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Volumn 106, Issue 21, 2009, Pages 8549-8554

Menaquinone as pool quinone in a purple bacterium

Author keywords

Electron transport; Evolution; Photosynthesis

Indexed keywords

MENAQUINONE; OXYGEN; PROTEIN SUBUNIT; QUINONE DERIVATIVE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 66649119126     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0813173106     Document Type: Article
Times cited : (104)

References (40)
  • 1
    • 0017339395 scopus 로고
    • Vectorial chemiosmotic processes
    • Mitchell P (1977) Vectorial chemiosmotic processes. Annu Rev Biochem 46:996-1005.
    • (1977) Annu Rev Biochem , vol.46 , pp. 996-1005
    • Mitchell, P.1
  • 2
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications
    • Collins MD, Jones D (1981) Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications. Microbiol Rev 45:316-354. (Pubitemid 11032202)
    • (1981) Microbiological Reviews , vol.45 , Issue.2 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 3
    • 0021604038 scopus 로고
    • Distribution of rhodoquinone in Rhodospirillaceae and its taxonomic implications
    • Hiraishi A, Hoshino Y (1984) Distribution of rhodoquinone in Rhodospirillaceae and its taxonomic implication. J Gen Appl Microbiol 30:435-448. (Pubitemid 15078908)
    • (1984) Journal of General and Applied Microbiology , vol.30 , Issue.6 , pp. 435-448
    • Hiraishi, A.1    Hoshino, Y.2
  • 4
    • 0035085306 scopus 로고    scopus 로고
    • Respiratory enzymes from Sulfolobus acidocaldarius
    • DOI 10.1016/S0076-6879(01)31071-6
    • Schäfer G, Moll R, Schmidt CL (2001) Respiratory enzymes from Sulfolobus acidocaldarius. Methods Enzymol 331:369-410. (Pubitemid 32242361)
    • (2001) Methods in Enzymology , vol.331 , pp. 369-410
    • Schafer, G.1    Moll, R.2    Schmidt, C.L.3
  • 5
    • 0001477938 scopus 로고
    • From naphtho- to benzoquinones-(r)evolutionary reorganizations of electron transfer chains
    • ed Mathis P (Kluwer Academic, Dordrecht, The Netherlands)
    • Nitschke W, Kramer DM, Riedel A, Liebl U (1995) From naphtho- to benzoquinones-(r)evolutionary reorganizations of electron transfer chains. Photosynthesis: From Light to Biosphere, ed Mathis P (Kluwer Academic, Dordrecht, The Netherlands), Vol I, pp 945-950.
    • (1995) Photosynthesis: from Light to Biosphere , vol.1 , pp. 945-950
    • Nitschke, W.1    Kramer, D.M.2    Riedel, A.3    Liebl, U.4
  • 6
    • 0034697992 scopus 로고    scopus 로고
    • Early evolution of cytochrome bc complexes
    • Schütz M, et al. (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
  • 7
    • 0000133750 scopus 로고    scopus 로고
    • Iron-sulfur centers involved in photosynthetic light reactions
    • Schoepp B, Brugna M, Lebrun E, Nitschke W (1999) Iron-sulfur centers involved in photosynthetic light reactions. Adv Inorg Chem 47:335-360.
    • (1999) Adv Inorg Chem , vol.47 , pp. 335-360
    • Schoepp, B.1    Brugna, M.2    Lebrun, E.3    Nitschke, W.4
  • 9
    • 0021682230 scopus 로고
    • Quinones of phototrophic purple bacteria
    • DOI 10.1016/0378-1097(84)90052-1
    • Imhoff JF (1984) Quinones of phototrophic purple bacteria. FEMS Microbiol Lett 25:85-89. (Pubitemid 15217305)
    • (1984) FEMS Microbiology Letters , vol.25 , Issue.1 , pp. 85-89
    • Imhoff, J.F.1
  • 10
    • 0027141836 scopus 로고
    • Total DNA restriction pattern and quinone composition of members of the family Ectothiorhodospiraceae
    • Ventura S, Giovannetti L, Gori A, Viti C, Materassi R (1993) Total DNA restriction pattern and quinone composition of members of the family Ectothiorhodospiraceae. System Appl Microbiol 16:405-410. (Pubitemid 24010292)
    • (1993) Systematic and Applied Microbiology , vol.16 , Issue.3 , pp. 405-410
    • Ventura, S.1    Giovannetti, L.2    Gori, A.3    Viti, C.4    Materassi, R.5
  • 11
    • 0001228592 scopus 로고
    • Reaction center associated cytochromes
    • eds Blankenship RE, Madigan MT, Bauer CE (Kluwer Academic, Dordrecht, The Netherlands)
    • Nitschke W, Dracheva SM (1995) Reaction center associated cytochromes. in Anoxygenic Photosynthetic Bacteria, eds Blankenship RE, Madigan MT, Bauer CE (Kluwer Academic, Dordrecht, The Netherlands), pp 775-805.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 775-805
    • Nitschke, W.1    Dracheva, S.M.2
  • 12
