메뉴 건너뛰기




Volumn 46, Issue 30, 2007, Pages 8785-8797

Determination of the partial reactions of rotational catalysis in F 1-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CONCENTRATION (PROCESS); HYDROLYSIS; MOLECULAR ORIENTATION; REACTION KINETICS;

EID: 34547626611     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700610m     Document Type: Article
Times cited : (30)

References (71)
  • 5
    • 0037070150 scopus 로고    scopus 로고
    • Catalytic site occupancy during ATP synthase catalysis
    • Boyer, P. D. (2002) Catalytic site occupancy during ATP synthase catalysis, FEBS Lett. 512, 29-32.
    • (2002) FEBS Lett , vol.512 , pp. 29-32
    • Boyer, P.D.1
  • 15
    • 0031027579 scopus 로고    scopus 로고
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits, J. Biol. Chem. 272, 2300-2306.
    • (1997) J. Biol. Chem , vol.272 , pp. 2300-2306
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 16
    • 0029040551 scopus 로고
    • The ATP synthase γ subunit: Suppressor mutagenesis reveals three helical regions involved in energy coupling
    • Nakamoto, R. K., Al-Shawi, M. K., and Futai, M. (1995) The ATP synthase γ subunit: suppressor mutagenesis reveals three helical regions involved in energy coupling, J. Biol. Chem. 270, 14042-14046.
    • (1995) J. Biol. Chem , vol.270 , pp. 14042-14046
    • Nakamoto, R.K.1    Al-Shawi, M.K.2    Futai, M.3
  • 17
    • 0027471965 scopus 로고
    • The γ subunit of the Escherichia coli ATP synthase: Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant, γMet-23→Lys
    • Nakamoto, R. K., Maeda, M., and Futai, M. (1993) The γ subunit of the Escherichia coli ATP synthase: mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant, γMet-23→Lys, J. Biol. Chem. 268, 867-872.
    • (1993) J. Biol. Chem , vol.268 , pp. 867-872
    • Nakamoto, R.K.1    Maeda, M.2    Futai, M.3
  • 18
    • 0023350878 scopus 로고
    • The defective proton-ATPase of uncA mutants of Escherichia coli: ATP-binding and ATP-induced conformational change in mutant α-subunits
    • Rao, R., Perlin, D. S., and Senior, A. E. (1987) The defective proton-ATPase of uncA mutants of Escherichia coli: ATP-binding and ATP-induced conformational change in mutant α-subunits, Arch. Biochem. Biophys. 255, 309-315.
    • (1987) Arch. Biochem. Biophys , vol.255 , pp. 309-315
    • Rao, R.1    Perlin, D.S.2    Senior, A.E.3
  • 19
    • 0023645163 scopus 로고
    • The defective proton-ATPase of uncA mutants of Escherichia coli: Identification by DNA sequencing of residues in the α-subunit which are essential for catalysis or normal assembly
    • Maggio, M. B., Pagan, J., Parsonage, D., Hatch, L., and Senior, A. E. (1987) The defective proton-ATPase of uncA mutants of Escherichia coli: identification by DNA sequencing of residues in the α-subunit which are essential for catalysis or normal assembly, J. Biol. Chem. 262, 8981-8984.
    • (1987) J. Biol. Chem , vol.262 , pp. 8981-8984
    • Maggio, M.B.1    Pagan, J.2    Parsonage, D.3    Hatch, L.4    Senior, A.E.5
  • 22
    • 0000240031 scopus 로고    scopus 로고
    • The Escherichia coli ATP synthase a subunit Arg-376: The catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to steady state
    • Le, N. P., Omote, H., Wada, Y., Al-Shawi, M. K., Nakamoto, R. K., and Futai, M. (2000) The Escherichia coli ATP synthase a subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to steady state, Biochemistry 39, 2778-2783.
    • (2000) Biochemistry , vol.39 , pp. 2778-2783
    • Le, N.P.1    Omote, H.2    Wada, Y.3    Al-Shawi, M.K.4    Nakamoto, R.K.5    Futai, M.6
  • 23
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied
    • 1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied, J. Biol. Chem. 268, 20126-20133.
