메뉴 건너뛰기




Volumn 103, Issue 6, 2012, Pages 1218-1226

On the thermodynamic efficiency of Ca2+-ATPase molecular machines

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; CALCIUM;

EID: 84866503276     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.07.057     Document Type: Article
Times cited : (13)

References (49)
  • 2
    • 0019891830 scopus 로고
    • Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • M. Caffrey, and G.W. Feigenson Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics Biochemistry 20 1981 1949 1961
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 3
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: The case of the calcium pump
    • DOI 10.1016/S0304-4157(98)00010-0, PII S0304415798000100
    • A.G. Lee How lipids interact with an intrinsic membrane protein: the case of the calcium pump Biochim. Biophys. Acta 1376 1998 381 390 (Pubitemid 28517887)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 381-390
    • Lee, A.G.1
  • 4
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • DOI 10.1146/annurev.biophys.36.040306.132643
    • O.S. Andersen, and R.E. Koeppe 2nd Bilayer thickness and membrane protein function: an energetic perspective Annu. Rev. Biophys. Biomol. Struct. 36 2007 107 130 (Pubitemid 46998112)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 5
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function - The hydrophobic matching hypothesis revisited
    • DOI 10.1016/j.bbamem.2004.06.009, PII S0005273604001634, Lipid-Protein Interactions
    • M.O. Jensen, and O.G. Mouritsen Lipids do influence protein function - the hydrophobic matching hypothesis revisited Biochim. Biophys. Acta 1666 2004 205 226 (Pubitemid 39429479)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 7
    • 79955879215 scopus 로고    scopus 로고
    • Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes
    • Y. Sonntag, and M. Musgaard L. Thogersen Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes Nat. Commun. 2 2012 304
    • (2012) Nat. Commun. , vol.2 , pp. 304
    • Sonntag, Y.1    Musgaard, M.2    Thogersen, L.3
  • 8
    • 0014940130 scopus 로고
    • Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum
    • D.H. MacLennan Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum J. Biol. Chem. 245 1970 4508 4518
    • (1970) J. Biol. Chem. , vol.245 , pp. 4508-4518
    • MacLennan, D.H.1
  • 10
    • 0030908304 scopus 로고    scopus 로고
    • 2+-ATPase: ATP hydrolysis, ATP synthesis and heat production
    • DOI 10.1016/S0014-5793(97)00244-5, PII S0014579397002445
    • 2+-ATPase: ATP hydrolysis, ATP synthesis and heat production FEBS Lett. 406 1997 201 204 (Pubitemid 27156990)
    • (1997) FEBS Letters , vol.406 , Issue.1-2 , pp. 201-204
    • De Meis, L.1    Bianconi, M.L.2    Suzano, V.A.3
  • 11
    • 0035816710 scopus 로고    scopus 로고
    • 2+-ATPase. Regulation by ADP
    • 2+-ATPase. Regulation by ADP J. Biol. Chem. 276 2001 25078 25087
    • (2001) J. Biol. Chem. , vol.276 , pp. 25078-25087
    • De Meis, L.1
  • 12
    • 0036628770 scopus 로고    scopus 로고
    • 2+-ATPases (SERCA): Energy transduction and heat production in transport ATPases
    • DOI 10.1007/s00232-001-0171-5
    • 2+-ATPases (SERCA): energy transduction and heat production in transport ATPases J. Membr. Biol. 188 2002 1 9 (Pubitemid 34743697)
    • (2002) Journal of Membrane Biology , vol.188 , Issue.1 , pp. 1-9
    • De Meis, L.1
  • 13
    • 0037053302 scopus 로고    scopus 로고
