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Volumn 47, Issue 1, 2008, Pages 73-83

Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; ENZYMES; MICROORGANISMS; MOLECULAR STRUCTURE; MUTAGENESIS; RESPIRATORY MECHANICS;

EID: 38049091274     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701643a     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • Hosler, J. P., Ferguson-Miller, S., and Mills, D. A. (2006) Energy transduction: proton transfer through the respiratory complexes, Annu. Rev. Biochem. 75, 165-187.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 2
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • Gennis, R. B. (2004) Coupled proton and electron transfer reactions in cytochrome oxidase, Front. Biosci. 9, 581-591.
    • (2004) Front. Biosci , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 3
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • Brzezinski, P. (2004) Redox-driven membrane-bound proton pumps, Trends Biochem. Sci. 29, 380-387.
    • (2004) Trends Biochem. Sci , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 4
    • 0024571740 scopus 로고
    • Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping
    • Wikström, M. (1989) Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping, Nature 338, 776-778.
    • (1989) Nature , vol.338 , pp. 776-778
    • Wikström, M.1
  • 5
    • 0041846657 scopus 로고    scopus 로고
    • M and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase
    • 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
  • 6
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • Proshlyakov, D. A., Pressler, M. A., DeMaso, C., Leykam, J. F., DeWitt, D. L., and Babcock, G. T. (2000) Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244, Science 290, 1588-1591.
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    DeMaso, C.3    Leykam, J.F.4    DeWitt, D.L.5    Babcock, G.T.6
  • 7
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: Investigation of the oxygen reaction in the R. sphaeroides enzyme
    • Ädelroth, P., Ek, M., and Brzezinski, P. (1998) Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme, Biochim. Biophys. Acta 1367, 107-117.
    • (1998) Biochim. Biophys. Acta , vol.1367 , pp. 107-117
    • Ädelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 8
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • Morgan, J. E., Verkhovsky, M. I., and Wikström, M. (1996) Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase, Biochemistry 35, 12235-12240.
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 9
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén, K., Gilderson, G., Ädelroth, P., and Brzezinski, P. (2005) A mechanistic principle for proton pumping by cytochrome c oxidase, Nature 437, 286-289.
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 11
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek, M., Abramson, J., Larsson, G., Törnroth, S., Brzezinski, P., and Iwata, S. (2002) The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides, J. Mol. Biol. 321, 329-339.
    • (2002) J. Mol. Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 12
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8 Å 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
  • 14
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström, M., Jasaitis, A., Backgren, C., Puustinen, A., and Verkhovsky, M. I. (2000) The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases, Biochim. Biophys. Acta 1459, 514-520.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 18
    • 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
  • 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
    • Konstantinov, A. A., Siletsky, S., Mitchell, D., Kaulen, A., and Gennis, R. B. (1997) 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, 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
  • 21
    • 0030692008 scopus 로고    scopus 로고
    • Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: Influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies
    • Tsubaki, M., Hori, H., and Mogi, T. (1997) Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies, FEBS Lett. 416, 247-250.
    • (1997) FEBS Lett , vol.416 , pp. 247-250
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3
  • 23
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase
    • Ädelroth, P., Karpefors, M., Gilderson, G., Tomson, F. L., Gennis, R. B., and Brzezinski, P. (2000) Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase, Biochim. Biophys. Acta 1459, 533-539.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 533-539
    • Ädelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 24
    • 17344382320 scopus 로고    scopus 로고
    • Effects of mutation of the conserved glutamic acid-286 in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides
    • Jünemann, S., Meunier, B., Fisher, N., and Rich, P. R. (1999) Effects of mutation of the conserved glutamic acid-286 in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides, Biochemistry 38, 5248-5255.
