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Volumn 1807, Issue 9, 2011, Pages 1083-1094

Proton-transport mechanisms in cytochrome c oxidase revealed by studies of kinetic isotope effects

Author keywords

Cytochrome aa3; Electron transfer; Electrostatics; Energy transduction; Membrane protein; Respiration

Indexed keywords

CYTOCHROME C OXIDASE; ISOTOPE; OXYGEN; PROTON PUMP;

EID: 79960566156     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.03.012     Document Type: Article
Times cited : (33)

References (88)
  • 1
    • 36148938761 scopus 로고    scopus 로고
    • Molecular mechanism of proton translocation by cytochrome c oxidase
    • DOI 10.1089/ars.2007.1705
    • I. Belevich, and M.I. Verkhovsky Molecular mechanism of proton translocation by cytochrome c oxidase Antioxid. Redox Signal. 10 2008 1 29 (Pubitemid 350115984)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.1 , pp. 1-29
    • Belevich, I.1    Verkhovsky, M.I.2
  • 2
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • d505-999
    • R.B. Gennis Coupled proton and electron transfer reactions in cytochrome oxidase Front. Biosci. 9 2004 581 591 (Pubitemid 39043736)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 3
    • 57049180108 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Exciting progress and remaining mysteries
    • P. Brzezinski, and R.B. Gennis Cytochrome c oxidase: exciting progress and remaining mysteries J. Bioenerg. Biomembr. 40 2008 521 531
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 521-531
    • Brzezinski, P.1    Gennis, R.B.2
  • 4
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2006.05.020, PII S0005272806001472
    • G. Brändén, R.B. Gennis, and P. Brzezinski Transmembrane proton translocation by cytochrome c oxidase Biochim. Biophys. Acta 1757 2006 1052 1063 (Pubitemid 44467836)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1052-1063
    • Branden, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 5
    • 33746601087 scopus 로고    scopus 로고
    • Design principles of proton-pumping haem-copper oxidases
    • DOI 10.1016/j.sbi.2006.06.012, PII S0959440X06001163
    • P. Brzezinski, and P. Ädelroth Design principles of proton-pumping haem-copper oxidases Curr. Opin. Struct. Biol. 16 2006 465 472 (Pubitemid 44149073)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.4 , pp. 465-472
    • Brzezinski, P.1    Adelroth, P.2
  • 6
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • DOI 10.1016/j.bbabio.2007.06.008, PII S0005272807001533
    • M. Wikström, and M.I. Verkhovsky Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases Biochim. Biophys. Acta BBA Bioenerg. 1767 2007 1200 1214 (Pubitemid 47498307)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1200-1214
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 7
    • 33748885262 scopus 로고    scopus 로고
    • Towards the mechanism of proton pumping by the haem-copper oxidases
    • DOI 10.1016/j.bbabio.2006.01.010, PII S0005272806000235
    • M. Wikström, and M.I. Verkhovsky Towards the mechanism of proton pumping by the haem-copper oxidases Biochim. Biophys. Acta Bioenerg. 1757 2006 1047 1051 (Pubitemid 44427754)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1047-1051
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 8
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • DOI 10.1146/annurev.biochem.75.062003.101730
    • J.P. Hosler, S. Ferguson-Miller, and D.A. Mills Energy transduction: proton transfer through the respiratory complexes Annu. Rev. Biochem. 75 2006 165 187 (Pubitemid 44118030)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 9
    • 10444234271 scopus 로고    scopus 로고
    • Cytochrome c oxidase, ligands and electrons
    • DOI 10.1016/j.jinorgbio.2004.10.011, PII S0162013404003162, Heme-Diatomic Interactions, Part 1
    • M. Brunori, A. Giuffre, and P. Sarti Cytochrome c oxidase, ligands and electrons J. Inorg. Biochem. 99 2005 324 336 (Pubitemid 39642985)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 324-336
    • Brunori, M.1    Giuffre, A.2    Sarti, P.3
  • 10
    • 1942536202 scopus 로고    scopus 로고
    • The influence of subunit III of cytochrome c oxidase on the D pathway, the proton exit pathway and mechanism-based inactivation in subunit I
    • DOI 10.1016/j.bbabio.2003.06.009, PII S0005272803002111
