메뉴 건너뛰기




Volumn 45, Issue , 2008, Pages 153-184

ATP synthesis by decarboxylation phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CITRIC ACID; ION; SODIUM;

EID: 44449151647     PISSN: 00801844     EISSN: 18610412     Source Type: Book Series    
DOI: 10.1007/400_2007_045     Document Type: Article
Times cited : (24)

References (143)
  • 3
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • Angevine CM, Fillingame RH (2003) Aqueous access channels in subunit a of rotary ATP synthase. J Biol Chem 278:6066-6074
    • (2003) J Biol Chem , vol.278 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 4
    • 0345255628 scopus 로고    scopus 로고
    • Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane
    • Angevine CM, Herold KA, Fillingame RH (2003) Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. Proc Natl Acad Sci USA 100:13179-13183
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13179-13183
    • Angevine, C.M.1    Herold, K.A.2    Fillingame, R.H.3
  • 5
    • 0031785261 scopus 로고    scopus 로고
    • The biotin protein MadF of the malonate decarboxylase from Malonomonas rubra
    • Berg M, Dimroth P (1998) The biotin protein MadF of the malonate decarboxylase from Malonomonas rubra. Arch Microbiol 170:464-468
    • (1998) Arch Microbiol , vol.170 , pp. 464-468
    • Berg, M.1    Dimroth, P.2
  • 6
    • 0029983383 scopus 로고    scopus 로고
    • The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5_@'-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group
    • Berg M, Hilbi H, Dimroth P (1996) The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5_@'-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group. Biochemistry 35:4689-4696
    • (1996) Biochemistry , vol.35 , pp. 4689-4696
    • Berg, M.1    Hilbi, H.2    Dimroth, P.3
  • 8
    • 0030893492 scopus 로고    scopus 로고
    • Anaerobic citrate metabolism and its regulation in enterobacteria
    • Bott M (1997) Anaerobic citrate metabolism and its regulation in enterobacteria. Arch Microbiol 167:78-88
    • (1997) Arch Microbiol , vol.167 , pp. 78-88
    • Bott, M.1
  • 9
    • 0028134866 scopus 로고
    • Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: Localization, sequencing and expression
    • Bott M, Dimroth P (1994) Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: Localization, sequencing and expression. Mol Microbiol 14:347-356
    • (1994) Mol Microbiol , vol.14 , pp. 347-356
    • Bott, M.1    Dimroth, P.2
  • 10
    • 0029619792 scopus 로고
    • Regulation of anaerobic citrate metabolism in Klebsiella pneumoniae
    • Bott M, Meyer M, Dimroth P (1995) Regulation of anaerobic citrate metabolism in Klebsiella pneumoniae. Mol Microbiol 18:533-546
    • (1995) Mol Microbiol , vol.18 , pp. 533-546
    • Bott, M.1    Meyer, M.2    Dimroth, P.3
  • 11
    • 0031465120 scopus 로고    scopus 로고
    • Methylmalonyl-CoA decarboxylase from Propionigenium modestum: Cloning and sequencing of the structural genes and purification of the enzyme complex
    • Bott M, Pfister K, Burda P, Kalbermatter O, Woehlke G, Dimroth P (1997) Methylmalonyl-CoA decarboxylase from Propionigenium modestum: cloning and sequencing of the structural genes and purification of the enzyme complex. Eur J Biochem 250:590-599
    • (1997) Eur J Biochem , vol.250 , pp. 590-599
    • Bott, M.1    Pfister, K.2    Burda, P.3    Kalbermatter, O.4    Woehlke, G.5    Dimroth, P.6
  • 12
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase-some probabilities and possibilities
    • Boyer PD (1993) The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim Biophys Acta 1140:215-250
