메뉴 건너뛰기




Volumn 7, Issue 3, 2006, Pages 276-282

Catalytic and mechanical cycles in F-ATP synthases: Fourth in the Cycles Review Series

Author keywords

ATP cycle; C ring structure; Catalytic reaction cycle; F ATP synthase; Ion translocation model; Mechanical rotation; Na+ binding site

Indexed keywords

ADENOSINE DIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 33645796449     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400646     Document Type: Review
Times cited : (114)

References (43)
  • 3
    • 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
  • 4
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer PD (1997) The ATP synthase - a splendid molecular machine. Annu Rev Biochem 66: 717-749
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 11
    • 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
  • 15
    • 0021756489 scopus 로고
    • oATP synthase from Escherichia coli as inferred from labeling with 3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine
    • oATP synthase from Escherichia coli as inferred from labeling with 3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine. Biochem 23: 5610-5616
    • (1984) Biochem , vol.23 , pp. 5610-5616
    • Hoppe, J.1    Brunner, J.2    Jorgensen, B.B.3
  • 16
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jang 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
    • Jang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 17
    • 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
  • 18
    • 0032531926 scopus 로고    scopus 로고
    • Voltage-generated torque drives the motor of the ATP synthase
    • Kaim G, Dimroth P (1998) 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
  • 19
    • 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
  • 20
    • 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
  • 23
    • 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
  • 24
    • 4344658080 scopus 로고    scopus 로고
    • Thermophilic ATP synthase has a decamer c-ring: Indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling
    • Mitome N, Suzuki T, Hayashi S, Yoshida M (2004) Thermophilic ATP synthase has a decamer c-ring: Indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling. Proc Natl Acad Sci USA 101: 12159-12164
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12159-12164
    • Mitome, N.1    Suzuki, T.2    Hayashi, S.3    Yoshida, M.4
  • 27
    • 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
  • 29
    • 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
  • 30
    • 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
  • 33
    • 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
  • 37
    • 0027970177 scopus 로고
    • 0 ATP synthases suggested by double mutants of the a subunit
    • 0 ATP synthases 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
  • 41
    • 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
  • 43
    • 0037457911 scopus 로고    scopus 로고
    • Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein
    • Zhang D, Vik SB (2003) Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein. Biochemistry 42: 331-337
    • (2003) Biochemistry , vol.42 , pp. 331-337
    • Zhang, D.1    Vik, S.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.