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Volumn 287, Issue 27, 2012, Pages 22771-22780

Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATpase

Author keywords

[No Author keywords available]

Indexed keywords

ATP SYNTHASE; CARBOXYL-TERMINAL; CATALYTIC CYCLES; CATALYTIC RATES; DURATION TIME; RATE LIMITING; RATE-LIMITING STEPS; ROTATIONAL CATALYSIS; ROTOR-STATOR INTERACTIONS; SINGLE MOLECULE; TEMPERATURE DEPENDENCE;

EID: 84863331366     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.374868     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase: A splendid molecular machine
    • Boyer, P. D. (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
  • 4
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • DOI 10.1016/S0014-5793(03)01101-3
    • Fillingame, R. H., Angevine, C. M., and Dmitriev, O. Y. (2003) Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 555, 29-34 (Pubitemid 37431092)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 7
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K. (1997) Direct observation of the rotation of F1-ATPase. Nature 386, 299-302
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 14
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A. G., and Walker, J. E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705 (Pubitemid 129515869)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 15
    • 34547626611 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1021/bi700610m
    • Scanlon, J. A., Al-Shawi, M. K., Le, N. P., and Nakamoto, R. K. (2007) Determination of the partial reactions of rotational catalysis in F1-ATPase. Biochemistry 46, 8785-8797 (Pubitemid 47204444)
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8785-8797
    • Baylis, S.J.A.1    Al-Shawi, M.K.2    Nga, P.L.3    Nakamoto, R.K.4
  • 18
    • 0035912221 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1038/35073513
    • Yasuda, R., Noji, H., Yoshida, M., Kinosita, K., Jr., and Itoh, H. (2001) Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 410, 898-904 (Pubitemid 32335828)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita Jr., K.4    Itoh, H.5
  • 19
    • 69249148218 scopus 로고    scopus 로고
    • Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of γ-βsubunit interactions in the catalytic dwell
    • Sekiya, M., Nakamoto, R. K., Al-Shawi, M. K., Nakanishi-Matsui, M., and Futai, M. (2009) Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of γ-βsubunit interactions in the catalytic dwell. J. Biol. Chem. 284, 22401-22410
    • (2009) J. Biol. Chem. , vol.284 , pp. 22401-22410
    • Sekiya, M.1    Nakamoto, R.K.2    Al-Shawi, M.K.3    Nakanishi-Matsui, M.4    Futai, M.5
  • 20
    • 0030612021 scopus 로고    scopus 로고
    • i: Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway
    • i: 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
  • 21
    • 0033922250 scopus 로고    scopus 로고
    • Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals
    • Zheng, J., and Ramirez, V. D. (2000) Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals. Br. J. Pharmacol. 130, 1115-1123 (Pubitemid 30453547)
    • (2000) British Journal of Pharmacology , vol.130 , Issue.5 , pp. 1115-1123
    • Zheng, J.1    Ramirez, V.D.2
  • 25
    • 65549128343 scopus 로고    scopus 로고
    • Inhibition of ATPase activity of Escherichia coli ATP synthase by polyphenols
    • Dadi, P. K., Ahmad, M., and Ahmad, Z. (2009) Inhibition of ATPase activity of Escherichia coli ATP synthase by polyphenols. Int. J. Biol. Macromol. 45, 72-79
    • (2009) Int. J. Biol. Macromol. , vol.45 , pp. 72-79
    • Dadi, P.K.1    Ahmad, M.2    Ahmad, Z.3
  • 26
    • 79958858245 scopus 로고    scopus 로고
    • 1) from Escherichia coli in an autoinhibited conformation
    • 1) from Escherichia coli in an autoinhibited conformation. Nat. Struct. Mol. Biol. 18, 701-707
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2
  • 27
    • 0025233785 scopus 로고
    • +-ATPase γsubunit of Escherichia coli: Role of the conserved carboxyl-terminal region
    • +-ATPase γsubunit of Escherichia coli: role of the conserved carboxyl-terminal region. J. Biol. Chem. 265, 5043-5048
    • (1990) J. Biol. Chem. , vol.265 , pp. 5043-5048
    • Iwamoto, A.1    Miki, J.2    Maeda, M.3    Futai, M.4
  • 28
    • 0028981359 scopus 로고
    • +-ATPase (ATP synthase):β subunit amino acid replacements suppress a γ subunit mutation having a long unrelated carboxyl terminus
    • +-ATPase (ATP synthase):β subunit amino acid replacements suppress a γ subunit mutation having a long unrelated carboxyl terminus. J. Biol. Chem. 270, 22850-22854
    • (1995) J. Biol. Chem. , vol.270 , pp. 22850-22854
    • Jeanteur-De Beukelaer, C.1    Omote, H.2    Iwamoto-Kihara, A.3    Maeda, M.4    Futai, M.5
  • 29
    • 0026612451 scopus 로고
    • 1-ATPase γsubunit mutations perturb the coupling between catalysis and transport
    • 1-ATPase γsubunit mutations perturb the coupling between catalysis and transport. J. Biol. Chem. 267, 20835-20839
    • (1992) J. Biol. Chem. , vol.267 , pp. 20835-20839
    • Shin, K.1    Nakamoto, R.K.2    Maeda, M.3    Futai, M.4
  • 30
    • 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→233Lys. J. Biol. Chem. 268, 867-872 (Pubitemid 23019715)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 867-872
    • Nakamoto, R.K.1    Maeda, M.2    Futai, M.3
  • 31
    • 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
  • 32
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.