    • 2+-ATPase. Coupling effects of dimethyl sulfoxide and low temperature
    • DOI 10.1074/jbc.M200648200
    • 2+-ATPase: coupling effects of dimethyl sulfoxide and low temperature J. Biol. Chem. 277 2002 16868 16872 (Pubitemid 34967711)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16868-16872
    • Barata, H.1    De Meis, L.2
  • 14
    • 0142149162 scopus 로고    scopus 로고
    • 2+-ATPase: Uncoupled ATP hydrolysis and thermogenic activity
    • DOI 10.1074/jbc.M308280200
    • 2+-ATPase: uncoupled ATP hydrolysis and thermogenic activity J. Biol. Chem. 278 2003 41856 41861 (Pubitemid 37310446)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41856-41861
    • De Meis, L.1
  • 18
    • 33947654952 scopus 로고    scopus 로고
    • Microscopic detection of thermogenesis in a single HeLa cell
    • M. Suzuki, and V. Tseeb S. Ishiwata Microscopic detection of thermogenesis in a single HeLa cell Biophys. J. 92 2007 L46 L48
    • (2007) Biophys. J. , vol.92
    • Suzuki, M.1    Tseeb, V.2    Ishiwata, S.3
  • 19
    • 48249119161 scopus 로고    scopus 로고
    • Water polarization under thermal gradients
    • F. Bresme, and A. Lervik S. Kjelstrup Water polarization under thermal gradients Phys. Rev. Lett. 101 2008 020602
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 020602
    • Bresme, F.1    Lervik, A.2    Kjelstrup, S.3
  • 20
    • 84858025741 scopus 로고    scopus 로고
    • Thermomolecular orientation of nonpolar fluids
    • F. Römer, and F. Bresme J.M. Rubí Thermomolecular orientation of nonpolar fluids Phys. Rev. Lett. 108 2012 105901
    • (2012) Phys. Rev. Lett. , vol.108 , pp. 105901
    • Römer, F.1    Bresme, F.2    Rubí, J.M.3
  • 24
    • 0026457728 scopus 로고
    • Standard thermodynamic formation properties for the adenosine 5′-triphosphate series
    • R.A. Alberty, and R.N. Goldberg Standard thermodynamic formation properties for the adenosine 5′-triphosphate series Biochemistry 31 1992 10610 10615
    • (1992) Biochemistry , vol.31 , pp. 10610-10615
    • Alberty, R.A.1    Goldberg, R.N.2
  • 25
    • 0345415144 scopus 로고    scopus 로고
    • Thermodynamics of the hydrolysis of adenosine triphosphate as a function of temperature, pH, pMg, and ionic strength
    • R.A. Alberty Thermodynamics of the hydrolysis of adenosine triphosphate as a function of temperature, pH, pMg, and ionic strength J. Phys. Chem. B 107 2003 12324 12330
    • (2003) J. Phys. Chem. B , vol.107 , pp. 12324-12330
    • Alberty, R.A.1
  • 26
    • 41549116226 scopus 로고    scopus 로고
    • Anticipating antiport in P-type ATPases
    • V. Niggli, and E. Sigel Anticipating antiport in P-type ATPases Trends Biochem. Sci. 33 2008 156 160
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 156-160
    • Niggli, V.1    Sigel, E.2
  • 28
    • 0021262493 scopus 로고
    • Channel-mediated monovalent cation fluxes in isolated sarcoplasmic reticulum vesicles
    • A.M. Garcia, and C. Miller Channel-mediated monovalent cation fluxes in isolated sarcoplasmic reticulum vesicles J. Gen. Physiol. 83 1984 819 839 (Pubitemid 14116895)
    • (1984) Journal of General Physiology , vol.83 , Issue.6 , pp. 819-839
    • Garcia, A.M.1    Miller, C.2
  • 29
    • 0031961854 scopus 로고    scopus 로고
    • Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles
    • F. Kamp, P. Donoso, and C. Hidalgo Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles Biophys. J. 74 1998 290 296 (Pubitemid 28041756)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 290-296