    • J.P. Hosler The influence of subunit III of cytochrome c oxidase on the D pathway, the proton exit pathway and mechanism-based inactivation in subunit I Biochim. Biophys. Acta 2004 332 339 (Pubitemid 38526196)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 332-339
    • Hosler, J.P.1
  • 11
    • 33745844057 scopus 로고    scopus 로고
    • Surface proton donors for the D-pathway of cytochrome c oxidase in the absence of subunit III
    • DOI 10.1021/bi0605843
    • P. Ädelroth, and J. Hosler Surface proton donors for the D-pathway of cytochrome c oxidase in the absence of subunit III Biochemistry 45 2006 8308 8318 (Pubitemid 44036537)
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8308-8318
    • Adelroth, P.1    Hosler, J.2
  • 12
    • 33947285426 scopus 로고    scopus 로고
    • Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: A general framework for examining energetics and mechanistic alternatives
    • DOI 10.1016/j.bbabio.2007.01.015, PII S0005272807000199
    • M.H.M. Olsson, P.E.M. Siegbahn, M.R.A. Blomberg, and A. Warshel Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: a general framework for examining energetics and mechanistic alternatives Biochim. Biophys. Acta Bioenerg. 1767 2007 244 260 (Pubitemid 46420433)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.3 , pp. 244-260
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Blomberg, M.R.A.3    Warshel, A.4
  • 13
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 Years of the elusive proton pump
    • DOI 10.1016/j.bbabio.2003.07.013, PII S0005272803002330
    • M. Wikström Cytochrome c oxidase: 25 years of the elusive proton pump Biochim. Biophys. Acta 1655 2004 241 247 (Pubitemid 38526186)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 241-247
    • Wikstrom, M.1
  • 14
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • P.R. Rich Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases Aust. J. Plant Physiol. 22 1995 479 486
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 15
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the heme-copper superfamily in archaea: Insights from genomics and structural modeling
    • J. Hemp, and R.B. Gennis Diversity of the heme-copper superfamily in archaea: insights from genomics and structural modeling Results Probl. Cell Differ. 45 2008 1 31
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 16
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta Bioenerg. 1505 2001 185 208 (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 18
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a
    • DOI 10.1021/bi9924821
    • H.M. Lee, T.K. Das, D.L. Rousseau, D. Mills, S. Ferguson-Miller, and R.B. Gennis Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a Biochemistry 39 2000 2989 2996 (Pubitemid 30159404)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 2989-2996
    • Lee, H.-M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.4    Ferguson-Miller, S.5    Gennis, R.B.6
  • 19
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • A.A. Konstantinov, S. Siletsky, D. Mitchell, A. Kaulen, and R.B. Gennis The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer Proc. Natl. Acad. Sci. U. S. A. 94 1997 9085 9090
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 20
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases
    • DOI 10.1016/S0005-2728(00)00191-2, PII S0005272800001912
    • M. Wikström, A. Jasaitis, C. Backgren, A. Puustinen, and M.I. Verkhovsky The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases Biochim. Biophys. Acta 1459 2000 514 520 (Pubitemid 30612427)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1459 , Issue.2-3 , pp. 514-520
    • Wikstrom, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 21
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochrome c oxidase
    • DOI 10.1023/A:1020567729941
    • P. Brzezinski, and P. Ädelroth Pathways of proton transfer in cytochrome c oxidase J. Bioenerg. Biomembr. 30 1998 99 107 (Pubitemid 28262413)
    • (1998) Journal of Bioenergetics and Biomembranes , vol.30 , Issue.1 , pp. 99-107
    • Brzezinski, P.1    Adelroth, P.2
  • 22
    • 49349116297 scopus 로고    scopus 로고
    • Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme
    • R. Sugitani, E.S. Medvedev, and A.A. Stuchebrukhov Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme Biochim. Biophys. Acta Bioenerg. 1777 2008 1129 1139
    • (2008) Biochim. Biophys. Acta Bioenerg. , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 23
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • P.E.M. Siegbahn, M.R.A. Blomberg, and M.L. Blomberg Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase J. Phys. Chem. B 107 2003 10946 10955
    • (2003) J. Phys. Chem. B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 26
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping-A discussion
    • H. Michel Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping-a discussion Biochemistry 38 1999 15129 15140 (Pubitemid 129520343)
    • (1999) Biochemistry , vol.38 , Issue.46 , pp. 15129-15140
    • Michel, H.1
  • 27
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochrome c oxidase by a second electron leads to proton translocation
    • DOI 10.1038/416099a
    • M. Ruitenberg, A. Kannt, E. Bamberg, K. Fendler, and H. Michel Reduction of cytochrome c oxidase by a second electron leads to proton translocation Nature 417 2002 99 102 (Pubitemid 34498824)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 99-102
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 29
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • DOI 10.1038/nature03921
    • K. Faxén, G. Gilderson, P. Ädelroth, and P. Brzezinski A mechanistic principle for proton pumping by cytochrome c oxidase Nature 437 2005 286 289 (Pubitemid 41294494)
    • (2005) Nature , vol.437 , Issue.7056 , pp. 286-289
    • Faxen, K.1    Gilderson, G.2    Adelroth, P.3    Brzezinski, P.4
  • 30
    • 77953770537 scopus 로고    scopus 로고
    • Variable proton-pumping stoichiometry in structural variants of cytochrome c oxidase
    • P. Brzezinski, and A.L. Johansson Variable proton-pumping stoichiometry in structural variants of cytochrome c oxidase Biochim. Biophys. Acta Bioenerg. 1797 2010 710 723
    • (2010) Biochim. Biophys. Acta Bioenerg. , vol.1797 , pp. 710-723
    • Brzezinski, P.1    Johansson, A.L.2
  • 31
    • 0037452497 scopus 로고    scopus 로고
    • Intramolecular proton-transfer reactions in a membrane-bound proton pump: The effect of pH on the peroxy to ferryl transition in cytochrome c oxidase
    • DOI 10.1021/bi026524o
    • A. Namslauer, A. Aagaard, A. Katsonouri, and P. Brzezinski Intramolecular proton-transfer reactions in a membrane-bound proton pump: the effect of pH on the peroxy to ferryl transition in cytochrome c oxidase Biochemistry 42 2003 1488 1498 (Pubitemid 36205955)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 32
    • 0038408885 scopus 로고    scopus 로고
    • Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH
    • DOI 10.1021/bi0341298
    • G. Gilderson, L. Salomonsson, A. Aagaard, J. Gray, P. Brzezinski, and J. Hosler Subunit III of Cytochrome c Oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH Biochemistry 42 2003 7400 7409 (Pubitemid 36740492)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7400-7409
    • Gilderson, G.1    Salomonsson, L.2    Aagaard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 33
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping
    • DOI 10.1021/bi026582+
    • A.S. Pawate, J. Morgan, A. Namslauer, D. Mills, P. Brzezinski, S. Ferguson-Miller, and R.B. Gennis A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping Biochemistry 41 2002 13417 13423 (Pubitemid 35303901)
    • (2002) Biochemistry , vol.41 , Issue.45 , pp. 13417-13423
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.4    Brzezinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 34
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • DOI 10.1021/bi992235x
    • U. Pfitzner, K. Hoffmeier, A. Harrenga, A. Kannt, H. Michel, E. Bamberg, O.M.H. Richter, and B. Ludwig Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans Biochemistry 39 2000 6756 6762 (Pubitemid 30390366)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 6756-6762
    • Pfitzner, U.1    Hoffmeier, K.2    Harrenga, A.3    Kannt, A.4    Michel, H.5    Bamberg, E.6    Richter, O.-M.H.7    Ludwig, B.8
  • 35
    • 77955127137 scopus 로고    scopus 로고
    • A new model for the origin of kinetic hydrogen isotope effects
    • J.P. Klinman A new model for the origin of kinetic hydrogen isotope effects J. Phys. Org. Chem. 23 2010 606 612
