메뉴 건너뛰기




Volumn 75, Issue 4, 1998, Pages 1980-1988

Nucleotide and Mg2+ dependency of the thermal denaturation of mitochondrial F1-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; MAGNESIUM; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0031595469     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77639-8     Document Type: Article
Times cited : (17)

References (39)
  • 2
    • 0026766543 scopus 로고
    • Differential scanning calorimetric study of the thermal unfolding of β-lactamase I from Bacillus cereus
    • Arriaga, P., M. Menéndez, J. M. Villacorta, and J. Laynez. 1992. Differential scanning calorimetric study of the thermal unfolding of β-lactamase I from Bacillus cereus. Biochemistry. 31:6603-6607.
    • (1992) Biochemistry , vol.31 , pp. 6603-6607
    • Arriaga, P.1    Menéndez, M.2    Villacorta, J.M.3    Laynez, J.4
  • 4
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase. Some probabilities and possibilities
    • Boyer, P. D. 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
  • 6
    • 0020491221 scopus 로고
    • Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic studies
    • Cross, R. L., C. Grubmeyer, and H. S. Penefsky. 1982. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic studies. J. Biol. Chem. 257:12101-12105.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12101-12105
    • Cross, R.L.1    Grubmeyer, C.2    Penefsky, H.S.3
  • 7
    • 0020490477 scopus 로고
    • 1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites
    • 1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites. J. Biol. Chem. 257:2874-2881.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2874-2881
    • Cross, R.L.1    Nalin, C.M.2
  • 8
    • 0027114208 scopus 로고
    • 1-ATPase activity by binding of (2-azido-)ADP to a slowly exchangeable non-catalytic nucleotide binding site
    • 1-ATPase activity by binding of (2-azido-)ADP to a slowly exchangeable non-catalytic nucleotide binding site. Biochim. Biophys. Acta. 1100:329-338.
    • (1992) Biochim. Biophys. Acta. , vol.1100 , pp. 329-338
    • Edel, C.M.1    Hartog, A.F.2    Berden, J.A.3
  • 10
    • 0025285535 scopus 로고
    • Calorimetrically determined dynamics of complex unfolding transitions in proteins
    • Freire, E., W. W. Osdol, O. L. Mayorga, and J. M. Sánchez-Ruiz. 1990. Calorimetrically determined dynamics of complex unfolding transitions in proteins. Annu. Rev. Biophys. Chem. 19:159-188.
    • (1990) Annu. Rev. Biophys. Chem. , vol.19 , pp. 159-188
    • Freire, E.1    Osdol, W.W.2    Mayorga, O.L.3    Sánchez-Ruiz, J.M.4
  • 11
    • 0028792140 scopus 로고
    • +-ATPase (ATP synthase): Catalytic site and roles of subunit interactions in energy coupling
    • +-ATPase (ATP synthase): catalytic site and roles of subunit interactions in energy coupling. Biochem. Soc. Trans. 23:785-789.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 785-789
    • Futai, M.1    Omote, H.2    Maeda, M.3
  • 12
  • 13
    • 0016818871 scopus 로고
    • Interaction of adenine nucleotides with multiple binding sites of beef heart mitochondrial adenosine triphosphatase
    • Garret, N. E., and H. S. Penefsky. 1975. Interaction of adenine nucleotides with multiple binding sites of beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 250:6640-6647.
    • (1975) J. Biol. Chem. , vol.250 , pp. 6640-6647
    • Garret, N.E.1    Penefsky, H.S.2
  • 14
    • 0020491305 scopus 로고
    • 1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model
    • 1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model. J. Biol. Chem. 257: 12030-12038.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12030-12038
    • Gresser, M.J.1    Myers, J.A.2    Boyer, P.D.3
  • 15
    • 0019887897 scopus 로고
    • Cooperativity between catalytic sites in the mechanism of action of beef heart mitochondrial adenosine triphosphatase
    • Grubmeyer, C., and H. S. Penefsky. 1981. Cooperativity between catalytic sites in the mechanism of action of beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 256:3728-3734.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3728-3734
    • Grubmeyer, C.1    Penefsky, H.S.2
  • 16
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and E. Freire. 1995. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta. 1241: 295-322.
    • (1995) Biochim. Biophys. Acta. , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 18
    • 0027982788 scopus 로고
    • 1-ATPaseis due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP
    • 1-ATPaseis due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP. J. Biol. Chem. 269:319-325.
    • (1994) J. Biol. Chem. , vol.269 , pp. 319-325
    • Jault, J.M.1    Allison, W.S.2
  • 19
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge, W., H. Lill, and S. Engelbrecht. 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
  • 20
    • 0023007366 scopus 로고
