메뉴 건너뛰기




Volumn 85, Issue 4, 2003, Pages 2253-2266

On the mechanism of ATP hydrolysis in F1-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; WATER;

EID: 0141642135     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74650-5     Document Type: Article
Times cited : (125)

References (69)
  • 4
    • 0032577020 scopus 로고    scopus 로고
    • Walden-inversion-enforced transition-state stabilization in a protein tyrosine phosphatase
    • Alhambra, C., L. Wu, Z. Zhang, and J. Gao. 1998. Walden-inversion-enforced transition-state stabilization in a protein tyrosine phosphatase. J. Am. Chem. Soc. 120:3858-3866.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3858-3866
    • Alhambra, C.1    Wu, L.2    Zhang, Z.3    Gao, J.4
  • 5
    • 0028356171 scopus 로고
    • 1-ATPase β-subunit probed by introducing different carboxylate-containing side chains
    • 1-ATPase β-subunit probed by introducing different carboxylate-containing side chains. FEBS Lett. 348:93-98.
    • (1994) FEBS Lett. , vol.348 , pp. 93-98
    • Amano, T.1    Tozawa, K.2    Yoshida, M.3    Murakami, H.4
  • 6
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential-based method using charge restraints for deriving atomic charges: The RESP model
    • Baily, C., P. Cieplak, W. Cornell, and P. Kollman. 1993. A well-behaved electrostatic potential-based method using charge restraints for deriving atomic charges: The RESP model. J. Phys. Chem. 97:10269-10280.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Baily, C.1    Cieplak, P.2    Cornell, W.3    Kollman, P.4
  • 7
    • 0345713551 scopus 로고    scopus 로고
    • Hybrid models for combined quantum mechanical and molecular mechanical approaches
    • Bakowies, D., and W. Thiel. 1996. Hybrid models for combined quantum mechanical and molecular mechanical approaches. J. Phys. Chem. 100:10580-10594.
    • (1996) J. Phys. Chem. , vol.100 , pp. 10580-10594
    • Bakowies, D.1    Thiel, W.2
  • 8
    • 0025743628 scopus 로고
    • Computer simulation and analysis of the reaction pathway of triosephosphate isomerase
    • Bash, P., J. Field, R. Davenport, G. Petsko, D. Ringe, and M. Karplus. 1991. Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry. 30:5826-5832.
    • (1991) Biochemistry , vol.30 , pp. 5826-5832
    • Bash, P.1    Field, J.2    Davenport, R.3    Petsko, G.4    Ringe, D.5    Karplus, M.6
  • 10
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase: Some probabilities and possibilities
    • Boyer, P. 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.1
  • 11
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P. 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.1
  • 12
    • 0034737943 scopus 로고    scopus 로고
    • Catalytic site forms and controls in ATP synthase catalysis
    • Boyer, P. 2000. Catalytic site forms and controls in ATP synthase catalysis. Biochim. Biophys. Acta. 1458:252-262.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 252-262
    • Boyer, P.1
  • 15
    • 0037051671 scopus 로고    scopus 로고
    • Enzymatic GTP hydrolysis: Insights from an ab initio molecular dynamics study
    • Cavalli, A., and P. Carloni. 2001. Enzymatic GTP hydrolysis: insights from an ab initio molecular dynamics study. J. Am. Chem. Soc. 124:3763-3768.
    • (2001) J. Am. Chem. Soc. , vol.124 , pp. 3763-3768
    • Cavalli, A.1    Carloni, P.2
  • 16
    • 0037174379 scopus 로고    scopus 로고
    • Environmental effects on phosphoryl group bonding probed by vibrational spectroscopy: Implications for understanding phosphoryl transfer and enzymatic catalysis
    • Cheng, H., I. Nikolic-Hughes, J. Wang, H. Deng, P. O'Brien, L. Wu, Z. Zhang, D. Herschlag, and R. Callender. 2002. Environmental effects on phosphoryl group bonding probed by vibrational spectroscopy: implications for understanding phosphoryl transfer and enzymatic catalysis. J. Am. Chem. Soc. 124:11295-11306.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11295-11306
    • Cheng, H.1    Nikolic-Hughes, I.2    Wang, J.3    Deng, H.4    O'Brien, P.5    Wu, L.6    Zhang, Z.7    Herschlag, D.8    Callender, R.9
  • 18
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle Mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 20
    • 84986513644 scopus 로고
    • A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations
    • Field, M., P. Bash, and M. Karplus. 1990. A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations. J. Comp. Chem. 11:700-733.