    • 0343750768 scopus 로고
    • The function of ubiquinone and menaquinone in the respiratory chain of Escherichia coli
    • ed. Trumpower, BL (Academic Press, New York, USA)
    • Jones RW, Garland PB (1982) The function of ubiquinone and menaquinone in the respiratory chain of Escherichia coli. Functions of quinones in energy conserving systems ed. Trumpower, BL (Academic Press, New York, USA), pp 465-476.
    • (1982) Functions of Quinones in Energy Conserving Systems , pp. 465-476
    • Jones, R.W.1    Garland, P.B.2
  • 15
    • 0000134772 scopus 로고
    • Cytochromes, iron-sulfur, and copper proteins mediating electron transfer from the cyt bc1 complex to photosynthetic reaction complexes
    • eds Blankenship RE, Madigan MT, Bauer CE (Kluwer Academic, Dordrecht, The Netherlands)
    • Meyer TE, Donohue TJ (1995) Cytochromes, iron-sulfur, and copper proteins mediating electron transfer from the cyt bc1 complex to photosynthetic reaction complexes. Anoxygenic Photosynthetic Bacteria, eds Blankenship RE, Madigan MT, Bauer CE (Kluwer Academic, Dordrecht, The Netherlands), pp 725-745.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 725-745
    • Meyer, T.E.1    Donohue, T.J.2
  • 16
    • 0013593621 scopus 로고
    • The function of menaquinone in bacterial electron transport
    • ed Lenaz G (Wiley, London)
    • Kröger A, Unden G (1985) The function of menaquinone in bacterial electron transport. Coenzyme Q, ed Lenaz G (Wiley, London), pp 285-300.
    • (1985) Coenzyme Q , pp. 285-300
    • Kröger, A.1    Unden, G.2
  • 17
    • 0018787864 scopus 로고
    • Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties
    • Takamiya KI, Dutton PL (1979) Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties. Biochim Biophys Acta 546:1-16.
    • (1979) Biochim Biophys Acta , vol.546 , pp. 1-16
    • Takamiya, K.I.1    Dutton, P.L.2
  • 18
    • 0020633916 scopus 로고
    • Menaquinone is the sole quinone in the facultatively aerobic green photosynthetic bacterium. Chloroflexus aurantiacus
    • Hale MB, Blankenship RE, Fuller RC (1983) Menaquinone is the sole quinone in the facultatively aerobic green photosynthetic bacterium. Chloroflexus aurantiacus. Biochim Biophys Acta 723:376-382.
    • (1983) Biochim Biophys Acta , vol.723 , pp. 376-382
    • Hale, M.B.1    Blankenship, R.E.2    Fuller, R.C.3
  • 19
    • 0000469240 scopus 로고
    • Occurrence of menaquinone as the sole isoprenoid quinone in the photosynthetic bacterium Heliobacterium chlorum
    • Hiraishi A (1989) Occurrence of menaquinone as the sole isoprenoid quinone in the photosynthetic bacterium Heliobacterium chlorum. Arch Microbiol 151:378-379.
    • (1989) Arch Microbiol , vol.151 , pp. 378-379
    • Hiraishi, A.1
  • 20
    • 0000739474 scopus 로고
    • Photoreaction center of Ectothiorhodospira sp. Pigment, heme, quinone, and polypeptide composition
    • Lefebvre S, Picorel R, Cloutier Y, Gingras G (1984) Photoreaction center of Ectothiorhodospira sp. Pigment, heme, quinone, and polypeptide composition. Biochemistry 23:5279-5288.
    • (1984) Biochemistry , vol.23 , pp. 5279-5288
    • Lefebvre, S.1    Picorel, R.2    Cloutier, Y.3    Gingras, G.4
  • 21
    • 0035852875 scopus 로고    scopus 로고
    • B pocket in bacterial chromatophores: Dependence on the state of QA
    • B pocket in bacterial chromatophores: Dependence on the state of QA. Biochemistry 40:1812-1823.
    • (2001) Biochemistry , vol.40 , pp. 1812-1823
    • Ginet, N.1    Lavergne, J.2
  • 22
    • 0021830124 scopus 로고
    • The chromone inhibitor stigmatellin - Binding to the ubiquinol oxidation center at the C-side of the mitochondrial membrane
    • DOI 10.1016/0014-5793(85)80929-7
    • von Jagow G, Ohnishi T (1985) The chromone inhibitor stigmatellin - Binding to the UQ oxidation center at the C-side of the mitochondrial membrane. FEBS Lett 17:311-315. (Pubitemid 15068060)
    • (1985) FEBS Letters , vol.185 , Issue.2 , pp. 311-315
    • Von Jagow, G.1    Ohnishi, T.2
  • 23
    • 0025019450 scopus 로고
    • Evidence for a unique Rieske iron-sulphur centre in Heliobacterium chlorum
    • DOI 10.1016/0014-5793(90)80608-L
    • Liebl U, Rutherford AW, Nitschke W (1990) Evidence for a unique Rieske iron-sulphur centerin Heliobacterium chlorum. FEBS Lett 261(2):427-430. (Pubitemid 20075010)
    • (1990) FEBS Letters , vol.261 , Issue.2 , pp. 427-430
