메뉴 건너뛰기




Volumn 239, Issue 3, 1996, Pages 857-864

Sodium ion translocation by N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from methanosarcina mazei Go1 reconstituted in ether lipid liposomes

Author keywords

Ether lipid liposomes; N5 methyltetrahydromethanopterin:coenzyme M methyltransferase; Sodium ion translocation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); MEMBRANE PROTEIN; METHYLTRANSFERASE;

EID: 0029956986     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0857u.x     Document Type: Article
Times cited : (47)

References (41)
  • 1
    • 0000694228 scopus 로고
    • Molecular weight estimation of proteins by electrophoresis in polyacrylamide gels of graded porosity
    • Andersson, L.-O., Borg, H. & Mikaelsson, M. (1972) Molecular weight estimation of proteins by electrophoresis in polyacrylamide gels of graded porosity. FEBS Lett. 20, 199-202.
    • (1972) FEBS Lett. , vol.20 , pp. 199-202
    • Andersson, L.-O.1    Borg, H.2    Mikaelsson, M.3
  • 2
    • 0026568856 scopus 로고
    • The methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina mazei strain Gö1 is a primary sodium pump
    • Becher, B., Müller, V. & Gottschalk, G. (1992a) The methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina mazei strain Gö1 is a primary sodium pump, FEMS Microbiol. Lett. 91, 239-244.
    • (1992) FEMS Microbiol. Lett. , vol.91 , pp. 239-244
    • Becher, B.1    Müller, V.2    Gottschalk, G.3
  • 4
    • 0028181851 scopus 로고
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarciana mazei Gö1
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarciana mazei Gö1. J. Bacteriol. 176, 2543-2550.
    • (1994) J. Bacteriol. , vol.176 , pp. 2543-2550
    • Becher, B.1    Müller, V.2
  • 5
    • 0028265243 scopus 로고
    • Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum
    • Bertram, P. A., Schmitz, R. A., Linder, D. & Thauer, R. K. (1994) Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum, Arch. Microbiol. 161, 220-228.
    • (1994) Arch. Microbiol. , vol.161 , pp. 220-228
    • Bertram, P.A.1    Schmitz, R.A.2    Linder, D.3    Thauer, R.K.4
  • 6
    • 0002325176 scopus 로고
    • Energetics of methanogens
    • (Krulwich. T. A., ed.) Academic Press, Inc., New York
    • Blaut, M., Müller, V. & Gottschalk, G. (1990) Energetics of methanogens, in Bacterial enegetics (Krulwich. T. A., ed.) pp. 505-537. Academic Press, Inc., New York.
    • (1990) Bacterial Enegetics , pp. 505-537
    • Blaut, M.1    Müller, V.2    Gottschalk, G.3
  • 7
    • 0026494662 scopus 로고
    • Energetics of methanogenesis studied in vesicular systems
    • Blaut, M., Müller, V. & Gottschalk, G. (1992) Energetics of methanogenesis studied in vesicular systems, J. Bioenerg. Biomembr: 24, 529-546.
    • (1992) J. Bioenerg. Biomembr , vol.24 , pp. 529-546
    • Blaut, M.1    Müller, V.2    Gottschalk, G.3
  • 8
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H. & Gross, H. J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels, Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0027076754 scopus 로고
    • Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran : Tetrahydromethanopterin formyl-transferase from the extreme thermophile Methanopyrus kandleri
    • Breitung, J., Börner, G., Scholz, S., Linder, D., Stetter, K. O. & Thauer, R. K. (1992) Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran : tetrahydromethanopterin formyl-transferase from the extreme thermophile Methanopyrus kandleri, Eur. J. Biochem. 210, 971-981.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 971-981
    • Breitung, J.1    Börner, G.2    Scholz, S.3    Linder, D.4    Stetter, K.O.5    Thauer, R.K.6
  • 11
    • 0028983268 scopus 로고
    • Involvement of the 'A' isoenzyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine
    • Burke, S. A. & Krzycki, J. A. (1995) Involvement of the 'A' isoenzyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine, J. Bacteriol. 177, 4410-4416.