    • (1993) J. Biol. Chem , vol.268 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.-F.3    Grell, E.4    Senior, A.E.5
  • 25
    • 0020491269 scopus 로고
    • Mechanism of ATP hydrolysis by beef-heart mitochondrial ATPase: Rate constants for elementary steps in catalysis at a single site
    • Grubmeyer, C., Cross, R. L., and Penefsky, H. S. (1982) Mechanism of ATP hydrolysis by beef-heart mitochondrial ATPase: rate constants for elementary steps in catalysis at a single site, J. Biol. Chem. 257, 12092-12100.
    • (1982) J. Biol. Chem , vol.257 , pp. 12092-12100
    • Grubmeyer, C.1    Cross, R.L.2    Penefsky, H.S.3
  • 26
    • 0020491221 scopus 로고
    • Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase: Rate enhancements resulting from cooperative interactions between multiple catalytic sites
    • Cross, R. L., Grubmeyer, C., and Penefsky, H. S. (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase: rate enhancements resulting from cooperative interactions between multiple catalytic sites, 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
  • 27
    • 0021835794 scopus 로고
    • The defective proton-ATPase of uncD mutations of Escherichia coli: Two mutations which affect the catalytic mechanism
    • Duncan, T. M., and Senior, A. E. (1985) The defective proton-ATPase of uncD mutations of Escherichia coli: two mutations which affect the catalytic mechanism, J. Biol. Chem. 260, 4901-4907.
    • (1985) J. Biol. Chem , vol.260 , pp. 4901-4907
    • Duncan, T.M.1    Senior, A.E.2
  • 30
    • 0026515488 scopus 로고
    • 1-ATPase. Characterization of unisite catalysis at varied pH
    • 1-ATPase. Characterization of unisite catalysis at varied pH, Biochemistry 31, 878-885.
    • (1992) Biochemistry , vol.31 , pp. 878-885
    • Al-Shawi, M.K.1    Senior, A.E.2
  • 31
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the e subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky, D. J., Brusilow, W. S. A., and Simoni, R. D. (1984) In vivo evidence for the role of the e subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli, J. Bacteriol. 160, 1055-1060.
    • (1984) J. Bacteriol , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.A.2    Simoni, R.D.3
  • 37
    • 0017063935 scopus 로고
    • A chemical quenching apparatus for studying rapid reactions
    • Froehlich, J. P., Sullivan, J. V., and Berger, R. L. (1976) A chemical quenching apparatus for studying rapid reactions, Anal. Biochem. 73, 331-341.
    • (1976) Anal. Biochem , vol.73 , pp. 331-341
    • Froehlich, J.P.1    Sullivan, J.V.2    Berger, R.L.3
  • 38
    • 0001615790 scopus 로고
    • The specific precipitation of orthophosphate and some biochemical applications
    • Sugino, Y., and Miyoshi, Y. (1964) The specific precipitation of orthophosphate and some biochemical applications, J. Biol. Chem. 239, 2360-2364.
    • (1964) J. Biol. Chem , vol.239 , pp. 2360-2364
    • Sugino, Y.1    Miyoshi, Y.2
  • 39
    • 0023685584 scopus 로고
    • r 1-92 alleles of the Oli-2 region of the yeast Saccharomyces cerevisiae. Analysis of related amino acid substitutions and protein antibiotic interaction
    • r 1-92 alleles of the Oli-2 region of the yeast Saccharomyces cerevisiae. Analysis of related amino acid substitutions and protein antibiotic interaction, Biochim. Biophys. Acta 951, 213-219.
    • (1988) Biochim. Biophys. Acta , vol.951 , pp. 213-219
    • Ray, M.K.1    Connerton, I.F.2    Griffiths, D.E.3
  • 40
    • 0018743553 scopus 로고
    • The use of linear models and matrix least squares in clinical chemistry
    • Deming, S. N., and Morgan, S. L. (1979) The use of linear models and matrix least squares in clinical chemistry, Clin. Chem. 25, 840-855.
    • (1979) Clin. Chem , vol.25 , pp. 840-855
    • Deming, S.N.1    Morgan, S.L.2
  • 42
    • 34547645341 scopus 로고    scopus 로고
    • MicroMath Research (1995) MicroMath Scientist: for Experimental Data Fitting/Microsoft Windows, Version 2.0, MicroMath Research, St. Louis, MO
    • MicroMath Research (1995) MicroMath Scientist: for Experimental Data Fitting/Microsoft Windows, Version 2.0, MicroMath Research, St. Louis, MO.