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 606-612
    • Klinman, J.P.1
  • 37
    • 34547456661 scopus 로고    scopus 로고
    • Origin of the temperature dependence of isotope effects in enzymatic reactions: The case of dihydrofolate reductase
    • DOI 10.1021/jp070938f
    • H. Liu, and A. Warshel Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase J. Phys. Chem. B 111 2007 7852 7861 (Pubitemid 47169697)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.27 , pp. 7852-7861
    • Liu, H.1    Warshel, A.2
  • 39
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochrome c oxidase: Catalytic turnover in the absence of subunit III alters the active site
    • M.R. Bratton, M.A. Pressler, and J.P. Hosler Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site Biochemistry 38 1999 16236 16245 (Pubitemid 129520544)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 40
    • 0020346954 scopus 로고
    • Solvent isotope effects on enzyme systems
    • K.B. Schowen, and R.L. Schowen Solvent isotope effects on enzyme systems Methods Enzymol. 87 1982 551 606
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 41
    • 79751528117 scopus 로고    scopus 로고
    • Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects
    • S. Chakrabarty, I. Namslauer, P. Brzezinski, and A. Warshel Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects Biochim. Biophys. Acta Bioenerg. 1807 2011 413 426
    • (2011) Biochim. Biophys. Acta Bioenerg. , vol.1807 , pp. 413-426
    • Chakrabarty, S.1    Namslauer, I.2    Brzezinski, P.3    Warshel, A.4
  • 42
    • 4243810035 scopus 로고
    • Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches
    • J. Åqvist, and A. Warshel Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches Chem. Rev. 93 1993 2523 2544
    • (1993) Chem. Rev. , vol.93 , pp. 2523-2544
    • Åqvist, J.1    Warshel, A.2
  • 43
    • 33751386561 scopus 로고
    • A quantized classical path approach for calculations of quantum mechanical rate constants
    • J.-K. Hwang, and A. Warshel A quantized classical path approach for calculations of quantum mechanical rate constants J. Phys. Chem. 97 1993 10053 10058
    • (1993) J. Phys. Chem. , vol.97 , pp. 10053-10058
    • Hwang, J.-K.1    Warshel, A.2
  • 44
    • 0029951263 scopus 로고    scopus 로고
    • How important are quantum mechanical nuclear motions in enzyme catalysis?
    • DOI 10.1021/ja962007f
    • J.-K. Hwang, and A. Warshel How important are quantum mechanical nuclear motions in enzyme catalysis? J. Am. Chem. Soc. 118 1996 11745 11751 (Pubitemid 26417463)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.47 , pp. 11745-11751
    • Hwang, J.-K.1    Warshel, A.2
  • 45
    • 33750995244 scopus 로고    scopus 로고
    • Hybrid quantum/classical path integral approach for simulation of hydrogen transfer reactions in enzymes
    • Q. Wang, and S. Hammes-Schiffer Hybrid quantum/classical path integral approach for simulation of hydrogen transfer reactions in enzymes J. Chem. Phys. 126 1-11 2006 184102
    • (2006) J. Chem. Phys. , vol.126 , Issue.111 , pp. 184102
    • Wang, Q.1    Hammes-Schiffer, S.2
  • 46
    • 34547853504 scopus 로고    scopus 로고
    • Nuclear quantum effects on an enzyme-catalyzed reaction with reaction path potential: Proton transfer in triosephosphate isomerase
    • M. Wang, Z. Lu, and W. Yang Nuclear quantum effects on an enzyme-catalyzed reaction with reaction path potential: proton transfer in triosephosphate isomerase J. Chem. Phys. 124 1-8 2006 124516
    • (2006) J. Chem. Phys. , vol.124 , Issue.18 , pp. 124516
    • Wang, M.1    Lu, Z.2    Yang, W.3
  • 47
    • 33845569858 scopus 로고    scopus 로고
    • A combined quantum mechanical and molecular mechanical study of the reaction mechanism and α-amino acidity in alanine racemase
    • DOI 10.1021/ja066334r
    • D.T. Major, and J.L. Gao A combined quantum mechanical and molecular mechanical study of the reaction mechanism and α-amino acidity in alanine racemase J. Am. Chem. Soc. 128 2006 16345 16357 (Pubitemid 44936630)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.50 , pp. 16345-16357
    • Major, D.T.1    Gao, J.2
  • 48
    • 0035861065 scopus 로고    scopus 로고
    • Hydride transfer in liver alcohol dehydrogenase: Quantum dynamics, kinetic isotope effects, and role of enzyme motion