    • (1995) J. Bacteriol. , vol.177 , pp. 4410-4416
    • Burke, S.A.1    Krzycki, J.A.2
  • 13
    • 0026664856 scopus 로고
    • Formation of unilamellar liposomes from total polar lipid extracts of methanogens
    • Choquet, C. G., Patel, C. B., Beveridge, T. J. & Sprott, G. D. (1992) Formation of unilamellar liposomes from total polar lipid extracts of methanogens, Appl. Environ. Microbiol. 58, 2894-2900.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2894-2900
    • Choquet, C.G.1    Patel, C.B.2    Beveridge, T.J.3    Sprott, G.D.4
  • 14
    • 0028790975 scopus 로고
    • Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Gö1
    • Deppenmeier, U. (1995) Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Gö1, Arch. Microbiol. 164, 370-376.
    • (1995) Arch. Microbiol. , vol.164 , pp. 370-376
    • Deppenmeier, U.1
  • 15
    • 0022578265 scopus 로고
    • Structure, biosynthesis, and physicochemical properties of archaebacterial lipids
    • De Rosa, M., Gambacorta, A. & Gliozzi, A. (1986) Structure, biosynthesis, and physicochemical properties of archaebacterial lipids, Microbiol. Rev. 50, 70-80.
    • (1986) Microbiol. Rev. , vol.50 , pp. 70-80
    • De Rosa, M.1    Gambacorta, A.2    Gliozzi, A.3
  • 16
    • 0002453871 scopus 로고
    • Archaebacteria: Lipids, membrane structures, and adaption to environmental stresses
    • (di Prisco, G., ed.) Springer-Verlag, Berlin
    • De Rosa, M., Trincone, A., Nicolaus, B. & Gambacorta, A. (1991) Archaebacteria: lipids, membrane structures, and adaption to environmental stresses, in Life under extreme conditions (di Prisco, G., ed.) pp. 61-87, Springer-Verlag, Berlin.
    • (1991) Life under Extreme Conditions , pp. 61-87
    • De Rosa, M.1    Trincone, A.2    Nicolaus, B.3    Gambacorta, A.4
  • 18
    • 0005779957 scopus 로고
    • + extrusion coupled to decarboxylation reactions
    • (Bakker, E. P., ed.) CRC Press, Boca Raton, FL
    • + extrusion coupled to decarboxylation reactions, in Alkali cation transport systems in prokaryotes (Bakker, E. P., ed.) pp. 77-100, CRC Press, Boca Raton, FL.
    • (1993) Alkali Cation Transport Systems in Prokaryotes , pp. 77-100
    • Dimroth, P.1
  • 19
    • 0026543822 scopus 로고
    • Functional reconstitution of membrane proteins in monolayer liposomes from bipolar lipids of Sulfolobus acidocaldarius
    • Elferink, M. G. L., de Wit, J. G., Demel, R., Driessen, A. J. M. & Konings, W. N. (1992) Functional reconstitution of membrane proteins in monolayer liposomes from bipolar lipids of Sulfolobus acidocaldarius, J. Biol. Chem. 267, 1375-1381.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1375-1381
    • Elferink, M.G.L.1    De Wit, J.G.2    Demel, R.3    Driessen, A.J.M.4    Konings, W.N.5
  • 21
    • 0028172838 scopus 로고
    • 5-Methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Catalytic mechanism and sodium ion dependence
    • 5-Methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Catalytic mechanism and sodium ion dependence, Eur. J. Biochem. 226, 465-472.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 465-472
    • Gärtner, P.1    Weiss, D.S.2    Harms, U.3    Thauer, R.K.4
  • 22
    • 0024962345 scopus 로고
    • Different isoenzymes of methylcobalamin:2-mercaptoethanesolfonate methyltransferase predominate in methanol- Versus acetate-grown Methanosarcina barkeri