    • Kamp, F.1    Donoso, P.2    Hidalgo, C.3
  • 30
    • 0019469837 scopus 로고
    • Calcium transport and monovalent cation and proton fluxes in sarcoplasmic reticulum vesicles
    • G. Meissner Calcium transport and monovalent cation and proton fluxes in sarcoplasmic reticulum vesicles J. Biol. Chem. 256 1981 636 643 (Pubitemid 11151434)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.2 , pp. 636-643
    • Meissner, G.1
  • 33
    • 28944448017 scopus 로고    scopus 로고
    • The mesoscopic dynamics of thermodynamic systems
    • DOI 10.1021/jp052904i
    • D. Reguera, J.M. Rubí, and J.M.G. Vilar The mesoscopic dynamics of thermodynamic systems J. Phys. Chem. B 109 2005 21502 21515 (Pubitemid 41784776)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.46 , pp. 21502-21515
    • Reguera, D.1    Rubi, J.M.2    Vilar, J.M.G.3
  • 34
    • 36849130198 scopus 로고
    • Some deductions from a formal statistical mechanical theory of chemical kinetics
    • J. Ross, and P. Mazur Some deductions from a formal statistical mechanical theory of chemical kinetics J. Chem. Phys. 35 1961 19 28
    • (1961) J. Chem. Phys. , vol.35 , pp. 19-28
    • Ross, J.1    Mazur, P.2
  • 38
    • 0033214701 scopus 로고    scopus 로고
    • 2+-ATPase of blood platelets. Effect of the platelet activating factor
    • 2+-ATPase of blood platelets. Effect of the platelet activating factor J. Biol. Chem. 274 1999 28344 28350
    • (1999) J. Biol. Chem. , vol.274 , pp. 28344-28350
    • Mitidieri, F.1    De Meis, L.2
  • 40
    • 0035817358 scopus 로고    scopus 로고
    • Slippage and uncoupling in P-type cation pumps; implications for energy transduction mechanisms and regulation of metabolism
    • DOI 10.1016/S0005-2736(01)00356-X, PII S000527360100356X
    • M.C. Berman Slippage and uncoupling in P-type cation pumps; implications for energy transduction mechanisms and regulation of metabolism Biochim. Biophys. Acta 1513 2001 95 121 (Pubitemid 32706409)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1513 , Issue.2 , pp. 95-121
    • Berman, M.C.1
  • 42
    • 52549098388 scopus 로고    scopus 로고
    • Inhibition of a cardiac sarcoplasmic reticulum chloride channel by tamoxifen
    • S. Beca, and E. Pavlov G.J. Kargacin Inhibition of a cardiac sarcoplasmic reticulum chloride channel by tamoxifen Pflugers Arch. 457 2008 121 135
    • (2008) Pflugers Arch. , vol.457 , pp. 121-135
    • Beca, S.1    Pavlov, E.2    Kargacin, G.J.3
  • 46
    • 23844508956 scopus 로고    scopus 로고
    • The nonequilibrium thermodynamics of small systems
    • C. Bustamante, J. Liphardt, and F. Ritort The nonequilibrium thermodynamics of small systems Phys. Today 58 2005 43 48 (Pubitemid 41148702)
    • (2005) Physics Today , vol.58 , Issue.7 , pp. 43-48
    • Bustamante, C.1    Liphardt, J.2    Ritort, F.3
  • 47
    • 84954358552 scopus 로고    scopus 로고
    • Energetics of kinesin-1 stepping mechanism
    • K. Kawaguchi Energetics of kinesin-1 stepping mechanism FEBS Lett. 582 2008 3719 3722
    • (2008) FEBS Lett. , vol.582 , pp. 3719-3722
    • Kawaguchi, K.1
  • 48
    • 0031003997 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of a Brownian motor
    • DOI 10.1126/science.276.5314.917
    • R.D. Astumian Thermodynamics and kinetics of a Brownian motor Science 276 1997 917 922 (Pubitemid 27209083)
    • (1997) Science , vol.276 , Issue.5314 , pp. 917-922
    • Astumian, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.