    • DOI 10.1021/ja011384b
    • S.R. Billeter, S.P. Webb, P.K. Agarwal, T. Iordanov, and S. Hammes-Schiffer Hydride transfer in liver alcohol dehydrogenase: quantum dynamics, kinetic isotope effects, and role of enzyme motion J. Am. Chem. Soc. 123 2001 11262 11272 (Pubitemid 33065363)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.45 , pp. 11262-11272
    • Billeter, S.R.1    Webb, S.P.2    Agarwal, P.K.3    Iordanov, T.4    Hammes-Schiffer, S.5
  • 49
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: Insight from computer simulations
    • A. Warshel, and W.W. Parson Dynamics of biochemical and biophysical reactions: insight from computer simulations Q. Rev. Biophys. 34 2001 563 670
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 563-670
    • Warshel, A.1    Parson, W.W.2
  • 51
    • 0001053428 scopus 로고
    • Quantum classical crossover of the transition rate in the damped double well
    • M.J. Gillan Quantum classical crossover of the transition rate in the damped double well J. Phys. C Solid State Phys. 20 1987 3621 3641
    • (1987) J. Phys. C Solid State Phys. , vol.20 , pp. 3621-3641
    • Gillan, M.J.1
  • 52
    • 0642311214 scopus 로고    scopus 로고
    • Path-Integral Centroid Methods in Quantum Statistical Mechanics and Dynamics
    • New Methods in Computational Quantum Mechanics
    • G.A. Voth Path-integral centroid methods in quantum statistical mechanics and dynamics Adv. Chem. Phys. 93 1996 135 218 (Pubitemid 126072367)
    • (1996) Advances in Chemical Physics , vol.93 , pp. 135-218
    • Voth, G.A.1
  • 53
    • 0041290286 scopus 로고
    • Rigorous formulation of quantum transition state theory and its dynamical corrections
    • G.A. Voth, D. Chandler, and W.H. Miller Rigorous formulation of quantum transition state theory and its dynamical corrections J. Chem. Phys. 91 1989 7749
    • (1989) J. Chem. Phys. , vol.91 , pp. 7749
    • Voth, G.A.1    Chandler, D.2    Miller, W.H.3
  • 54
    • 0040193886 scopus 로고
    • Simulations of quantum mechanical corrections for rate constants of hydride-transfer reactions in enzymes and solutions
    • J.-K. Hwang, Z.T. Chu, A. Yadav, and A. Warshel Simulations of quantum mechanical corrections for rate constants of hydride-transfer reactions in enzymes and solutions J. Phys. Chem. 95 1991 8445 8448
    • (1991) J. Phys. Chem. , vol.95 , pp. 8445-8448
    • Hwang, J.-K.1    Chu, Z.T.2    Yadav, A.3    Warshel, A.4
  • 55
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • DOI 10.1021/cr040427e
    • M.H.M. Olsson, W.W. Parson, and A. Warshel Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis Chem. Rev. 106 2006 1737 1756 (Pubitemid 43792778)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 56
    • 1542382717 scopus 로고
    • Simulation of the dynamics of electron transfer reactions in polar solvents: Semiclassical trajectories and dispersed polaron approaches
    • A. Warshel, and J.-K. Hwang Simulation of the dynamics of electron transfer reactions in polar solvents: semiclassical trajectories and dispersed polaron approaches J. Chem. Phys. 84 1986 4938 4957
    • (1986) J. Chem. Phys. , vol.84 , pp. 4938-4957
    • Warshel, A.1    Hwang, J.-K.2
  • 57
    • 0041642741 scopus 로고
    • Quantum corrections for rate constants of diabatic and adiabatic reactions in solutions
    • A. Warshel, and Z.T. Chu Quantum corrections for rate constants of diabatic and adiabatic reactions in solutions J. Chem. Phys. 93 1990 4003 4015
    • (1990) J. Chem. Phys. , vol.93 , pp. 4003-4015
    • Warshel, A.1    Chu, Z.T.2
  • 58
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics
    • DOI 10.1046/j.1432-1033.2002.03022.x
    • M.J. Knapp, and J.P. Klinman Environmentally coupled hydrogen tunneling - linking catalysis to dynamics Eur. J. Biochem. 269 2002 3113 3121 (Pubitemid 34748097)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.13 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 60
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis
    • A.M. Kuznetsov, and J. Ulstrup Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis Can. J. Chem. Rev. Canadian De Chimie 77 1999 1085 1096 (Pubitemid 129658853)
    • (1999) Canadian Journal of Chemistry , vol.77 , Issue.5-6 , pp. 1085-1096
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 61