  • 43
    • 0016355478 scopus 로고
    • A new look at the statistical model identification
    • Akaike, H. (1974) A new look at the statistical model identification, IEEE Trans. Autom. Control 19, 716-723.
    • (1974) IEEE Trans. Autom. Control , vol.19 , pp. 716-723
    • Akaike, H.1
  • 44
    • 0002357422 scopus 로고
    • What is Akaike information criterion
    • Akaike, H. (1976) What is Akaike information criterion, Math. Sci. (Tokyo) 14, 5-11.
    • (1976) Math. Sci. (Tokyo) , vol.14 , pp. 5-11
    • Akaike, H.1
  • 45
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A., and Fabiato, F. (1979) Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells, J. Physiol. (Paris) 75, 463-505.
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 46
    • 0024297454 scopus 로고
    • Directed mutagenesis of the strongly conserved aspartate 242 in the β-Subunit of Escherichia coli proton-ATPase
    • Al-Shawi, M. K., Parsonage, D., and Senior, A. E. (1988) Directed mutagenesis of the strongly conserved aspartate 242 in the β-Subunit of Escherichia coli proton-ATPase, J. Biol. Chem. 263, 19633-19639.
    • (1988) J. Biol. Chem , vol.263 , pp. 19633-19639
    • Al-Shawi, M.K.1    Parsonage, D.2    Senior, A.E.3
  • 48
    • 0020490899 scopus 로고
    • 1-ATPase: Specificity of cooperative interactions
    • 1-ATPase: specificity of cooperative interactions, J. Biol. Chem. 257, 8055-8060.
    • (1982) J. Biol. Chem , vol.257 , pp. 8055-8060
    • Nalin, C.M.1    Cross, R.L.2
  • 49
    • 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
  • 56
    • 0030680983 scopus 로고    scopus 로고
    • 1-ATP synthase: The uncoupling mutation, γM23K, disrupts the use of binding energy to drive catalysis
    • 1-ATP synthase: the uncoupling mutation, γM23K, disrupts the use of binding energy to drive catalysis, Biochemistry 36, 12954-12960.
    • (1997) Biochemistry , vol.36 , pp. 12954-12960
    • Al-Shawi, M.K.1    Nakamoto, R.K.2
  • 57
    • 0000691153 scopus 로고
    • A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions
    • Boyer, P., Cross, R. L., and Momsen, W. (1973) A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions, Proc. Natl. Acad. Sci. U.S.A. 70, 2837-2839.
    • (1973) Proc. Natl. Acad. Sci. U.S.A , vol.70 , pp. 2837-2839
    • Boyer, P.1    Cross, R.L.2    Momsen, W.3
  • 58
    • 0030612021 scopus 로고    scopus 로고
    • 0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway
    • 0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway, Biochemistry 36, 12961-12969.
    • (1997) Biochemistry , vol.36 , pp. 12961-12969
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 61
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps, Cell 93, 1117-1124.
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita, K.3    Yoshida, M.4
  • 65
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implication for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implication for the mechanism of rotary catalysis, Cell 106, 331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.W.3
  • 66
    • 0016853664 scopus 로고
    • A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport
    • Boyer, P. D. (1975) A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport, FEBS Lett. 58, 1-6.
    • (1975) FEBS Lett , vol.58 , pp. 1-6
    • Boyer, P.D.1
  • 67
    • 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
  • 70
    • 0034622430 scopus 로고    scopus 로고
    • 1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously
    • 1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously, Biochemistry 39, 9583-9590.
    • (2000) Biochemistry , vol.39 , pp. 9583-9590
    • Nadanaciva, S.1    Weber, J.2    Senior, A.E.3
  • 71
    • 0029744684 scopus 로고    scopus 로고
    • 1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis
    • 1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis, J. Biol. Chem. 271, 18711-18718.
    • (1996) J. Biol. Chem , vol.271 , pp. 18711-18718
    • Weber, J.1    Bowman, C.2    Senior, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.