    • (1990) J. Comp. Chem. , vol.11 , pp. 700-733
    • Field, M.1    Bash, P.2    Karplus, M.3
  • 21
    • 0002687757 scopus 로고
    • Phosphorus compounds of muscle and liver
    • Fiske, C., and Y. Subbarow. 1929. Phosphorus compounds of muscle and liver. Science. 70:381-382.
    • (1929) Science , vol.70 , pp. 381-382
    • Fiske, C.1    Subbarow, Y.2
  • 22
    • 0030858487 scopus 로고    scopus 로고
    • A fundamental assumption about OH-attack in phosphate ester hydrolysis is not fully justified
    • Florián, J., and A. Warshel. 1997. A fundamental assumption about OH-attack in phosphate ester hydrolysis is not fully justified. J. Am. Chem. Soc. 119:5473-5474.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5473-5474
    • Florián, J.1    Warshel, A.2
  • 23
    • 0031646592 scopus 로고    scopus 로고
    • Phosphate ester hydrolysis in aqueous solution: Associative versus dissociative mechanisms
    • Florián, J., and A. Warshel. 1998. Phosphate ester hydrolysis in aqueous solution: associative versus dissociative mechanisms. J. Phys. Chem. B. 102:719-734.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 719-734
    • Florián, J.1    Warshel, A.2
  • 24
    • 0032796313 scopus 로고    scopus 로고
    • Ab initio study of the role of lysine 16 for the molecular switching mechanism of Ras protein p21
    • Futatsugi, N., H. Masayuki, T. Hoshino, and M. Tsuda. 1999. Ab initio study of the role of lysine 16 for the molecular switching mechanism of Ras protein p21. Biophys. J. 77:3287-3292.
    • (1999) Biophys. J. , vol.77 , pp. 3287-3292
    • Futatsugi, N.1    Masayuki, H.2    Hoshino, T.3    Tsuda, M.4
  • 26
    • 0034663856 scopus 로고    scopus 로고
    • How does GAP catalyze the GTPase reaction of Ras? A computer simulation study
    • Glennon, T., J. Villá, and A. Warshel. 2000. How does GAP catalyze the GTPase reaction of Ras? A computer simulation study. Biochemistry. 39:9641-9651.
    • (2000) Biochemistry , vol.39 , pp. 9641-9651
    • Glennon, T.1    Villá, J.2    Warshel, A.3
  • 27
    • 26744445949 scopus 로고
    • Dynamic force field models: Molecular dynamics simulations of human carbonic anhydrase II using a quantum mechanical/molecular mechanical coupled potential
    • Hartsough, D., and K. Merz, Jr. 1995. Dynamic force field models: molecular dynamics simulations of human carbonic anhydrase II using a quantum mechanical/molecular mechanical coupled potential. J. Phys. Chem. 99:11266-11275.
    • (1995) J. Phys. Chem. , vol.99 , pp. 11266-11275
    • Hartsough, D.1    Merz K., Jr.2
  • 28
    • 0034321020 scopus 로고    scopus 로고
    • Proton transfer in bacteriorhodopsin: Structure, excitation, IR spectra, and potential energy surface analysis by an ab initio QM/MM method
    • Hayashi, S., and I. Ohmine. 2000. Proton transfer in bacteriorhodopsin: structure, excitation, IR spectra, and potential energy surface analysis by an ab initio QM/MM method. J. Phys. Chem. B. 104:10678-10691.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10678-10691
    • Hayashi, S.1    Ohmine, I.2
  • 30
  • 33
    • 0034728898 scopus 로고    scopus 로고
    • A rotary molecular motor that can work at near 100% efficiency
    • Kinosita, K. J., R. Yasuda, and H. Noji. 2000. A rotary molecular motor that can work at near 100% efficiency. Phil. Trans. R. Soc. Lond. B. 355:473-489.
