메뉴 건너뛰기




Volumn 1797, Issue 4, 2010, Pages 435-442

Stimulation of F1-ATPase activity by sodium dodecyl sulfate

Author keywords

ATP hydrolysis; ATP synthase; Detergent; Optical microscopy; Single molecule; Torque

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DODECYL SULFATE SODIUM; GLASS; POLYSTYRENE;

EID: 76849086411     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.12.018     Document Type: Article
Times cited : (2)

References (28)
  • 1
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase-some probabilities and possibilities
    • Boyer P.D. The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim. Biophys. Acta 1993, 1140:215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 3
    • 3042640723 scopus 로고    scopus 로고
    • Rotation of F1-ATPase: how an ATP-driven molecular machine may work
    • Kinosita K., Adachi K., Itoh H. Rotation of F1-ATPase: how an ATP-driven molecular machine may work. Annu. Rev. Biophys. Biomol. Struct. 2004, 33:245-268.
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 245-268
    • Kinosita, K.1    Adachi, K.2    Itoh, H.3
  • 5
    • 0002888351 scopus 로고
    • The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts
    • Elsevier, Amsterdam, The Netherlands, B.R. Selman, S. Selman-Reimer (Eds.)
    • Boyer P.D., Kohlbrenner W.E. The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts. Energy Coupling in Photosynthesis 1981, 231-240. Elsevier, Amsterdam, The Netherlands. B.R. Selman, S. Selman-Reimer (Eds.).
    • (1981) Energy Coupling in Photosynthesis , pp. 231-240
    • Boyer, P.D.1    Kohlbrenner, W.E.2
  • 6
    • 0022824129 scopus 로고
    • The loose coupling mechanism in molecular machines of living cells
    • Oosawa F., Hayashi S. The loose coupling mechanism in molecular machines of living cells. Adv. Biophys. 1986, 22:151-183.
    • (1986) Adv. Biophys. , vol.22 , pp. 151-183
    • Oosawa, F.1    Hayashi, S.2
  • 7
    • 0028114231 scopus 로고
    • Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E. Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria. Nature 1994, 370:621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 8
    • 0035912221 scopus 로고    scopus 로고
    • Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
    • Yasuda R., Noji H., Yoshida M., Kinosita K., Itoh H. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 2001, 410:898-904.
    • (2001) Nature , vol.410 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita, K.4    Itoh, H.5
  • 9
    • 0345166868 scopus 로고    scopus 로고
    • Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1ms before 40° substep rotation
    • Shimabukuro K., Yasuda R., Muneyuki E., Hara K.Y., Kinosita K., Yoshida M. Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1ms before 40° substep rotation. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:14731-14736.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14731-14736
    • Shimabukuro, K.1    Yasuda, R.2    Muneyuki, E.3    Hara, K.Y.4    Kinosita, K.5    Yoshida, M.6
  • 10
    • 0742270602 scopus 로고    scopus 로고
    • Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation
    • Nishizaka T., Oiwa K., Noji H., Kimura S., Muneyuki E., Yoshida M., Kinosita K. Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. Nat. Struct. Mol. Biol. 2004, 11:142-148.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 142-148
    • Nishizaka, T.1    Oiwa, K.2    Noji, H.3    Kimura, S.4    Muneyuki, E.5    Yoshida, M.6    Kinosita, K.7
  • 11
    • 34447628890 scopus 로고    scopus 로고
    • Coupling of rotation and catalysis in F1-ATPase revealed by single molecule imaging and manipulation
    • Adachi K., Oiwa K., Nishizaka T., Furuike S., Noji H., Itoh H., Yoshida M., Kinosita K. Coupling of rotation and catalysis in F1-ATPase revealed by single molecule imaging and manipulation. Cell 2007, 130:309-321.
    • (2007) Cell , vol.130 , pp. 309-321
    • Adachi, K.1    Oiwa, K.2    Nishizaka, T.3    Furuike, S.4    Noji, H.5    Itoh, H.6    Yoshida, M.7    Kinosita, K.8
  • 14
    • 0028770892 scopus 로고
    • Inhibition and inactivation of the F1 adenosinetriphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide
    • Paik S.R., Jault J.-M., Allison W.S. Inhibition and inactivation of the F1 adenosinetriphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide. Biochemistry 1994, 33:126-133.