    • (1993) Biochim Biophys Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 13
    • 0035342621 scopus 로고    scopus 로고
    • Sodium ion-translocating decarboxylases
    • Buckel W (2001). Sodium ion-translocating decarboxylases. Biochim Biophys Acta 1505:15-27
    • (2001) Biochim Biophys Acta , vol.1505 , pp. 15-27
    • Buckel, W.1
  • 14
    • 0021093632 scopus 로고
    • Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria
    • Buckel W, Semmler R (1983) Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria. Eur J Biochem 136:427-434
    • (1983) Eur J Biochem , vol.136 , pp. 427-434
    • Buckel, W.1    Semmler, R.2
  • 15
    • 0036431660 scopus 로고    scopus 로고
    • The transporter classification (TC) system, 2002
    • Busch W, Saier MH Jr (2002) The transporter classification (TC) system, 2002. Crit Rev Biochem Mol Biol 37:287-337
    • (2002) Crit Rev Biochem Mol Biol , vol.37 , pp. 287-337
    • Busch, W.1    Saier Jr, M.H.2
  • 17
    • 0033971704 scopus 로고    scopus 로고
    • Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase
    • Capaldi RA, Schulenberg B, Murray J, Aggeler R (2000) Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase. J Exp Biol 203(Pt1):29-33
    • (2000) J Exp Biol , vol.203 , Issue.PT1 , pp. 29-33
    • Capaldi, R.A.1    Schulenberg, B.2    Murray, J.3    Aggeler, R.4
  • 18
    • 8644259130 scopus 로고    scopus 로고
    • Oxaloacetate decarboxylase of Archaeoglobus fulgidus: Cloning of genes and expression in Escherichia coli
    • Dahinden P, Dimroth P (2004) Oxaloacetate decarboxylase of Archaeoglobus fulgidus: Cloning of genes and expression in Escherichia coli. Arch Microbiol 182:414-420
    • (2004) Arch Microbiol , vol.182 , pp. 414-420
    • Dahinden, P.1    Dimroth, P.2
  • 19
    • 13844270780 scopus 로고    scopus 로고
    • Oxaloacetate decarboxylase of Vibrio cholerae: Purification, characterization, and expression of the genes in Escherichia coli
    • Dahinden P, Auchli Y, Granjon T, Taralczak M, Wild M, Dimroth P (2005a) Oxaloacetate decarboxylase of Vibrio cholerae: Purification, characterization, and expression of the genes in Escherichia coli. Arch Microbiol 183:121-129
    • (2005) Arch Microbiol , vol.183 , pp. 121-129
    • Dahinden, P.1    Auchli, Y.2    Granjon, T.3    Taralczak, M.4    Wild, M.5    Dimroth, P.6
  • 21
    • 51249176406 scopus 로고
    • Malonomonas rubra gen. nov., sp. nov., a microaerotolerant anaerobic bacterium growing by decarboxylation of malonate
    • Dehning I, Schink B (1989) Malonomonas rubra gen. nov., sp. nov., a microaerotolerant anaerobic bacterium growing by decarboxylation of malonate. Arch Microbiol 151:427-433
    • (1989) Arch Microbiol , vol.151 , pp. 427-433
    • Dehning, I.1    Schink, B.2
  • 22
    • 0026507063 scopus 로고
    • Energy conservation by succinate decarboxylation in Veillonella parvula
    • Denger K, Schink B (1982) Energy conservation by succinate decarboxylation in Veillonella parvula. J Gen Microbiol 138:967-971
    • (1982) J Gen Microbiol , vol.138 , pp. 967-971
    • Denger, K.1    Schink, B.2
  • 23
    • 0029092741 scopus 로고
    • + pump and its individual subunits in Escherichia coli and analysis of their function
    • + pump and its individual subunits in Escherichia coli and analysis of their function. Eur J Biochem 231:790-801
    • (1995) Eur J Biochem , vol.231 , pp. 790-801
    • DiBerardino, M.1    Dimroth, P.2
  • 26
    • 0019335466 scopus 로고
    • A new sodium-transport system energized by the decarboxylation of oxaloacetate
    • Dimroth P (1980) A new sodium-transport system energized by the decarboxylation of oxaloacetate. FEBS Lett 122:234-236
