and Rieske-type iron-sulphur proteins. J. Bioenerg. Biomembr. 33:9-26.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 9-26
    • Schmidt, C.1    Shaw, L.2
  • 23
    • 0032587408 scopus 로고    scopus 로고
    • O-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton
    • O-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton. FEBS Lett. 450:245-251.
    • (1999) FEBS Lett. , vol.450 , pp. 245-251
    • Schoepp, B.1    Brugna, M.2    Riedel, A.3    Nitschke, W.4    Kramer, D.M.5
  • 24
    • 0034697992 scopus 로고    scopus 로고
    • Early evolution of cytochrome bc complexes
    • Schütz, M., M. Brugna, E. Lebrun et al. (9 co-authors). 2000. Early evolution of cytochrome bc complexes. J. Mol. Biol. 300:663-675.
    • (2000) J. Mol. Biol. , vol.300 , pp. 663-675
    • Schütz, M.1    Brugna, M.2    Lebrun, E.3
  • 25
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thomson, J. D., T. J. Gilson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acid Res. 24:4876-4882.
    • (1997) Nucleic Acid Res. , vol.24 , pp. 4876-4882
    • Thomson, J.D.1    Gilson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 26
    • 0025765988 scopus 로고
    • Membrane-bound cytochromes in Chloroflexus aurantiacus studied by EPR
    • van Vliet, P. Z. D., W. Nitschke, and A. W. Rutherford. 1991. Membrane-bound cytochromes in Chloroflexus aurantiacus studied by EPR. Eur. J. Biochem. 199:317-323.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 317-323
    • Van Vliet, P.Z.D.1    Nitschke, W.2    Rutherford, A.W.3
  • 27
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25:455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 29
    • 0037070163 scopus 로고    scopus 로고
    • Fractionation of cytochromes of phototrophically grown Chloroflexus aurantiacus. Is there a cytochrome bc complex among them?
    • Yanyushin, M. F. 2002. Fractionation of cytochromes of phototrophically grown Chloroflexus aurantiacus. Is there a cytochrome bc complex among them? FEBS Lett. 512:125-128.
    • (2002) FEBS Lett. , vol.512 , pp. 125-128
    • Yanyushin, M.F.1
  • 30
    • 0001777360 scopus 로고
    • A thermodynamic analysis of the plasma membrane electron transport components in photoheterotrophically grown cells of Chloroflexus aurantiacus: An optical and electron paramagnetic resonance study
    • Zannoni, D., and W. J. Ingledew. 1985. A thermodynamic analysis of the plasma membrane electron transport components in photoheterotrophically grown cells of Chloroflexus aurantiacus: an optical and electron paramagnetic resonance study. FEBS Lett. 193:93-98.
    • (1985) FEBS Lett. , vol.193 , pp. 93-98
    • Zannoni, D.1    Ingledew, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.