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Volumn 46, Issue 45, 2007, Pages 13141-13148

Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans

Author keywords

[No Author keywords available]

Indexed keywords

DENITRIFICATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; OXYGEN; PROTON TRANSFER; PROTONATION; REAL TIME SYSTEMS;

EID: 36049009410     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701614w     Document Type: Article
Times cited : (41)

References (42)
  • 1
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • Wikström, M., and Verkhovsky, M. I. (2007) Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases, Biochim. Biophys. Acta 1767, 1200-1214.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 3
    • 33748885262 scopus 로고    scopus 로고
    • Towards the mechanism of proton pumping by the haem-copper oxidases
    • Wikström, M., and Verkhovsky, M. I. (2006) Towards the mechanism of proton pumping by the haem-copper oxidases, Biochim. Biophys. Acta 1757, 1047-1051.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1047-1051
    • Wikström, M.1    Verkhovsky, M.I.2
  • 4
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • Belevich, I., Verkhovsky, M. I., and Wikström, M. (2006) Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase, Nature 440, 829-832.
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 5
    • 0028890031 scopus 로고
    • Structure at 2.8-Angstrom resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8-Angstrom resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 7
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen, Biochemistry 36, 13824-13829.
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Ek, M.S.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 8
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxoferryl formation
    • Smirnova, I. A., Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1999) Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxoferryl formation, Biochemistry 38, 6826-6833.
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 9
    • 0025629995 scopus 로고
    • Simultaneous monitoring of light-induced-changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared-spectroscopy
    • Gerwert, K., Souvignier, G., and Hess, B. (1990) Simultaneous monitoring of light-induced-changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared-spectroscopy, Proc. Natl. Acad. Sci. U.S.A. 87, 9774-9778.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 9774-9778
    • Gerwert, K.1    Souvignier, G.2    Hess, B.3
  • 10
    • 0033545872 scopus 로고    scopus 로고
    • a changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy
    • a changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy, Proc. Natl. Acad. Sci. U.S.A. 96, 5498-5503.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 5498-5503
    • Zscherp, C.1    Schlesinger, R.2    Tittor, J.3    Oesterhelt, D.4    Heberle, J.5
  • 11
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • Garczarek, F., and Gerwert, K. (2006) Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy, Nature 439, 109-112.
    • (2006) Nature , vol.439 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2
  • 12
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • Remy, A., and Gerwert, K. (2003) Coupling of light-induced electron transfer to proton uptake in photosynthesis, Nature Struct. Biol. 10, 637-644.
    • (2003) Nature Struct. Biol , vol.10 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 13
    • 34249850930 scopus 로고    scopus 로고
    • Deactivation and proton transfer in light-induced metarhodopsin II/ metarhodopsin III conversion: A time-resolved Fourier transform infrared spectroscopic study
    • Ritter, E., Elgeti, M., Hofmann, K. P., and Bartl, F. J. (2007) Deactivation and proton transfer in light-induced metarhodopsin II/ metarhodopsin III conversion: a time-resolved Fourier transform infrared spectroscopic study, J. Biol. Chem. 282, 10720-10730.
    • (2007) J. Biol. Chem , vol.282 , pp. 10720-10730
    • Ritter, E.1    Elgeti, M.2    Hofmann, K.P.3    Bartl, F.J.4
  • 14
    • 0033535929 scopus 로고    scopus 로고
    • Time-resolved FT-IR studies on the CO adduct of Paracoccus denitrificans cytochrome c oxidase: Comparison of the fully reduced and the mixed valence form
    • Rost, B., Behr, J., Hellwig, P., Richter, O. M. H., Ludwig, B., Michel, H., and Mäntele, W. (1999) Time-resolved FT-IR studies on the CO adduct of Paracoccus denitrificans cytochrome c oxidase: Comparison of the fully reduced and the mixed valence form, Biochemistry 38, 7565-7571.