    • (1980) FEBS Lett , vol.122 , pp. 234-236
    • Dimroth, P.1
  • 27
    • 0020077527 scopus 로고
    • The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes
    • Dimroth P (1982a) The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur J Biochem 121:435-441
    • (1982) Eur J Biochem , vol.121 , pp. 435-441
    • Dimroth, P.1
  • 28
    • 0020076670 scopus 로고
    • +-activated oxaloacetate decarboxylase from Klebsiella aerogenes
    • +-activated oxaloacetate decarboxylase from Klebsiella aerogenes. Eur J Biochem 121:443-449
    • (1982) Eur J Biochem , vol.121 , pp. 443-449
    • Dimroth, P.1
  • 29
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • Dimroth P (1997) Primary sodium ion translocating enzymes. Biochim Biophys Acta 1318:11-51
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 30
  • 31
    • 7244259181 scopus 로고    scopus 로고
    • +-coupled ATP synthases operating at low electrochemical potential
    • +-coupled ATP synthases operating at low electrochemical potential. Adv Microb Physiol 49:175-218
    • (2004) Adv Microb Physiol , vol.49 , pp. 175-218
    • Dimroth, P.1    Cook, G.M.2
  • 32
    • 0030851254 scopus 로고    scopus 로고
    • Enzymic and genetic basis for bacterial growth on malonate
    • Dimroth P, Hilbi H (1997) Enzymic and genetic basis for bacterial growth on malonate. Mol Microbiol 25:3-10
    • (1997) Mol Microbiol , vol.25 , pp. 3-10
    • Dimroth, P.1    Hilbi, H.2
  • 33
    • 0031818761 scopus 로고    scopus 로고
    • Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria
    • Dimroth P, Schink B (1998) Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria. Arch Microbiol 170:69-77
    • (1998) Arch Microbiol , vol.170 , pp. 69-77
    • Dimroth, P.1    Schink, B.2
  • 34
    • 0020993273 scopus 로고
    • Subunit composition of oxaloacetate decarboxylase and characterization of the alpha chain as carboxyltransferase
    • Dimroth P, Thomer A (1983) Subunit composition of oxaloacetate decarboxylase and characterization of the alpha chain as carboxyltransferase. Eur J Biochem 137:107-112
    • (1983) Eur J Biochem , vol.137 , pp. 107-112
    • Dimroth, P.1    Thomer, A.2
  • 35
    • 0027474059 scopus 로고
    • On the mechanism of sodium ion translocation by oxaloacetate decarboxylase of Klebsiella pneumoniae
    • Dimroth P, Thomer A (1993) On the mechanism of sodium ion translocation by oxaloacetate decarboxylase of Klebsiella pneumoniae. Biochemistry 32:1734-1739
    • (1993) Biochemistry , vol.32 , pp. 1734-1739
    • Dimroth, P.1    Thomer, A.2
  • 36
    • 0033609081 scopus 로고    scopus 로고
    • Energy transduction in the sodium F-ATPase of Propionigenium modestum
    • Dimroth P, Wang H, Grabe M, Oster G (1999) Energy transduction in the sodium F-ATPase of Propionigenium modestum. Proc Natl Acad Sci USA 96:4924-4929
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4924-4929
    • Dimroth, P.1    Wang, H.2    Grabe, M.3    Oster, G.4
  • 38
    • 33645796449 scopus 로고    scopus 로고
    • Catalytic and mechanical cycles in F-ATP synthases. Fourth in the cycles review series
    • Dimroth P, von Ballmoos C, Meier T (2006) Catalytic and mechanical cycles in F-ATP synthases. Fourth in the cycles review series. EMBO Rep 7:276-282
    • (2006) EMBO Rep , vol.7 , pp. 276-282
    • Dimroth, P.1    von Ballmoos, C.2    Meier, T.3
  • 39
    • 0032576724 scopus 로고    scopus 로고
    • Energy transduction in ATP synthase
    • Elston T, Wang H, Oster G (1998) Energy transduction in ATP synthase. Nature 391:510-513
    • (1998) Nature , vol.391 , pp. 510-513