    • 1-ATPase. Conditions that affect occupancy of catalytic and noncatalytic sites
    • 1-ATPase. Conditions that affect occupancy of catalytic and noncatalytic sites. J. Biol. Chem. 261:12544-12549.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12544-12549
    • Kironde, F.A.S.1    Cross, R.L.2
  • 21
    • 0015523814 scopus 로고
    • The subunit structure of beef heart mitochondrial adenosine triphosphatase. Isolation procedures
    • Knowles, A. F., and H. S. Penefsky. 1972. The subunit structure of beef heart mitochondrial adenosine triphosphatase. Isolation procedures. J. Biol. Chem. 247:6617-6623.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6617-6623
    • Knowles, A.F.1    Penefsky, H.S.2
  • 22
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • Lepock, J. R., K. P. Ritchie, M. C. Kolios, A. M. Rodahl, K. A. Heinz, and J. Kruuv. 1992. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry. 31:12706-12712.
    • (1992) Biochemistry , vol.31 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, A.M.4    Heinz, K.A.5    Kruuv, J.6
  • 23
    • 0030615047 scopus 로고    scopus 로고
    • 1-ATPase catalytic sites under crystallization conditions
    • 1-ATPase catalytic sites under crystallization conditions. FEBS Lett. 404:15-18.
    • (1997) FEBS Lett. , vol.404 , pp. 15-18
    • Löbau, S.1    Weber, J.2    Senior, A.E.3
  • 24
    • 0027451387 scopus 로고
    • 1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites
    • 1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites. J. Biol. Chem. 268:23179-23185.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23179-23185
    • Milgrom, Y.M.1    Cross, R.L.2
  • 25
    • 0027102911 scopus 로고
    • 2+- and ADP-dependent inactivation during ATP hydrolysis
    • 2+- and ADP-dependent inactivation during ATP hydrolysis. Biochemistry. 31:12885-12892.
    • (1992) Biochemistry , vol.31 , pp. 12885-12892
    • Murataliev, M.B.1
  • 27
    • 0020490899 scopus 로고
    • 1-ATPase. Specificity of cooperative interactions between catalytic sites
    • 1-ATPase. Specificity of cooperative interactions between catalytic sites. J. Biol. Chem. 257:8055-8060.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8055-8060
    • Nalin, C.M.1    Cross, R.L.2
  • 29
    • 0030464057 scopus 로고    scopus 로고
    • 1 moiety are kinetically equivalent in hydrolyzing ATP
    • 1 moiety are kinetically equivalent in hydrolyzing ATP. J. Biol. Chem. 271:32546-32550.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32546-32550
    • Reynafarje, B.D.1    Pedersen, P.L.2
  • 30
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sánchez-Ruiz, J. M. 1992. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61:921-935.
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sánchez-Ruiz, J.M.1
  • 31
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Subcellular Biochemistry. B. B. Biswas and Siddharta Roy, editors. Plenum Press, New York
    • Sánchez-Ruiz, J. M. 1995. Differential scanning calorimetry of proteins. In Subcellular Biochemistry. Proteins: Structure, Function and Engineering, Vol 24. B. B. Biswas and Siddharta Roy, editors. Plenum Press, New York. 133-176.
    • (1995) Proteins: Structure, Function and Engineering , vol.24 , pp. 133-176
    • Sánchez-Ruiz, J.M.1
  • 32
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolisin
    • Sánchez-Ruiz, J. M., J. L. López-Lacomba, M. Cortijo, and P. L. Mateo. 1988. Differential scanning calorimetry of the irreversible thermal denaturation of thermolisin. Biochemistry. 27:1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sánchez-Ruiz, J.M.1    López-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 34
    • 0025856007 scopus 로고
    • Four tight nucleotide binding sites of chloroplast coupling factor 1
    • Shapiro, A. B., A. H. Huber, and R. E. McCarty. 1991. Four tight nucleotide binding sites of chloroplast coupling factor 1. J. Biol. Chem. 266:4194-4200.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4194-4200
    • Shapiro, A.B.1    Huber, A.H.2    McCarty, R.E.3
  • 35
    • 0019840442 scopus 로고
    • Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN′, and the inhibitor-subtilisin complex
    • Takahashi, K., and J. M. Sturtevant. 1981. Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN′, and the inhibitor-subtilisin complex. Biochemistry. 20:6185-6190.
    • (1981) Biochemistry , vol.20 , pp. 6185-6190
    • Takahashi, K.1    Sturtevant, J.M.2
  • 38
    • 0030592112 scopus 로고    scopus 로고
    • 0-ATP synthase: Development of direct optical probes of the catalytic mechanism
    • 0-ATP synthase: development of direct optical probes of the catalytic mechanism. Biochim. Biophys. Acta. 1275:101-104.
    • (1996) Biochim. Biophys. Acta. , vol.1275 , pp. 101-104
    • Weber, J.1    Senior, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.