    • (1999) Biochemistry , vol.38 , pp. 5248-5255
    • Jünemann, S.1    Meunier, B.2    Fisher, N.3    Rich, P.R.4
  • 25
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • Brändén, G., Gennis, R. B., and Brzezinski, P. (2006) Transmembrane proton translocation by cytochrome c oxidase, Biochim. Biophys. Acta 1757, 1052-1063.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1052-1063
    • Brändén, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 26
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen, A., and Wikström, M. (1999) Proton exit from the heme-copper oxidase of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 96, 35-37.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 27
    • 23244450116 scopus 로고    scopus 로고
    • Water Chain Formation and Possible Proton Pumping Routes in Rhodobacter sphaeroides Cytochrome c Oxidase: A Molecular Dynamics Comparison of the Wild Type and R481K Mutant
    • Seibold, S. A., Mills, D. A., Ferguson-Miller, S., and Cukier, R. I. (2005) Water Chain Formation and Possible Proton Pumping Routes in Rhodobacter sphaeroides Cytochrome c Oxidase: A Molecular Dynamics Comparison of the Wild Type and R481K Mutant, Biochemistry 44, 10475-10485.
    • (2005) Biochemistry , vol.44 , pp. 10475-10485
    • Seibold, S.A.1    Mills, D.A.2    Ferguson-Miller, S.3    Cukier, R.I.4
  • 28
    • 23244459036 scopus 로고    scopus 로고
    • The protonation state of a heme propionate controls electron transfer in cytochrome c oxidase
    • Brändén, G., Brändén, M., Schmidt, B., Mills, D. A., Ferguson-Miller, S., and Brzezinski, P. (2005) The protonation state of a heme propionate controls electron transfer in cytochrome c oxidase, Biochemistry 44, 10466-10474.
    • (2005) Biochemistry , vol.44 , pp. 10466-10474
    • Brändén, G.1    Brändén, M.2    Schmidt, B.3    Mills, D.A.4    Ferguson-Miller, S.5    Brzezinski, P.6
  • 29
    • 0031559894 scopus 로고    scopus 로고
    • Bound water in the proton translocation mechanism of the haem-copper oxidases
    • Riistama, S., Hummer, G., Puustinen, A., Dyer, R. B., Woodruff, W. H., and Wikström, M. (1997) Bound water in the proton translocation mechanism of the haem-copper oxidases, FEBS Lett. 414, 275-280.
    • (1997) FEBS Lett , vol.414 , pp. 275-280
    • Riistama, S.1    Hummer, G.2    Puustinen, A.3    Dyer, R.B.4    Woodruff, W.H.5    Wikström, M.6
  • 31
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikström, M., Verkhovsky, M. I., and Hummer, G. (2003) Water-gated mechanism of proton translocation by cytochrome c oxidase, Biochim. Biophys. Acta 1604, 61-65.
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 32
    • 2642586355 scopus 로고    scopus 로고
    • Quantum molecular dynamics simulation of proton transfer in cytochrome c oxidase
    • Cukier, R. I. (2004) Quantum molecular dynamics simulation of proton transfer in cytochrome c oxidase, Biochim. Biophys. Acta 1656, 189-202.
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 189-202
    • Cukier, R.I.1
  • 33
    • 13244260957 scopus 로고    scopus 로고
    • Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase
    • Tashiro, M., and Stuchebrukhov, A. A. (2005) Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase, J. Phys. Chem. B 109, 1015-1022.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1015-1022
    • Tashiro, M.1    Stuchebrukhov, A.A.2
  • 34
    • 0037716158 scopus 로고    scopus 로고
    • Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: Lessons from other proteins
    • Mills, D. A., and Ferguson-Miller, S. (2003) Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins. FEBS Lett. 545, 47-51.
    • (2003) FEBS Lett , vol.545 , pp. 47-51
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 35
    • 33750282788 scopus 로고    scopus 로고
    • Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase
    • Busenlehner, L. S., Salomonsson, L., Brzezinski, P., and Armstrong, R. N. (2006) Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase. Proc. Natl. Acad. Sci. U.S.A. 103, 15398-15403.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 15398-15403
    • Busenlehner, L.S.1    Salomonsson, L.2    Brzezinski, P.3    Armstrong, R.N.4
  • 36
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith, D. L., Deng, Y., and Zhang, Z. (1997) Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry, J. Mass. Spectrom. 32, 135-146.