    • Grahame, D. A. (1989) Different isoenzymes of methylcobalamin:2-mercaptoethanesolfonate methyltransferase predominate in methanol- versus acetate-grown Methanosarcina barkeri, J. Biol. Chem. 264, 12890-12894.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12890-12894
    • Grahame, D.A.1
  • 23
    • 0028988304 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterum thermoauto-trophicum is composed of eight different subunits
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterum thermoauto-trophicum is composed of eight different subunits. Eur. J. Biochem. 228, 640-648.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 640-648
    • Harms, U.1    Weiss, D.S.2    Gärtner, P.3    Linder, D.4    Thauer, R.K.5
  • 24
    • 0345194051 scopus 로고
    • Utilization of trimethylamine and other methyl compounds and methane formation by Methanosarcina barkeri
    • Hippe, H., Caspari, D., Fiehig, K. & Gottschalk, G. (1979) Utilization of trimethylamine and other methyl compounds and methane formation by Methanosarcina barkeri, Proc. Natl Acad. Sci. USA 76, 494-498.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 494-498
    • Hippe, H.1    Caspari, D.2    Fiehig, K.3    Gottschalk, G.4
  • 25
    • 0001693812 scopus 로고
    • Reductive activation of the methyl-tetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH
    • Kengen, S. W. M., Mosterd, J. J., Nelissen, R. L. H., Keltjens, J. T., van der Drift, C. & Vogels, G. D. (1988) Reductive activation of the methyl-tetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH, Arch. Microbiol. 150, 405-412.
    • (1988) Arch. Microbiol. , vol.150 , pp. 405-412
    • Kengen, S.W.M.1    Mosterd, J.J.2    Nelissen, R.L.H.3    Keltjens, J.T.4    Van Der Drift, C.5    Vogels, G.D.6
  • 26
    • 0026503633 scopus 로고
    • Isolation of a 5-hydroxybenzi-midazolylcobamide-containing enzyme involved in the methyltetrahydromethanopterin-coenzyme M methyltransferase reaction in Methanobacterium thermoautotrophicum
    • Kengen, S. W. M., Daas, P. J. H., Duits, E. F. G., Keltjens, J. T., van der Drift, C. & Vogels, G. D. (1992) Isolation of a 5-hydroxybenzi-midazolylcobamide-containing enzyme involved in the methyltetrahydromethanopterin-coenzyme M methyltransferase reaction in Methanobacterium thermoautotrophicum, Biochim. Biophys. Acta 1118, 249-260.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 249-260
    • Kengen, S.W.M.1    Daas, P.J.H.2    Duits, E.F.G.3    Keltjens, J.T.4    Van Der Drift, C.5    Vogels, G.D.6
  • 27
    • 0001611489 scopus 로고
    • Lipids of archaebacteria
    • (Woese, C. R. & Wolfe, R. S., eds) Academic Press. Inc., Orlando, New York, Tokyo
    • Langworthy, T. A. (1985) Lipids of archaebacteria, in The bacteria (Woese, C. R. & Wolfe, R. S., eds) vol. 8, pp. 459-497, Academic Press. Inc., Orlando, New York, Tokyo.
    • (1985) The Bacteria , vol.8 , pp. 459-497
    • Langworthy, T.A.1
  • 28
    • 8944251661 scopus 로고
    • Membrane structure and salt dependence in extremely halophilic bacteria
    • (Heinrich, M. R., ed.) Academic Press, New York
    • Lanyi, J. K. (1976) Membrane structure and salt dependence in extremely halophilic bacteria in Extreme environments: mechanisms of microbiol adaption (Heinrich, M. R., ed.) pp. 295-303, Academic Press, New York.
