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Volumn 1777, Issue 7-8, 2008, Pages 912-918

Carboxyl group functions in the heme-copper oxidases: Information from mid-IR vibrational spectroscopy

Author keywords

Cytochrome c oxidase; Energy coupling; FTIR spectroscopy; Infrared spectroscopy; Proton transfer

Indexed keywords

ANION; ASPARTIC ACID; BACTERIAL ENZYME; CALCIUM ION; CARBOXYL GROUP; COPPER; CYTOCHROME C OXIDASE; GLUTAMIC ACID; HEME; LIGAND; PROPIONIC ACID; SODIUM ION;

EID: 46349099533     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.04.035     Document Type: Review
Times cited : (16)

References (97)
  • 3
    • 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. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 4
    • 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. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321 (2002) 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
  • 7
    • 24044442616 scopus 로고    scopus 로고
    • A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba(3) oxidase from Thermus thermophilus
    • Hunsicker-Wang L.M., Pacoma R.L., Chen Y., Fee J.A., and Stout C.D. A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba(3) oxidase from Thermus thermophilus. Acta Crystallog., Sect. D. 61 (2005) 340-343
    • (2005) Acta Crystallog., Sect. D. , vol.61 , pp. 340-343
    • Hunsicker-Wang, L.M.1    Pacoma, R.L.2    Chen, Y.3    Fee, J.A.4    Stout, C.D.5
  • 8
    • 0033539481 scopus 로고    scopus 로고
    • How oxygen is activated and reduced in respiration
    • Babcock G.T. How oxygen is activated and reduced in respiration. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12971-12973
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12971-12973
    • Babcock, G.T.1
  • 9
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock G.T., and Wikström M. 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
  • 10
    • 0347419305 scopus 로고    scopus 로고
    • The molecular machinery of Keilin's respiratory chain
    • Rich P.R. The molecular machinery of Keilin's respiratory chain. Biochem. Soc. Trans. 31 (2003) 1095-1105
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1095-1105
    • Rich, P.R.1
  • 11
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: proton transfer through the respiratory complexes
    • Hosler J.P., Ferguson-Miller S., and Mills D.A. Energy transduction: proton transfer through the respiratory complexes. Ann. Rev. Biochem. 75 (2006) 165-187
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 12
    • 33746601087 scopus 로고    scopus 로고
    • Design principles of proton-pumping haem-copper oxidases
    • Brzezinski P., and Ädelroth P. Design principles of proton-pumping haem-copper oxidases. Curr. Opin. Struct. Biol. 16 (2006) 465-472
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 465-472
    • Brzezinski, P.1    Ädelroth, P.2
  • 14
    • 33745622830 scopus 로고    scopus 로고
    • Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain
    • Papa S., Lorusso M., and di Paola M. Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain. Biochim. Biophys. Acta 1757 (2006) 428-436
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 428-436
    • Papa, S.1    Lorusso, M.2    di Paola, M.3
  • 17
    • 24944511130 scopus 로고    scopus 로고
    • Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in helices XI-XII cytoplasmic loop in cation binding
    • Kirichenko A., Pfitzner U., Ludwig B., Soares C.M., Vygodina T.V., and Konstantinov A.A. Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in helices XI-XII cytoplasmic loop in cation binding. Biochemistry 44 (2005) 12391-12401
    • (2005) Biochemistry , vol.44 , pp. 12391-12401
    • Kirichenko, A.1    Pfitzner, U.2    Ludwig, B.3    Soares, C.M.4    Vygodina, T.V.5    Konstantinov, A.A.6
  • 18
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • Rich P.R. Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases. Aust. Journ. Plant. Physiol. 22 (1995) 479-486
    • (1995) Aust. Journ. Plant. Physiol. , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 19
    • 0026650102 scopus 로고
    • Protonation states of the catalytic cycle intermediates of cytochrome c oxidase
    • Mitchell R., Mitchell P., and Rich P.R. Protonation states of the catalytic cycle intermediates of cytochrome c oxidase. Biochim. Biophys. Acta 1101 (1992) 188-191
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 188-191
    • Mitchell, R.1    Mitchell, P.2    Rich, P.R.3
  • 20
    • 0028241769 scopus 로고
    • Proton uptake by cytochrome c oxidase on reduction and on ligand binding
    • Mitchell R., and Rich P.R. Proton uptake by cytochrome c oxidase on reduction and on ligand binding. Biochim. Biophys. Acta 1186 (1994) 19-26