    • (1997) J. Mass. Spectrom , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 37
    • 9744270012 scopus 로고    scopus 로고
    • Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry
    • Busenlehner, L. S., and Armstrong, R. N. (2005) Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry, Arch. Biochem. Biophys. 423, 34-46.
    • (2005) Arch. Biochem. Biophys , vol.423 , pp. 34-46
    • Busenlehner, L.S.1    Armstrong, R.N.2
  • 38
    • 0034719162 scopus 로고    scopus 로고
    • Redesign of the proton-pumping machinery of cytochrome c oxidase: Proton pumping does not require Glu-(I-286)
    • Aagaard, A., Gilderson, G., Mills, D. A., Ferguson-Miller, S., and Brzezinski, P. (2000) Redesign of the proton-pumping machinery of cytochrome c oxidase: proton pumping does not require Glu-(I-286), Biochemistry 39, 15847-15850.
    • (2000) Biochemistry , vol.39 , pp. 15847-15850
    • Aagaard, A.1    Gilderson, G.2    Mills, D.A.3    Ferguson-Miller, S.4    Brzezinski, P.5
  • 40
    • 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
    • Lee, H. M., Das, T. K., Rousseau, D. L., Mills, D., Ferguson-Miller, S., and Gennis, R. B. (2000) 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, 2989-2996.
    • (2000) Biochemistry , vol.39 , 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
  • 41
    • 0032010153 scopus 로고    scopus 로고
    • A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
    • Zhang, Z., and Marshall, A. G. (1998) A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 9, 225-233.
    • (1998) J. Am. Soc. Mass Spectrom , vol.9 , pp. 225-233
    • Zhang, Z.1    Marshall, A.G.2
  • 42
    • 0028925948 scopus 로고
    • Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides
    • Ädelroth, P., Brzezinski, P., and Malmström, B. G. (1995) Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides, Biochemistry 34, 2844-2849.
    • (1995) Biochemistry , vol.34 , pp. 2844-2849
    • Ädelroth, P.1    Brzezinski, P.2    Malmström, B.G.3
  • 43
    • 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
  • 44
    • 34447519323 scopus 로고    scopus 로고
    • Plasticity of proton pathway structure and water coordination in cytochrome c oxidase
    • Namslauer, A., Lepp, H., Brändén, M., Jasaitis, A., Verkhovsky, M. I., and Brzezinski, P. (2007) Plasticity of proton pathway structure and water coordination in cytochrome c oxidase, J. Biol. Chem. 282, 15148-15158.
    • (2007) J. Biol. Chem , vol.282 , pp. 15148-15158
    • Namslauer, A.1    Lepp, H.2    Brändén, M.3    Jasaitis, A.4    Verkhovsky, M.I.5    Brzezinski, P.6
  • 46
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin, L., Hiser, C., Mulichak, A., Garavito, R. M., and Ferguson-Miller, S. (2006) Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 103, 16117-16122.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 49
    • 13444305368 scopus 로고    scopus 로고
    • Proton Exit Channels in Bovine Cytochrome c Oxidase
    • Popović, D. M., and Stuchebrukhov, A. A. (2005) Proton Exit Channels in Bovine Cytochrome c Oxidase, J. Phys. Chem. B 109, 1999-2006.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1999-2006
    • Popović, D.M.1    Stuchebrukhov, A.A.2
  • 50
    • 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
    • Namslauer, A., Aagaard, A., Katsonouri, A., and Brzezinski, P. (2003) 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, 1488-1498.
    • (2003) Biochemistry , vol.42 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 51
    • 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
  • 52
    • 0031862465 scopus 로고    scopus 로고
    • + conduction along hydrogen-bonded chains of water molecules
    • + conduction along hydrogen-bonded chains of water molecules, Biophys. J. 75, 33-40.
    • (1998) Biophys. J , vol.75 , pp. 33-40
    • Pomes, R.1    Roux, B.2
  • 53
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • Brzezinski, P., and Larsson, G. (2003) Redox-driven proton pumping by heme-copper oxidases, Biochim. Biophys. Acta 1605, 1-13.
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2


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