    • Elston, T.1    Wang, H.2    Oster, G.3
  • 41
    • 33745882947 scopus 로고    scopus 로고
    • 0 ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum
    • 0 ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum. J Bacteriol 188:5045-5054
    • (2006) J Bacteriol , vol.188 , pp. 5045-5054
    • Ferguson, S.A.1    Keis, S.2    Cook, G.M.3
  • 42
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • Fillingame RH, Angevine CM, Dmitriev OY (2003) Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett 555:29-34
    • (2003) FEBS Lett , vol.555 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 43
    • 0021136417 scopus 로고
    • Construction and characterization of an Escherichia coli strain with a uncI mutation
    • Gay NJ (1984) Construction and characterization of an Escherichia coli strain with a uncI mutation. J Bacteriol 158:820-825
    • (1984) J Bacteriol , vol.158 , pp. 820-825
    • Gay, N.J.1
  • 45
    • 5044222214 scopus 로고    scopus 로고
    • Transcarboxylase 5 S structures: Assembly and catalytic mechanism of a multienzyme complex subunit
    • Hall PR, Zheng R, Lizamma A, Pusztai-Carey M, Carey PR, Lee VC (2004) Transcarboxylase 5 S structures: Assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J 23:3621-3631
    • (2004) EMBO J , vol.23 , pp. 3621-3631
    • Hall, P.R.1    Zheng, R.2    Lizamma, A.3    Pusztai-Carey, M.4    Carey, P.R.5    Lee, V.C.6
  • 47
    • 0026694791 scopus 로고
    • Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme
    • Hilbi H, Dehning I, Schink B, Dimroth P (1992) Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur J Biochem 207:117-123
    • (1992) Eur J Biochem , vol.207 , pp. 117-123
    • Hilbi, H.1    Dehning, I.2    Schink, B.3    Dimroth, P.4
  • 49
    • 0021106008 scopus 로고
    • Purification and characterization of a new sodium-transport decarboxylase. Methylmalonyl-CoA decarboxylase from Veillonella alcalescens
    • Hilpert W, Dimroth P (1983) Purification and characterization of a new sodium-transport decarboxylase. Methylmalonyl-CoA decarboxylase from Veillonella alcalescens. Eur J Biochem 132:579-587
    • (1983) Eur J Biochem , vol.132 , pp. 579-587
    • Hilpert, W.1    Dimroth, P.2
  • 50
    • 0026059441 scopus 로고
    • On the mechanism of sodium ion translocation by methylmalonyl-CoAdecarboxylase from Veillonella alcalescens
    • Hilpert W, Dimroth P (1991) On the mechanism of sodium ion translocation by methylmalonyl-CoAdecarboxylase from Veillonella alcalescens. Eur J Biochem 19:79-86
    • (1991) Eur J Biochem , vol.19 , pp. 79-86
    • Hilpert, W.1    Dimroth, P.2
  • 52
    • 0019926213 scopus 로고
    • An Asp-Asn substitution in the proteolipid subunit of the ATP synthase from Escherichia coli leads to a non-functional proton channel
    • Hoppe J, Scheirer HU, Friedl P, Sebald W (1982) An Asp-Asn substitution in the proteolipid subunit of the ATP synthase from Escherichia coli leads to a non-functional proton channel. FEBS Lett 145:21-29
    • (1982) FEBS Lett , vol.145 , pp. 21-29
    • Hoppe, J.1    Scheirer, H.U.2    Friedl, P.3    Sebald, W.4
  • 54
    • 0027367414 scopus 로고
    • Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula
    • Huder JB, Dimroth P (1993) Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula. J Biol Chem 268:24564-24571
    • (1993) J Biol Chem , vol.268 , pp. 24564-24571
    • Huder, J.B.1    Dimroth, P.2
  • 57
    • 0032499690 scopus 로고
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc Natl Acad Sci USA 95:6607-6612
    • (1988) Proc Natl Acad Sci USA , vol.95 , pp. 6607-6612
    • Jiang, W.1    Fillingame, R.H.2
  • 58