    • 0007836334 scopus 로고
    • Dynamics of reactions in polar solvents. Semiclassical trajectory studies of electron-transfer and proton-transfer reactions
    • A. Warshel Dynamics of reactions in polar solvents. Semiclassical trajectory studies of electron-transfer and proton-transfer reactions J. Phys. Chem. 86 1982 2218 2224
    • (1982) J. Phys. Chem. , vol.86 , pp. 2218-2224
    • Warshel, A.1
  • 62
    • 5544259571 scopus 로고
    • Molecular-dynamics simulation for a model nonadiabatic proton transfer reaction in solution
    • D. Borgis, and J.T. Hynes Molecular-dynamics simulation for a model nonadiabatic proton transfer reaction in solution J. Chem. Phys. 94 1991 3619 3628
    • (1991) J. Chem. Phys. , vol.94 , pp. 3619-3628
    • Borgis, D.1    Hynes, J.T.2
  • 64
    • 50449140483 scopus 로고
    • Computation of the intensities of vibrational spectra of electronic bands in diatomic molecules
    • C. Manneback Computation of the intensities of vibrational spectra of electronic bands in diatomic molecules Physica 17 1951 1001 1010
    • (1951) Physica , vol.17 , pp. 1001-1010
    • Manneback, C.1
  • 65
    • 0017420379 scopus 로고
    • Interpretation of resonance raman spectra of biological molecules
    • A. Warshel Interpretation of resonance raman spectra of biological molecules Annu. Rev. Biophys. Bioeng. 6 1977 273 300
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 273-300
    • Warshel, A.1
  • 66
    • 0032552970 scopus 로고    scopus 로고
    • Single electron reduction of cytochrome c oxidase compound F: Resolution of partial steps by transient spectroscopy
    • DOI 10.1021/bi981490z
    • D. Zaslavsky, R.C. Sadoski, K.F. Wang, B. Durham, R.B. Gennis, and F. Millett Single electron reduction of cytochrome c oxidase compound F: resolution of partial steps by transient spectroscopy Biochemistry 37 1998 14910 14916 (Pubitemid 28487600)
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14910-14916
    • Zaslavsky, D.1    Sadoski, R.C.2    Wang, K.3    Durham, B.4    Gennis, R.B.5    Millett, F.6
  • 67
    • 0034643829 scopus 로고    scopus 로고
    • Localized control of proton transfer through the D-pathway in cytochrome c oxidase: Application of the proton-inventory technique
    • DOI 10.1021/bi992719t
    • M. Karpefors, P. Ädelroth, and P. Brzezinski Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique Biochemistry 39 2000 6850 6856 (Pubitemid 30390377)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 6850-6856
    • Karpefors, M.1    Adelroth, P.2    Brzezinski, P.3
  • 68
    • 0034595189 scopus 로고    scopus 로고
    • The onset of the deuterium isotope effect in cytochrome c oxidase
    • DOI 10.1021/bi9925221
    • M. Karpefors, P. Ädelroth, and P. Brzezinski The onset of the deuterium isotope effect in cytochrome c oxidase Biochemistry 39 2000 5045 5050 (Pubitemid 30241624)
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 5045-5050
    • Karpefors, M.1    Adelroth, P.2    Brzezinski, P.3
  • 69
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase
    • DOI 10.1016/S0005-2728(00)00194-8, PII S0005272800001948
    • P. Ädelroth, M. Karpefors, G. Gilderson, F.L. Tomson, R.B. Gennis, and P. Brzezinski Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase Biochim. Biophys. Acta 1459 2000 533 539 (Pubitemid 30612430)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1459 , Issue.2-3 , pp. 533-539
    • Adelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 71
    • 40949134606 scopus 로고    scopus 로고
    • Deuterium isotope effect of proton pumping in cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2007.09.009, PII S0005272807002277
    • L. Salomonsson, G. Brändén, and P. Brzezinski Deuterium isotope effect of proton pumping in cytochrome c oxidase Biochim. Biophys. Acta Bioenerg. 1777 2008 343 350 (Pubitemid 351417725)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.4 , pp. 343-350
    • Salomonsson, L.1    Branden, G.2    Brzezinski, P.3
  • 72
    • 0037790647 scopus 로고    scopus 로고
    • A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase
    • DOI 10.1021/bi0341307
    • D.A. Mills, Z. Tan, S. Ferguson-Miller, and J. Hosler A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase Biochemistry 42 2003 7410 7417 (Pubitemid 36735818)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7410-7417