    • (2000) Phil. Trans. R. Soc. Lond. B , vol.355 , pp. 473-489
    • Kinosita, K.J.1    Yasuda, R.2    Noji, H.3
  • 34
    • 0026713142 scopus 로고
    • On the mechanism of guanosine triphosphate hydrolysis in ras p21 proteins
    • Langen, R., T. Schweins, and A. Warshel. 1992. On the mechanism of guanosine triphosphate hydrolysis in ras p21 proteins. Biochemistry. 31:8691-8696.
    • (1992) Biochemistry , vol.31 , pp. 8691-8696
    • Langen, R.1    Schweins, T.2    Warshel, A.3
  • 35
    • 12444259580 scopus 로고    scopus 로고
    • Computer simulation of biochemical reactions with QM/MM methods
    • O. Becker, A. MacKerell Jr., B. Roux, and M. Watanabe, editors. Marcel Dekker Inc., New York
    • Lyne, D., and O. Walsh. 2001. Computer simulation of biochemical reactions with QM/MM methods. In Computational Biochemistry and Biophysics. O. Becker, A. MacKerell Jr., B. Roux, and M. Watanabe, editors. Marcel Dekker Inc., New York. pp.221-235.
    • (2001) Computational Biochemistry and Biophysics , pp. 221-235
    • Lyne, D.1    Walsh, O.2
  • 36
    • 0000218385 scopus 로고    scopus 로고
    • Hybrid models for combined quantum mechanical and molecular mechanical approaches
    • Lyne, P., M. Hodoseck, and M. Karplus. 1999. Hybrid models for combined quantum mechanical and molecular mechanical approaches. J. Phys. Chem. A. 103:3462-3471.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 3462-3471
    • Lyne, P.1    Hodoseck, M.2    Karplus, M.3
  • 38
    • 84986527758 scopus 로고
    • IMOMM: A new integrated ab initio + molecular mechanics geometry optimization scheme of equilibrium structures and transition states
    • Maseras, F., and K. Morokuma. 1995. IMOMM: a new integrated ab initio + molecular mechanics geometry optimization scheme of equilibrium structures and transition states. J. Comp. Chem. 16:1170-1179.
    • (1995) J. Comp. Chem. , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 39
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanisms of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanisms of rotary catalysis. Cell. 106:331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.1    Walker, J.2    Leslie, A.3
  • 40
    • 0034716340 scopus 로고    scopus 로고
    • Ab initio QM/MM study of the citrate synthase mechanism. A low-barrier hydrogen bond is not involved
    • Mulholland, A., P. Lyne, and M. Karplus. 2000. Ab initio QM/MM study of the citrate synthase mechanism. A low-barrier hydrogen bond is not involved. J. Am. Chem. Soc. 122:534-535.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 534-535
    • Mulholland, A.1    Lyne, P.2    Karplus, M.3
  • 41
    • 0037188741 scopus 로고    scopus 로고
    • 1-ATPase, the C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation
    • 1-ATPase, the C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation. J. Biol. Chem. 277:23308-23313.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23308-23313
    • Müller, M.1    Pänke, O.2    Junge, W.3    Engelbrecht, S.4
  • 45
    • 0029040551 scopus 로고
    • The ATP synthase γ-subunit
    • Nakamoto, R., and M. Al-Shawi. 1995. The ATP synthase γ-subunit. J. Biol. Chem. 270:14042-14046.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14042-14046
    • Nakamoto, R.1    Al-Shawi, M.2
  • 46
    • 0027471965 scopus 로고
    • The γ-subunit of the Escherichia coli ATP synthase
    • Nakamoto, R., M. Maeda, and M. Futai. 1993. The γ-subunit of the Escherichia coli ATP synthase. J. Biol. Chem. 268:867-872.