    • (1999) Biochemistry , vol.38 , pp. 7565-7571
    • Rost, B.1    Behr, J.2    Hellwig, P.3    Richter, O.M.H.4    Ludwig, B.5    Michel, H.6    Mäntele, W.7
  • 15
    • 0036219767 scopus 로고    scopus 로고
    • Transient binding of CO to Cu-B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: A time-resolved step-scan Fourier transform infrared investigation
    • Heitbrink, D., Sigurdson, H., Bolwien, C., Brzezinski, P., and Heberle, J. (2002) Transient binding of CO to Cu-B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: A time-resolved step-scan Fourier transform infrared investigation, Biophys. J. 82, 1-10.
    • (2002) Biophys. J , vol.82 , pp. 1-10
    • Heitbrink, D.1    Sigurdson, H.2    Bolwien, C.3    Brzezinski, P.4    Heberle, J.5
  • 17
    • 0344961407 scopus 로고    scopus 로고
    • Ligand binding in a docking site of cytochrome c oxidase: A time-resolved step-scan Fourier transform infrared study
    • Koutsoupakis, C., Soulimane, T., and Varotsis, C. (2003) Ligand binding in a docking site of cytochrome c oxidase: A time-resolved step-scan Fourier transform infrared study, J. Am. Chem. Soc. 125, 14728-14732.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14728-14732
    • Koutsoupakis, C.1    Soulimane, T.2    Varotsis, C.3
  • 18
  • 19
    • 33746928351 scopus 로고    scopus 로고
    • Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286
    • Vakkasoglu, A. S., Morgan, J. E., Han, D., Pawate, A. S., and Gennis, R. B. (2006) Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286, FEBS Lett. 580, 4613-4617.
    • (2006) FEBS Lett , vol.580 , pp. 4613-4617
    • Vakkasoglu, A.S.1    Morgan, J.E.2    Han, D.3    Pawate, A.S.4    Gennis, R.B.5
  • 20
    • 0041846657 scopus 로고    scopus 로고
    • ATR-FTIR spectroscopy of the P-M and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase
    • Iwaki, M., Puustinen, A., Wikström, M., and Rich, P. R. (2003) ATR-FTIR spectroscopy of the P-M and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase, Biochemistry 42, 8809-8817.
    • (2003) Biochemistry , vol.42 , pp. 8809-8817
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 21
    • 34047233447 scopus 로고    scopus 로고
    • Protolytic reactions on reduction of cytochrome c oxidase studied by ATR-FTIR spectroscopy
    • Gorbikova, E. A., Belevich, N. P., Wikström, M., and Verkhovsky, M. I. (2007) Protolytic reactions on reduction of cytochrome c oxidase studied by ATR-FTIR spectroscopy, Biochemistry 46, 4177-4183.
    • (2007) Biochemistry , vol.46 , pp. 4177-4183
    • Gorbikova, E.A.1    Belevich, N.P.2    Wikström, M.3    Verkhovsky, M.I.4
  • 23
    • 0000336683 scopus 로고
    • Regularization Techniques for Inverse Problems in Molecular Biology
    • Deufhard, E, Hairer, E, Eds, pp, Birkhauser, Boston
    • Provencher, S. W., and Vogel, R. H. (1983) Regularization Techniques for Inverse Problems in Molecular Biology, Progress in Scientific Computing (Deufhard, E., Hairer, E., Eds.) pp 304-319, Birkhauser, Boston.
    • (1983) Progress in Scientific Computing , pp. 304-319
    • Provencher, S.W.1    Vogel, R.H.2
  • 25
    • 0029657964 scopus 로고    scopus 로고
    • 3-Cu-B binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy
    • 3-Cu-B binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy, Biophys. J. 71, 1036-1047.
    • (1996) Biophys. J , vol.71 , pp. 1036-1047
    • Park, S.1    Pan, L.P.2    Chan, S.I.3    Alben, J.O.4
  • 26
    • 0022871186 scopus 로고
    • Alpha and beta forms of cytochrome-c-oxidase observed in rat-heart myocytes by low-temperature Fourier-transform infrared-spectroscopy
    • Flamingo, F. G., Altschuld, R. A., and Alben, J. O. (1986) Alpha and beta forms of cytochrome-c-oxidase observed in rat-heart myocytes by low-temperature Fourier-transform infrared-spectroscopy, J. Biol. Chem. 261, 2976-2987.
    • (1986) J. Biol. Chem , vol.261 , pp. 2976-2987
    • Flamingo, F.G.1    Altschuld, R.A.2    Alben, J.O.3
  • 27
    • 33645461637 scopus 로고    scopus 로고
    • Proton-coupled electron equilibrium in soluble and membrane-bound cytochrome c oxidase from Paracoccus denitrificans
    • Belevich, I., Tuukkanen, A., Wikström, M., and Verkhovsky, M. I. (2006) Proton-coupled electron equilibrium in soluble and membrane-bound cytochrome c oxidase from Paracoccus denitrificans, Biochemistry 45, 4000-4006.