    • (1976) Extreme Environments: Mechanisms of Microbiol Adaption , pp. 295-303
    • Lanyi, J.K.1
  • 29
    • 0025249347 scopus 로고
    • Purification and characterization of a liposomal-forming tetraether lipid fraction
    • Lo, S. L. & Chang, E. L. (1990) Purification and characterization of a liposomal-forming tetraether lipid fraction, Biochem. Biophys. Res. Commun. 167, 238-243.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 238-243
    • Lo, S.L.1    Chang, E.L.2
  • 30
    • 0029004286 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei strain Gö1
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanosarcina mazei strain Gö1. J. Bacteriol. 177, 2245-2250.
    • (1995) J. Bacteriol. , vol.177 , pp. 2245-2250
    • Lu, W.-P.1    Becher, B.2    Gottschalk, G.3    Ragsdale, S.W.4
  • 32
    • 0024289450 scopus 로고
    • Electron-transport-driven sodium extrusion during methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri
    • Müller, V., Winner, C. & Gottschalk, G. (1988) Electron-transport-driven sodium extrusion during methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri, Eur. J. Biochem. 178, 519-525.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 519-525
    • Müller, V.1    Winner, C.2    Gottschalk, G.3
  • 34
    • 0023973588 scopus 로고
    • Bioenergetics of methanogenesis from acetate by Methanosarcina barkeri
    • Peinemann, S., Müller, V., Blaut, M. & Gottschalk, G. (1988) Bioenergetics of methanogenesis from acetate by Methanosarcina barkeri, J. Bacteriol. 170, 1369-1372.
    • (1988) J. Bacteriol. , vol.170 , pp. 1369-1372
    • Peinemann, S.1    Müller, V.2    Blaut, M.3    Gottschalk, G.4
  • 35
    • 0025683248 scopus 로고
    • Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and ΔH
    • Rospert, S., Linden, D., Ellermann, J. & Thauer, R. K. (1990) Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and ΔH, Eur. J. Biochem. 194, 871-877.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 871-877
    • Rospert, S.1    Linden, D.2    Ellermann, J.3    Thauer, R.K.4
  • 36
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 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 of 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 37
    • 0026485429 scopus 로고
    • A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
    • Schmitz, R. A., Albracht, S. P. J. & Thauer, R. K. (1992) A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei, Eur. J. Biochem. 209, 1013-1018.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 1013-1018
    • Schmitz, R.A.1    Albracht, S.P.J.2    Thauer, R.K.3
  • 38
    • 0027504341 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 27, 115 -121.
    • (1993) Eur. J. Biochem. , vol.27 , pp. 115-121
    • Stupperich, E.1    Juza, A.2    Hoppert, M.3    Mayer, F.4
  • 39
    • 0018377780 scopus 로고
    • Diphytanyl and dibiphytanyl ether lipids of methanogenic archaebacteria
    • Tornabene, T. G. & Langworthy, T. A. (1979) Diphytanyl and dibiphytanyl ether lipids of methanogenic archaebacteria, Science 203, 51-53.
    • (1979) Science , vol.203 , pp. 51-53
    • Tornabene, T.G.1    Langworthy, T.A.2
  • 40
    • 0028587832 scopus 로고
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor
    • 5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor, Eur. J. Biochem. 226, 799-809.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 799-809
    • Weiss, D.S.1    Cärtner, P.2    Thauer, R.K.3
  • 41
    • 0027157321 scopus 로고
    • Function of methylcobalmin: Coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri
    • Yeliseev, A., Gärtner, P., Harms, U., Linder, D. & Thauer, R. K. (1993) Function of methylcobalmin: coenzyme M methyltransferase isoenzyme II in Methanosarcina barkeri, Arch. Microbiol, 159, 530-536.
    • (1993) Arch. Microbiol , vol.159 , pp. 530-536
    • Yeliseev, A.1    Gärtner, P.2    Harms, U.3    Linder, D.4    Thauer, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.