메뉴 건너뛰기




Volumn 250, Issue 2, 1997, Pages 332-341

Cytochrome ba3 from natronbacterium pharaonis an. Archaeal four subunit cytochrom-c-type oxidase

Author keywords

Archaea; Cytochrome ba3; Natronobacterium pharaonis; Proton pump; Terminal oxidase

Indexed keywords

CYTOCHROME C OXIDASE; PROTON PUMP; CYTOCHROME B; CYTOCHROME BA3;

EID: 0031282998     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0332a.x     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T. & Wikström, M. (1992) Oxygen activation and the conservation of energy in cell respiration, Nature 356, 301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 2
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L. & Gennis, R. B. (1994) Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation, Annu. Rev. Biochem. 63, 675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 6
    • 0027491552 scopus 로고
    • Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
    • Thomas, J. W., Puustinen, A., Alben, J. O., Gennis, R. B. & Wikström, M. (1993) Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity, Biochemistry 32, 10923-10928.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5
  • 8
    • 0028913025 scopus 로고
    • 0 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp135→Asn
    • 0 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp135→Asn, Biochemistry 34, 4428-4433.
    • (1995) Biochemistry , vol.34 , pp. 4428-4433
    • García-Horsman, J.A.1    Puustinen, A.2    Gennis, R.B.3    Wikström, M.4
  • 9
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 12
    • 0029884379 scopus 로고    scopus 로고
    • Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy
    • Hellwig, P., Rost, B., Kaiser, U., Ostermeier, C., Michel, H. & Mäntele, W. (1996) Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy, FEBS Lett. 385, 53-57.
    • (1996) FEBS Lett. , vol.385 , pp. 53-57
    • Hellwig, P.1    Rost, B.2    Kaiser, U.3    Ostermeier, C.4    Michel, H.5    Mäntele, W.6
  • 13
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana, J., Lübben, M., Saraste, M. & Higgins, D. G. (1994) Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen, EMBO J. 13, 2516-2525.
    • (1994) EMBO J. , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lübben, M.2    Saraste, M.3    Higgins, D.G.4
  • 14
    • 0027469984 scopus 로고
    • Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis
    • Preisig, O., Anthamatten, D. & Hennecke, H. (1993) Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis, Proc. Natl Acad. Sci. USA 90, 3309-3313.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3309-3313
    • Preisig, O.1    Anthamatten, D.2    Hennecke, H.3
  • 15
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • Saraste, M. & Castresana, J. (1994) Cytochrome oxidase evolved by tinkering with denitrification enzymes, FEBS Lett. 341, 1-4.
    • (1994) FEBS Lett. , vol.341 , pp. 1-4
    • Saraste, M.1    Castresana, J.2
  • 16
    • 0028786047 scopus 로고
    • Evolution of energetic metabolism: The respiration-early hypothesis
    • Castresana, J. & Saraste, M. (1995) Evolution of energetic metabolism: The respiration-early hypothesis, Trends Biochem. Sci. 20, 443-448.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 443-448
    • Castresana, J.1    Saraste, M.2
  • 17
    • 0028920572 scopus 로고
    • Cytochromes of archaeal electron transfer chains
    • Lübben, M. (1995) Cytochromes of archaeal electron transfer chains, Biochim. Biophys. Acta Bio-Energetics 1229, 1-22.
    • (1995) Biochim. Biophys. Acta Bio-Energetics , vol.1229 , pp. 1-22
    • Lübben, M.1
  • 18
    • 0040984441 scopus 로고    scopus 로고
    • On the origin of respiration: Electron transport proteins from archaea to man
    • Schäfer, G., Purschke, W. & Schmidt, C. L. (1996) On the origin of respiration: electron transport proteins from archaea to man, FEMS Microbiol. Rev. 18, 173-188.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 173-188
    • Schäfer, G.1    Purschke, W.2    Schmidt, C.L.3
  • 19
    • 0026563750 scopus 로고
    • An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes
    • Lübben, M. Kolmerer, B. & Saraste, M. (1992) An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes, EMBO J. 11, 805-812.
    • (1992) EMBO J. , vol.11 , pp. 805-812
    • Lübben, M.1    Kolmerer, B.2    Saraste, M.3
  • 22
    • 33751385403 scopus 로고
    • Halocyanin, an archaebacterial blue copper protein (type I) from Natronobacterium pharaonis
    • Scharf, B. & Engelhard, M. (1993) Halocyanin, an archaebacterial blue copper protein (type I) from Natronobacterium pharaonis, Biochemistry 32, 12894-12900.
    • (1993) Biochemistry , vol.32 , pp. 12894-12900
    • Scharf, B.1    Engelhard, M.2
  • 26
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. & Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA, Nucleic Acids Res. 7, 1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 27
  • 28
    • 0028170549 scopus 로고
    • A simple method using T4 DNA polymerase to clone polymerase chain reaction products
    • Wang, K., Koop, B. F. & Hood, L. (1994) A simple method using T4 DNA polymerase to clone polymerase chain reaction products, BioTechniques 17, 236-238.
    • (1994) BioTechniques , vol.17 , pp. 236-238
    • Wang, K.1    Koop, B.F.2    Hood, L.3
  • 29