    • Mills, D.A.1    Tan, Z.2    Ferguson-Miller, S.3    Hosler, J.4
  • 74
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • DOI 10.1074/jbc.M407549200
    • S.A. Siletsky, A.S. Pawate, K. Weiss, R.B. Gennis, and A.A. Konstantinov Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase J. Biol. Chem. 279 2004 52558 52565 (Pubitemid 39656632)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2    Weiss, K.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 76
    • 33646268674 scopus 로고    scopus 로고
    • Monte Carlo simulations of proton pumps: On the working principles of the biological valve that controls proton pumping in cytochrome c oxidase
    • M.H. Olsson, and A. Warshel Monte Carlo simulations of proton pumps: on the working principles of the biological valve that controls proton pumping in cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 103 2006 6500 6505
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6500-6505
    • Olsson, M.H.1    Warshel, A.2
  • 77
    • 63449091255 scopus 로고    scopus 로고
    • Functional hydration and conformational gating of proton uptake in cytochrome c oxidase
    • R.M. Henry, C.H. Yu, T. Rodinger, and R. Pomès Functional hydration and conformational gating of proton uptake in cytochrome c oxidase J. Mol. Biol. 387 2009 1165 1185
    • (2009) J. Mol. Biol. , vol.387 , pp. 1165-1185
    • Henry, R.M.1    Yu, C.H.2    Rodinger, T.3    Pomès, R.4
  • 78
    • 33748365234 scopus 로고    scopus 로고
    • Transition state theory can be used in studies of enzyme catalysis: Lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems
    • DOI 10.1098/rstb.2006.1880
    • M.H. Olsson, J. Mavri, and A. Warshel Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems Philos. Trans. R. Soc. Lond. B Biol. Sci. 361 2006 1417 1432 (Pubitemid 44338501)
    • (2006) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.361 , Issue.1472 , pp. 1417-1432
    • Olsson, M.H.M.1    Mavri, J.2    Warshel, A.3
  • 79
    • 0033264078 scopus 로고    scopus 로고
    • The deuterium isotope effect as a tool to investigate enzyme catalysis: Proton-transfer control mechanisms in cytochrome c oxidase
    • M. Karpefors, P. Ädelroth, A. Aagaard, I.A. Smirnova, and P. Brzezinski The deuterium isotope effect as a tool to investigate enzyme catalysis: proton-transfer control mechanisms in cytochrome c oxidase Isr. J. Chem. 39 1999 427 437
    • (1999) Isr. J. Chem. , vol.39 , pp. 427-437
    • Karpefors, M.1    Ädelroth, P.2    Aagaard, A.3    Smirnova, I.A.4    Brzezinski, P.5
  • 81
    • 56249146306 scopus 로고    scopus 로고
    • A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate
    • K.L. Durr, J. Koepke, P. Hellwig, H. Muller, H. Angerer, G. Peng, E. Olkhova, O.M. Richter, B. Ludwig, and H. Michel A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate J. Mol. Biol. 384 2008 865 877
    • (2008) J. Mol. Biol. , vol.384 , pp. 865-877
    • Durr, K.L.1    Koepke, J.2    Hellwig, P.3    Muller, H.4    Angerer, H.5    Peng, G.6    Olkhova, E.7    Richter, O.M.8    Ludwig, B.9    Michel, H.10
  • 82
    • 1542317813 scopus 로고    scopus 로고
    • Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase
    • DOI 10.1021/ja037233l
    • M.H.M. Olsson, P.E.M. Siegbahn, and A. Warshel Simulations of the large kinetic isotope effect and the temperature dependence of the hydrogen atom transfer in lipoxygenase J. Am. Chem. Soc. 126 2004 2820 2828 (Pubitemid 38314288)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.9 , pp. 2820-2828
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Warshel, A.3
  • 84
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • G.T. Babcock, and M. Wikström Oxygen activation and the conservation of energy in cell respiration Nature 356 1992 301 309
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 86
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme
    • DOI 10.1016/S0005-2728(98)00142-X, PII S000527289800142X
    • P. Ädelroth, M. Ek, and P. Brzezinski Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides and bovine enzymes Biochim. Biophys. Acta 1367 1998 107 117 (Pubitemid 28451587)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1367 , Issue.1-3 , pp. 107-117
    • Adelroth, P.1    Ek, M.2    Brzezinski, P.3


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