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jiang W, Hermolin J, Fillingame RH (2001) The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc Natl Acad Sci USA 98:4966-4971
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 62
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W, Lill H, Engelbrecht S (1997) ATP synthase: An electrochemical transducer with rotatory mechanics. Trends Biochem Sci 22:420-423
    • (1997) Trends Biochem Sci , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 64
    • 0027144899 scopus 로고
    • 0 ATPase in Escherichia coli by homologous recombination
    • 0 ATPase in Escherichia coli by homologous recombination. Eur J Biochem 218:937-944
    • (1993) Eur J Biochem , vol.218 , pp. 937-944
    • Kaim, G.1    Dimroth, P.2
  • 66
    • 0028844612 scopus 로고
    • +-coupled ATP synthesis in the Escherichia coli host cells
    • +-coupled ATP synthesis in the Escherichia coli host cells. J Mol Biol 253:726-738
    • (1995) J Mol Biol , vol.253 , pp. 726-738
    • Kaim, G.1    Dimroth, P.2
  • 68
    • 0032531926 scopus 로고    scopus 로고
    • Voltage-generated torque drives the motor of the ATP synthase
    • Kaim G, Dimroth P (1998b) Voltage-generated torque drives the motor of the ATP synthase. EMBO J 17:5887-5895
    • (1998) EMBO J , vol.17 , pp. 5887-5895
    • Kaim, G.1    Dimroth, P.2
  • 69
    • 0033517144 scopus 로고    scopus 로고
    • ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage
    • Kaim G, Dimroth P (1999) ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage. EMBO J 18:4118-4127
    • (1999) EMBO J , vol.18 , pp. 4118-4127
    • Kaim, G.1    Dimroth, P.2
  • 70
    • 0026684344 scopus 로고
    • 0 part of the sodium-ion-dependent ATP synthase of Propionigenium modestum in Escherichia coli
    • 0 part of the sodium-ion-dependent ATP synthase of Propionigenium modestum in Escherichia coli. Eur J Biochem 207:463-470
    • (1992) Eur J Biochem , vol.207 , pp. 463-470
    • Kaim, G.1    Ludwig, W.2    Dimroth, P.3    Schleifer, K.H.4
  • 71
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36:9185-9194
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 75
    • 0027052393 scopus 로고
    • 0 ATPase from Propionigenium modestum: Discovery of a membrane potential dependent step
    • 0 ATPase from Propionigenium modestum: Discovery of a membrane potential dependent step. Biochemistry 31:12665-12672
    • (1992) Biochemistry , vol.31 , pp. 12665-12672
    • Kluge, C.1    Dimroth, P.2
  • 76
    • 0027340171 scopus 로고
    • + concentration: Probing the binding site for the coupling ions
    • + concentration: Probing the binding site for the coupling ions. Biochemistry 32:10378-10386
    • (1993) Biochemistry , vol.32 , pp. 10378-10386
    • Kluge, C.1    Dimroth, P.2
  • 77
    • 0027279864 scopus 로고
    • 0 ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide
    • 0 ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide. J Biol Chem 268:14557-14560
    • (1993) J Biol Chem , vol.268 , pp. 14557-14560
    • Kluge, C.1    Dimroth, P.2
  • 78
    • 0028273056 scopus 로고
    • 0-ATPase from Propionigenium modestum by dicyclohexylcarbodiimide
    • 0-ATPase from Propionigenium modestum by dicyclohexylcarbodiimide. FEBS Lett 340:245-248
    • (1994) FEBS Lett , vol.340 , pp. 245-248
    • Kluge, C.1    Dimroth, P.2
  • 81
    • 0024293219 scopus 로고
    • Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump
    • Laubinger W, Dimroth P (1988) Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry 27:7531-7537
    • (1988) Biochemistry , vol.27 , pp. 7531-7537
    • Laubinger, W.1    Dimroth, P.2