    • (1993) J. Biol. Chem. , vol.268 , pp. 867-872
    • Nakamoto, R.1    Maeda, M.2    Futai, M.3
  • 50
    • 0036930078 scopus 로고    scopus 로고
    • Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin
    • Saam, J., E. Tajkhorshid, S. Hayashi, and K. Schulten. 2002. Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin. Biophys. J. 83:3097-3112.
    • (2002) Biophys. J. , vol.83 , pp. 3097-3112
    • Saam, J.1    Tajkhorshid, E.2    Hayashi, S.3    Schulten, K.4
  • 52
    • 0028464366 scopus 로고
    • Why have mutagenesis studies not located the general base in ras p21?
    • Schweins, T., R. Langen, and A. Warshel. 1994. Why have mutagenesis studies not located the general base in ras p21? Nat. Struct. Biol. 1:476-484.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 476-484
    • Schweins, T.1    Langen, R.2    Warshel, A.3
  • 55
    • 84988053595 scopus 로고
    • - exchange reaction and gas phase protonation of polyethers
    • - exchange reaction and gas phase protonation of polyethers. J. Comp. Chem. 7:718-730.
    • (1986) J. Comp. Chem. , vol.7 , pp. 718-730
    • Singh, U.1    Kollman, P.2
  • 56
    • 33751156482 scopus 로고
    • An examination of a Hartree-Fock/molecular mechanical coupled potential
    • Stanton, R., L. Little, and K. Merz, Jr. 1995. An examination of a Hartree-Fock/molecular mechanical coupled potential. J. Phys. Chem. 99:17344-17348.
    • (1995) J. Phys. Chem. , vol.99 , pp. 17344-17348
    • Stanton, R.1    Little, L.2    Merz K., Jr.3
  • 58
    • 0041876227 scopus 로고    scopus 로고
    • Computer simulations of enzyme catalysis: Methods, progress and insights
    • Warshel, A. 2003. Computer simulations of enzyme catalysis: methods, progress and insights. Annu. Rev. Biophys. Biomol. Struct. 32:425-434.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 425-434
    • Warshel, A.1
  • 59
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel, A., and M. Levitt. 1976. Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103:227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 62
    • 0034737965 scopus 로고    scopus 로고
    • ATP synthase: What we know about ATP hydrolysis and what we do not know about ATP synthesis
    • Weber, J., S. Nadanaciva. and A. Senior. 2000b. ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. Biochim. Biophys. Acta. 1458:300-309.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 300-309
    • Weber, J.1    Nadanaciva, S.2    Senior, A.3
  • 65
    • 0028860486 scopus 로고
    • Mutagenesis and reversion analysis of residue MET-209 of the β-subunit of Escherichia coli ATP synthase
    • Wilke-Mounts, S., J. Pagan, and A. Senior. 1995. Mutagenesis and reversion analysis of residue MET-209 of the β-subunit of Escherichia coli ATP synthase. Arch. Biochem. Biophys. 324:153-158.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 153-158
    • Wilke-Mounts, S.1    Pagan, J.2    Senior, A.3
  • 66
    • 0021771669 scopus 로고
    • a mutants of Escherichia coli. 5′-adenylyl imidodiphosphate binding and ATP hydrolysis
    • a mutants of Escherichia coli. 5′-adenylyl imidodiphosphate binding and ATP hydrolysis. Biochemistry. 23:1426-1432.
    • (1984) Biochemistry , vol.23 , pp. 1426-1432
    • Wise, J.1    Latchney, L.2    Ferguson, A.3    Senior, A.4
  • 69
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang, L., and J. Hermans. 1996. Hydrophilicity of cavities in proteins. Pror. Struct. Funct. Gen. 24:433-438.
    • (1996) Pror. Struct. Funct. Gen. , vol.24 , pp. 433-438
    • Zhang, L.1    Hermans, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.