    • Liebl, U.1    Rutherford, A.W.2    Nitschke, W.3
  • 24
    • 58149286444 scopus 로고    scopus 로고
    • 1 and related bc complexes, the Rieske/cytochrome b complex as the functional core of a central electron/proton transfer complex
    • eds Hunter CN, Daldal F, Thurnauer MC, Beatty JT (Springler, Dordrecht, The Nederlands)
    • 1 and related bc complexes, the Rieske/cytochrome b complex as the functional core of a central electron/proton transfer complex in The Purple Phototrophic Bacteria, eds Hunter CN, Daldal F, Thurnauer MC, Beatty JT (Springler, Dordrecht, The Nederlands), pp 451-473.
    • (2009) The Purple Phototrophic Bacteria , pp. 451-473
    • Kramer, D.M.1    Nitschke, W.2    Cooley, J.W.3
  • 26
    • 0016156765 scopus 로고
    • Identification of ubiquinone as the secondary electron acceptor in the photosynthetic apparatus of Chromatium vinosum
    • Halsey YD, Parson WW (1974) Identification of ubiquinone as the secondary electron acceptor in the photosynthetic apparatus of Chromatium vinosum. Biochim Biophys Acta 347:404-416.
    • (1974) Biochim Biophys Acta , vol.347 , pp. 404-416
    • Halsey, Y.D.1    Parson, W.W.2
  • 27
    • 0001763192 scopus 로고
    • eds Clayton RK, Siström WF (Plenum, New York)
    • Parson WW (1978) in The Photosynthetic Bacteria, eds Clayton RK, Siström WF (Plenum, New York), pp 455-469.
    • (1978) The Photosynthetic Bacteria , pp. 455-469
    • Parson, W.W.1
  • 28
    • 0025752940 scopus 로고
    • Characterization of reaction center/antenna complexes from bacterio-chloroplyll a containing Ectothiorhodospiraceae
    • Leguijt T, Hellingwerf KJ (1991) Characterization of reaction center/antenna complexes from bacterio-chloroplyll a containing Ectothiorhodospiraceae. Biochim Biophys Acta 1057:353-360.
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 353-360
    • Leguijt, T.1    Hellingwerf, K.J.2
  • 30
    • 33947183722 scopus 로고    scopus 로고
    • The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species
    • DOI 10.1128/JB.01698-06
    • Murphy JN, Saltikov CW (2007) The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Schewanella species. J Bacteriol 189(6):2283-2290. (Pubitemid 46411342)
    • (2007) Journal of Bacteriology , vol.189 , Issue.6 , pp. 2283-2290
    • Murphy, J.N.1    Saltikov, C.W.2
  • 31
    • 58449135158 scopus 로고    scopus 로고
    • The multiple evolutionary histories of dioxygen reductases: Implications for the origin and evolution of aerobic respiration
    • Brochier-Armanet C, Talla E, Gribaldo S (2009) The multiple evolutionary histories of dioxygen reductases: Implications for the origin and evolution of aerobic respiration. Mol Biol Evol 26(2):285-297.
    • (2009) Mol Biol Evol , vol.26 , Issue.2 , pp. 285-297
    • Brochier-Armanet, C.1    Talla, E.2    Gribaldo, S.3
  • 33
    • 27144537879 scopus 로고    scopus 로고
    • 1 Complex
    • 1 Complex. J Biol Chem 280:34654-34660.
    • (2005) J Biol Chem , vol.280 , pp. 34654-34660
    • Cape, J.L.1
  • 34
    • 30144441164 scopus 로고    scopus 로고
    • Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30
    • Cape JL, Bowman MK, Kramer DM (2006) Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30. Trends Plants Sci 11:46-55.
    • (2006) Trends Plants Sci , vol.11 , pp. 46-55
    • Cape, J.L.1    Bowman, M.K.2    Kramer, D.M.3
  • 37
    • 2642582298 scopus 로고    scopus 로고
    • Apparent redundancy of electron transfer pathways via bc(1) complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans
    • Brasseur G, Levican G, Bonnefoy V, Holmes D, Jedlicki E, Lemesle-Meunier D (2004) Apparent redundancy of electron transfer pathways via bc(1) complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans. Biochim Biophys Acta 1656:114-126.
    • (2004) Biochim Biophys Acta , vol.1656 , pp. 114-126
    • Brasseur, G.1    Levican, G.2    Bonnefoy, V.3    Holmes, D.4    Jedlicki, E.5    Lemesle-Meunier, D.6
  • 38
    • 0015220486 scopus 로고
    • Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 11°K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa
    • Dutton PL (1971) Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 11°K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa. Biochim Biophys Acta 226:63-80.
    • (1971) Biochim Biophys Acta , vol.226 , pp. 63-80
    • Dutton, P.L.1


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