  • 82
    • 0024962378 scopus 로고
    • The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations
    • Laubinger W, Dimroth P (1989) The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations. Biochemistry 28:7194-7198
    • (1989) Biochemistry , vol.28 , pp. 7194-7198
    • Laubinger, W.1    Dimroth, P.2
  • 83
    • 0038731187 scopus 로고    scopus 로고
    • The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains
    • Lolkema JS, Boekema EJ (2003) The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains. FEBS Lett 543:47-50
    • (2003) FEBS Lett , vol.543 , pp. 47-50
    • Lolkema, J.S.1    Boekema, E.J.2
  • 84
    • 0032568845 scopus 로고    scopus 로고
    • 0 ATP synthase as determined by labeling of unique cysteine residues
    • 0 ATP synthase as determined by labeling of unique cysteine residues. J Biol Chem 273:16235-16240
    • (1998) J Biol Chem , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 85
    • 0033560680 scopus 로고    scopus 로고
    • NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulfate micelles
    • Matthey U, Kaim G, Braun D, Wüthrich K, Dimroth P (1999) NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulfate micelles. Eur J Biochem 261:459-467
    • (1999) Eur J Biochem , vol.261 , pp. 459-467
    • Matthey, U.1    Kaim, G.2    Braun, D.3    Wüthrich, K.4    Dimroth, P.5
  • 86
    • 85047698387 scopus 로고    scopus 로고
    • NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/ methanol/water (4: 4: 1)
    • Matthey U, Braun D, Dimroth P (2002) NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/ methanol/water (4: 4: 1). Eur J Biochem 269:1942-1946
    • (2002) Eur J Biochem , vol.269 , pp. 1942-1946
    • Matthey, U.1    Braun, D.2    Dimroth, P.3
  • 87
    • 0026685827 scopus 로고
    • Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3
    • Matthies C, Schink B (1992a) Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3. FEMS Microbiol Lett 79:221-225
    • (1992) FEMS Microbiol Lett , vol.79 , pp. 221-225
    • Matthies, C.1    Schink, B.2
  • 88
    • 0026763806 scopus 로고
    • Reciprocal isomerization of butyrate and isobutyrate by the strictly anaerobic bacterium strain WoGl3 and methanogenic isobutyrate degradation by a defined triculture
    • Matthies C, Schink B (1992b) Reciprocal isomerization of butyrate and isobutyrate by the strictly anaerobic bacterium strain WoGl3 and methanogenic isobutyrate degradation by a defined triculture. Appl Environ Microbiol 58:1435-1439
    • (1992) Appl Environ Microbiol , vol.58 , pp. 1435-1439
    • Matthies, C.1    Schink, B.2
  • 89
    • 0034023853 scopus 로고    scopus 로고
    • Pelospora glutarica gen. nov., sp. nov., a glutarate-fermenting, strictly anaerobic, spore-forming bacterium
    • Matthies C, Springer N, Ludwig W, Schink B (2000) Pelospora glutarica gen. nov., sp. nov., a glutarate-fermenting, strictly anaerobic, spore-forming bacterium. Int J Syst Evol Microbiol 50(Pt2):645-648
    • (2000) Int J Syst Evol Microbiol , vol.50 , Issue.PT2 , pp. 645-648
    • Matthies, C.1    Springer, N.2    Ludwig, W.3    Schink, B.4
  • 93
    • 0038719727 scopus 로고    scopus 로고
    • A unique resting position of the ATP synthase from chloroplasts
    • Mellwig C, Böttcher B (2003) A unique resting position of the ATP synthase from chloroplasts. J Biol Chem 278:18544-18549
    • (2003) J Biol Chem , vol.278 , pp. 18544-18549
    • Mellwig, C.1    Böttcher, B.2
  • 101
    • 32344451446 scopus 로고    scopus 로고
    • Phospholipids occupy the internal lumen of the c ring of the ATP synthase of Escherichia coli