    • (1994) Biochemistry , vol.33 , pp. 126-133
    • Paik, S.R.1    Jault, J.-M.2    Allison, W.S.3
  • 16
    • 0029658807 scopus 로고    scopus 로고
    • The α3Β3γ subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 with the ΒT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover
    • Jault J.-M., Dou C., Grodsky N.B., Matsui T., Yoshida M., Allison W.S. The α3Β3γ subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 with the ΒT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover. J. Biol. Chem. 1996, 271:28818-28824.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28818-28824
    • Jault, J.-M.1    Dou, C.2    Grodsky, N.B.3    Matsui, T.4    Yoshida, M.5    Allison, W.S.6
  • 17
    • 40949158758 scopus 로고    scopus 로고
    • Inhibition of the ATPase activity of the catalytic portion of ATP synthases by cationic amphiphiles
    • Datiles M.J., Johnson E.A., McCarty R.E. Inhibition of the ATPase activity of the catalytic portion of ATP synthases by cationic amphiphiles. Biochim. Biophys. Acta 2008, 1777:362-368.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 362-368
    • Datiles, M.J.1    Johnson, E.A.2    McCarty, R.E.3
  • 18
    • 0036087790 scopus 로고    scopus 로고
    • Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus α-amylases in a diluted anionic surfactant solution
    • Tanaka A., Hoshino E. Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus α-amylases in a diluted anionic surfactant solution. J. Biosci. Bioeng. 2002, 93:485-490.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 485-490
    • Tanaka, A.1    Hoshino, E.2
  • 19
    • 0029086522 scopus 로고
    • Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver
    • Shibatani T., Ward W.F. Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver. Arch. Biochem. Biophys. 1995, 321:160-166.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 160-166
    • Shibatani, T.1    Ward, W.F.2
  • 20
    • 13444278724 scopus 로고    scopus 로고
    • Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents
    • Mogensen J.E., Sehgal P., Otzen D.E. Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents. Biochemistry 2005, 44:1719-1730.
    • (2005) Biochemistry , vol.44 , pp. 1719-1730
    • Mogensen, J.E.1    Sehgal, P.2    Otzen, D.E.3
  • 21
    • 0037287424 scopus 로고    scopus 로고
    • Single molecule imaging of the rotation of F1-ATPase
    • Adachi K., Noji H., Kinosita K. Single molecule imaging of the rotation of F1-ATPase. Methods Enzymol. 2003, 361B:211-227.
    • (2003) Methods Enzymol. , vol.361 B , pp. 211-227
    • Adachi, K.1    Noji, H.2    Kinosita, K.3
  • 24
    • 0030610006 scopus 로고    scopus 로고
    • Catalytic activity of the α3Β3γ complex of F1-ATPase without noncatalytic nucleotide binding site
    • Matsui T., Muneyuki E., Honda M., Allison W.S., Dou C., Yoshida M. Catalytic activity of the α3Β3γ complex of F1-ATPase without noncatalytic nucleotide binding site. J. Biol. Chem. 1997, 272:8215-8221.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8215-8221
    • Matsui, T.1    Muneyuki, E.2    Honda, M.3    Allison, W.S.4    Dou, C.5    Yoshida, M.6
  • 26
    • 0027468973 scopus 로고
    • Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial Fl-ATPase
    • Jault J.-M., Allison W.S. Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial Fl-ATPase. J. Biol. Chem. 1993, 268:1558-1566.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1558-1566
    • Jault, J.-M.1    Allison, W.S.2
  • 27
    • 33751155438 scopus 로고
    • Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system
    • Turro N.J., Lei X.-G., Ananthapadmanabhan K.P., Aronson M. Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system. Langmuir 1995, 11:2525-2533.
    • (1995) Langmuir , vol.11 , pp. 2525-2533
    • Turro, N.J.1    Lei, X.-G.2    Ananthapadmanabhan, K.P.3    Aronson, M.4
  • 28
    • 38349193122 scopus 로고    scopus 로고
    • Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes
    • York J., Spetzler D., Hornung T., Ishmukhametov R., Martin J., Frasch W.D. Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes. J. Bioenerg. Biomembr. 2007, 39:435-439.
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 435-439
    • York, J.1    Spetzler, D.2    Hornung, T.3    Ishmukhametov, R.4    Martin, J.5    Frasch, W.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.