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P. & Vogelstein, B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity, Anal. Biochem. 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 31
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 32
    • 0028965178 scopus 로고
    • The primary structure of sensory rhodopsin II: A member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II
    • Seidel, R., Scharf, B., Gautel, M., Kleine, K., Oesterhelt, D. & Engelhard, M. (1995) The primary structure of sensory rhodopsin II: A member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II, Proc. Natl Acad. Sci. USA 92, 3036-3040.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3036-3040
    • Seidel, R.1    Scharf, B.2    Gautel, M.3    Kleine, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 33
    • 0000099234 scopus 로고
    • Diagnosis of chronic myeloid and acute lymphocytic leukemias by detection of leukemia-specific mRNA sequences amplified in vitro
    • Kawasaki, E. S., Clark, S. S., Coyne, M. Y., Smith, S. D., Champlin, R., Witte, O. N. & McCormick, F. P. (1988) Diagnosis of chronic myeloid and acute lymphocytic leukemias by detection of leukemia-specific mRNA sequences amplified in vitro, Proc. Natl Acad. Sci. USA 85, 5698-5702.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 5698-5702
    • Kawasaki, E.S.1    Clark, S.S.2    Coyne, M.Y.3    Smith, S.D.4    Champlin, R.5    Witte, O.N.6    McCormick, F.P.7
  • 34
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny interference package (version 3.2)
    • Felsenstein, J. (1989) PHYLIP - phylogeny interference package (version 3.2), Cladistics 5, 164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 36
    • 0028286154 scopus 로고
    • Blue halorhodopsin from Natronobacterium pharaonis: Wavelength regulation by anions
    • Scharf, B. & Engelhard, M. (1994) Blue halorhodopsin from Natronobacterium pharaonis: Wavelength regulation by anions, Biochemistry 33, 6387-6393.
    • (1994) Biochemistry , vol.33 , pp. 6387-6393
    • Scharf, B.1    Engelhard, M.2
  • 37
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. & Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra, Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 41
    • 0028339618 scopus 로고
    • The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem
    • Lübben, M., Warne, A., Albracht, S. P. J. & Saraste, M. (1994) The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem, Mol. Microbiol. 13, 327-335.
    • (1994) Mol. Microbiol. , vol.13 , pp. 327-335
    • Lübben, M.1    Warne, A.2    Albracht, S.P.J.3    Saraste, M.4
  • 42
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H. & von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form, Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 43
    • 0003108182 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix
    • Eckerskorn, C. & Lottspeich, F. (1989) Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix, Chromatographia 28, 92-94.
    • (1989) Chromatographia , vol.28 , pp. 92-94
    • Eckerskorn, C.1    Lottspeich, F.2
  • 45
    • 0027960408 scopus 로고
    • Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene operon from the extreme thermophile archaeon Sulfolobus acidocaldarius
    • Ramirez, C., Shimmin, L. C., Leggatt, P. & Matheson A. T. (1994) Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene operon from the extreme thermophile archaeon Sulfolobus acidocaldarius, J. Mol. Biol. 244, 242-249.
    • (1994) J. Mol. Biol. , vol.244 , pp. 242-249
    • Ramirez, C.1    Shimmin, L.C.2    Leggatt, P.3    Matheson, A.T.4
  • 46
    • 0028349908 scopus 로고
    • Compilation of halobacterial protein coding genes, the halobacterial codon usage table and its use
    • Soppa, J. (1994) Compilation of halobacterial protein coding genes, the halobacterial codon usage table and its use, System. Appl. Microbiol. 16, 725-733.
    • (1994) System. Appl. Microbiol. , vol.16 , pp. 725-733
    • Soppa, J.1
  • 47
    • 0028246909 scopus 로고
    • The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation
    • Mattar, S., Scharf, B., Kent, S. B. H., Rodewald, K., Oesterhelt, D. & Engelhard, M. (1994) The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation, J. Biol. Chem. 269, 14939-14945.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14939-14945
    • Mattar, S.1    Scharf, B.2    Kent, S.B.H.3    Rodewald, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 48
    • 0029030987 scopus 로고
    • New archaebacterial genes coding for redox proteins: Implications for the evolution of aerobic metabolism
    • Castresana, J., Lübben, M. & Saraste, M. (1995) New archaebacterial genes coding for redox proteins: Implications for the evolution of aerobic metabolism, J. Mol. Biol. 250, 202-210.
    • (1995) J. Mol. Biol. , vol.250 , pp. 202-210
    • Castresana, J.1    Lübben, M.2    Saraste, M.3
  • 50
    • 0025143777 scopus 로고
    • Halophilic proteins and the influence of solvent on protein stabilization
    • Zaccai, G. & Eisenberg, H. (1990) Halophilic proteins and the influence of solvent on protein stabilization, Trends Biochem. Sci. 15, 333-337.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 333-337
    • Zaccai, G.1    Eisenberg, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.