    • Oberfeld B, Brunner J, Dimroth P (2006) Phospholipids occupy the internal lumen of the c ring of the ATP synthase of Escherichia coli Biochemistry 45:1841-1851
    • (2006) Biochemistry , vol.45 , pp. 1841-1851
    • Oberfeld, B.1    Brunner, J.2    Dimroth, P.3
  • 104
    • 0030042331 scopus 로고    scopus 로고
    • +-dependent citrate carrier of Klebsiella pneumoniae: Evidence for asymmetric orientation of the carrier in proteoliposomes
    • +-dependent citrate carrier of Klebsiella pneumoniae: Evidence for asymmetric orientation of the carrier in proteoliposomes. Biochemistry 35:1018-1026
    • (1996) Biochemistry , vol.35 , pp. 1018-1026
    • Pos, K.M.1    Dimroth, P.2
  • 105
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi VK, Girvin ME (1999) Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402:263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 107
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • Rubinstein JL, Walker JE, Henderson R (2003) Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J 22:6182-6192
    • (2003) EMBO J , vol.22 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 109
    • 0031949366 scopus 로고    scopus 로고
    • +-dependent malonate transporter of Malonomonas rubra and its dependence on two seperate genes
    • +-dependent malonate transporter of Malonomonas rubra and its dependence on two seperate genes. J Bacteriol 180:2689-2693
    • (1998) J Bacteriol , vol.180 , pp. 2689-2693
    • Schaffitzel, C.1    Berg, M.2    Dimroth, P.3    Pos, K.M.4
  • 110
    • 0020434732 scopus 로고
    • Propionigenium modestum gen. nov. sp. nov., a new strictly anaerobic, nonsporing bacterium growing on succinate
    • Schink B, Pfennig N (1982) Propionigenium modestum gen. nov. sp. nov., a new strictly anaerobic, nonsporing bacterium growing on succinate. Arch Microbiol 133:209-216
    • (1982) Arch Microbiol , vol.133 , pp. 209-216
    • Schink, B.1    Pfennig, N.2
  • 113
    • 0034622627 scopus 로고    scopus 로고
    • Biosynthesis of the prosthetic group of citrate lyase
    • Schneider K, Dimroth P, Bott M (2000a) Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39:9438-9450
    • (2000) Biochemistry , vol.39 , pp. 9438-9450
    • Schneider, K.1    Dimroth, P.2    Bott, M.3
  • 114
    • 0034693262 scopus 로고    scopus 로고
    • Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group
    • Schneider K, Dimroth P, Bott M (2000b) Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett 483:165-168
    • (2000) FEBS Lett , vol.483 , pp. 165-168
    • Schneider, K.1    Dimroth, P.2    Bott, M.3
  • 115
    • 0036223584 scopus 로고    scopus 로고
    • Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group
    • Schneider K, Kästner CN, Meyer M, Wessel M, Dimroth P, Bott M (2002) Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J Bacteriol 184:2439-2446
    • (2002) J Bacteriol , vol.184 , pp. 2439-2446
    • Schneider, K.1    Kästner, C.N.2    Meyer, M.3    Wessel, M.4    Dimroth, P.5    Bott, M.6
  • 116
    • 2742613426 scopus 로고
    • N,Na′ dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatase from Neurospora crassa and Saccharomyces cerevisiae
    • Sebald W, Machleidt W, Wachter E (1980) N,Na′ dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatase from Neurospora crassa and Saccharomyces cerevisiae. Proc Natl Acad Sci USA 77:785-789
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 785-789
    • Sebald, W.1    Machleidt, W.2    Wachter, E.3
  • 120
    • 0032930779 scopus 로고    scopus 로고
    • +-reducing hydrogenase provides reduced pyridine nucleotides during citrate fermentation by Klebsiella pneumoniae