    • (2006) Biochemistry , vol.45 , pp. 4000-4006
    • Belevich, I.1    Tuukkanen, A.2    Wikström, M.3    Verkhovsky, M.I.4
  • 29
    • 0039242661 scopus 로고
    • Energy-dependent reversal of the cytochrome-oxidase reaction
    • Wikström, M. (1981) Energy-dependent reversal of the cytochrome-oxidase reaction, Proc. Natl. Acad. Sci. U.S.A. 78, 4051-4054.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 4051-4054
    • Wikström, M.1
  • 30
    • 0023013873 scopus 로고
    • 3 intermediate during turnover of cytochrome-c-oxidase
    • 3 intermediate during turnover of cytochrome-c-oxidase, J. Biol. Chem. 261, 8104-8107.
    • (1986) J. Biol. Chem , vol.261 , pp. 8104-8107
    • Witt, S.N.1    Blair, D.F.2    Chan, S.I.3
  • 31
    • 29244472486 scopus 로고    scopus 로고
    • An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans
    • Ribacka, C., Verkhovsky, M. I., Belevich, I., Bloch, D. A., Puustinen, A., and Wikström, M. (2005) An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans, Biochemistry 44, 16502-16512.
    • (2005) Biochemistry , vol.44 , pp. 16502-16512
    • Ribacka, C.1    Verkhovsky, M.I.2    Belevich, I.3    Bloch, D.A.4    Puustinen, A.5    Wikström, M.6
  • 32
    • 0042307434 scopus 로고    scopus 로고
    • Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase
    • Nyquist, R. M., Heitbrink, D., Bolwien, C., Gennis, R. B., and Heberle, J. (2003) Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 100, 8715-8720.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 8715-8720
    • Nyquist, R.M.1    Heitbrink, D.2    Bolwien, C.3    Gennis, R.B.4    Heberle, J.5
  • 35
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy
    • Hellwig, P., Behr, J., Ostermeier, C., Richter, O. M. H., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H., and Mäntele, W. (1998) Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy, Biochemistry 37, 7390-7399.
    • (1998) Biochemistry , vol.37 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2    Ostermeier, C.3    Richter, O.M.H.4    Pfitzner, U.5    Odenwald, A.6    Ludwig, B.7    Michel, H.8    Mäntele, W.9
  • 36
    • 33646355978 scopus 로고    scopus 로고
    • Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy
    • Gorbikova, E. A., Vuorilehto, K., Wikström, M., and Verkhovsky, M. I. (2006) Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy, Biochemistry 45, 5641-5649.
    • (2006) Biochemistry , vol.45 , pp. 5641-5649
    • Gorbikova, E.A.1    Vuorilehto, K.2    Wikström, M.3    Verkhovsky, M.I.4
  • 37
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands, Biopolymers 30, 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 38
    • 0029884379 scopus 로고    scopus 로고
    • Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy
    • Hellwig, P., Rost, B., Kaiser, U., Ostermeier, C., Michel, H., and Mäntele, W. (1996) Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy, FEBS Lett. 385, 53-57.
    • (1996) FEBS Lett , vol.385 , pp. 53-57
    • Hellwig, P.1    Rost, B.2    Kaiser, U.3    Ostermeier, C.4    Michel, H.5    Mäntele, W.6
  • 39
    • 0042307434 scopus 로고    scopus 로고
    • Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase
    • Nyquist, R. M., Heitbrink, D., Bolwien, C., Gennis, R. B., and Heberle, J. (2003) Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 100, 8715-8720.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 8715-8720
    • Nyquist, R.M.1    Heitbrink, D.2    Bolwien, C.3    Gennis, R.B.4    Heberle, J.5
  • 40
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck
    • Olsson, M. H. M., Sharma, P. K., and Warshel, A. (2005) Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck, FEBS Lett. 579, 2026-2034.
    • (2005) FEBS Lett , vol.579 , pp. 2026-2034
    • Olsson, M.H.M.1    Sharma, P.K.2    Warshel, A.3
  • 41
    • 33947280355 scopus 로고    scopus 로고
    • Storage of an excess proton in the hydrogen-bonded network of the D-pathway of cytochrome c oxidase: Identification of a protonated water cluster
    • Xu, J. C., Sharpe, M. A., Qin, L., Ferguson-Miller, S., and Voth, G. A. (2007) Storage of an excess proton in the hydrogen-bonded network of the D-pathway of cytochrome c oxidase: Identification of a protonated water cluster, J. Am. Chem. Soc. 129, 2910-2913.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 2910-2913
    • Xu, J.C.1    Sharpe, M.A.2    Qin, L.3    Ferguson-Miller, S.4    Voth, G.A.5


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