    • +-reducing hydrogenase provides reduced pyridine nucleotides during citrate fermentation by Klebsiella pneumoniae. J Bacteriol 181:241-245
    • (1999) J Bacteriol , vol.181 , pp. 241-245
    • Steuber, J.1    Krebs, W.2    Bott, M.3    Dimroth, P.4
  • 121
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AG, Walker JE (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286:1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 123
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer RK, Jungermann K, Decker K (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100-180
    • (1977) Bacteriol Rev , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 128
    • 0027970177 scopus 로고
    • 0 ATP synthase suggested by double mutants of the a subunit
    • 0 ATP synthase suggested by double mutants of the a subunit. J Biol Chem 269:30364-30369
    • (1994) J Biol Chem , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 132
    • 3843058939 scopus 로고    scopus 로고
    • The ion channel of F-ATP synthase is the target of toxic organotin compounds
    • von Ballmoos C, Brunner J, Dimroth P (2004) The ion channel of F-ATP synthase is the target of toxic organotin compounds. Proc Natl Acad Sci USA 101:11239-11244
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11239-11244
    • von Ballmoos, C.1    Brunner, J.2    Dimroth, P.3
  • 135
    • 0036000288 scopus 로고    scopus 로고
    • 0 of the sodium ion translocating ATP synthase of Propionigenium modestum from its heterologously expressed and purified subunits
    • 0 of the sodium ion translocating ATP synthase of Propionigenium modestum from its heterologously expressed and purified subunits. Eur J Biochem 269:2567-2573
    • (2002) Eur J Biochem , vol.269 , pp. 2567-2573
    • Wehrle, F.1    Appoldt, Y.2    Kaim, G.3    Dimroth, P.4
  • 136
    • 0036383051 scopus 로고    scopus 로고
    • 0 motor probed by mutational analyses of subunit a
    • 0 motor probed by mutational analyses of subunit a. J Mol Biol 322:369-381
    • (2002) J Mol Biol , vol.322 , pp. 369-381
    • Wehrle, F.1    Kaim, G.2    Dimroth, P.3
  • 137
    • 0041813291 scopus 로고    scopus 로고
    • Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase
    • Wendt KS, Schall I, Huber R, Buckel W, Jacob U (2003) Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase. EMBO J 22:3493-3502
    • (2003) EMBO J , vol.22 , pp. 3493-3502
    • Wendt, K.S.1    Schall, I.2    Huber, R.3    Buckel, W.4    Jacob, U.5
  • 138
    • 0024796057 scopus 로고
    • Isolation and characterization of oxaloacetate decarboxylase of Salmonella typhimurium, a sodium pump
    • Wifling K, Dimroth P (1989) Isolation and characterization of oxaloacetate decarboxylase of Salmonella typhimurium, a sodium pump. Arch Microbiol 152:584-588
    • (1989) Arch Microbiol , vol.152 , pp. 584-588
    • Wifling, K.1    Dimroth, P.2
  • 139
    • 0141988866 scopus 로고    scopus 로고
    • + pump of Klebsiella pneumoniae: Helix VIII comprises a portion of the sodium ion channel
    • + pump of Klebsiella pneumoniae: helix VIII comprises a portion of the sodium ion channel. Biochemistry 42:11615-11624
    • (2003) Biochemistry , vol.42 , pp. 11615-11624
    • Wild, M.R.1    Pos, K.M.2    Dimroth, P.3
  • 141
    • 0026495408 scopus 로고
    • Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium
    • Woehlke G, Wifling K, Dimroth P (1992) Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium. J Biol Chem 267:22798-22803
    • (1992) J Biol Chem , vol.267 , pp. 22798-22803
    • Woehlke, G.1    Wifling, K.2    Dimroth, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.