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 19-26
    • Mitchell, R.1    Rich, P.R.2
  • 21
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel H. The mechanism of proton pumping by cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 12819-12824
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 22
    • 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. Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase. Nature 440 (2006) 829-832
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 23
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén K., Gilderson G., Ädelroth P., and Brzezinski P. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437 (2005) 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 24
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • Calhoun M.W., Thomas J.W., and Gennis R.B. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem. Sci. 19 (1994) 325-330
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 25
    • 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 (1990) 1243-1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 26
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 74 (2000) 141-173
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 27
    • 33644656189 scopus 로고    scopus 로고
    • Infrared protein spectroscopy as a tool to study protonation reactions within proteins
    • Wikström M. (Ed), The Royal Society of Chemistry, Cambridge, U.K.
    • Rich P.R., and Iwaki M. Infrared protein spectroscopy as a tool to study protonation reactions within proteins. In: Wikström M. (Ed). Biophysical and Structural Aspects of Bioenergetics (2005), The Royal Society of Chemistry, Cambridge, U.K. 314-333
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 314-333
    • Rich, P.R.1    Iwaki, M.2
  • 28
    • 0029057198 scopus 로고
    • Bacteriorhodopsin as a model for proton pumps
    • Lanyi J.K. Bacteriorhodopsin as a model for proton pumps. Nature 375 (1995) 461-463
    • (1995) Nature , vol.375 , pp. 461-463
    • Lanyi, J.K.1
  • 30
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates
    • Braiman M.S., Bousché O., and Rothschild K.J. Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 2388-2392
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2388-2392
    • Braiman, M.S.1    Bousché, O.2    Rothschild, K.J.3
  • 31
    • 0033545872 scopus 로고    scopus 로고
    • In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy
    • Zscherp C., Schlesinger R., Tittor J., Oesterhelt D., and Heberle J. In situ determination of transient pKa 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 (1999) 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
  • 32
    • 0038182934 scopus 로고    scopus 로고
    • 3 from Acidianus ambivalens: evidence for the involvement of acidic residues in redox coupled proton translocation
    • 3 from Acidianus ambivalens: evidence for the involvement of acidic residues in redox coupled proton translocation. Biochemistry 42 (2003) 6179-6184
    • (2003) Biochemistry , vol.42 , pp. 6179-6184
    • Hellwig, P.1    Gomes, C.M.2    Teixeira, M.3
  • 33
    • 0040036627 scopus 로고    scopus 로고
    • Synthesis and characterization of ruthenium, rhenium and titanium formate, acetate and fluoroacetate complexes. Correlation of IR spectral propertied and bonding types
    • Gibson D.H., Ding Y., Miller R.L., Sleadd B.A., Mashuta M.S., and Richardson J.F. Synthesis and characterization of ruthenium, rhenium and titanium formate, acetate and fluoroacetate complexes. Correlation of IR spectral propertied and bonding types. Polyhedron 18 (1999) 1189-1200
    • (1999) Polyhedron , vol.18 , pp. 1189-1200
    • Gibson, D.H.1    Ding, Y.2    Miller, R.L.3    Sleadd, B.A.4    Mashuta, M.S.5    Richardson, J.F.6
  • 34
    • 0028948099 scopus 로고
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy. Biochim. Biophys. Acta 1228 (1995) 189-200
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 189-200
    • Noguchi, T.1    Ono, T.-A.2    Inoue, Y.3
  • 35
    • 85001163723 scopus 로고
    • Relationships between the carbon-oxygen stretching frequencies of carboxylate complexes and the type of carboxylate coordination
    • Deacon G.B., and Phillips R.S. Relationships between the carbon-oxygen stretching frequencies of carboxylate complexes and the type of carboxylate coordination. Coord. Chem. Rev. 33 (1980) 227-250
    • (1980) Coord. Chem. Rev. , vol.33 , pp. 227-250
    • Deacon, G.B.1    Phillips, R.S.2
  • 36
    • 0024621968 scopus 로고
    • FT-IR characterisation of metal acetates in aqueous solution
    • Tackett J.E. FT-IR characterisation of metal acetates in aqueous solution. Applied Spectroscopy 43 (1989) 483-489
    • (1989) Applied Spectroscopy , vol.43 , pp. 483-489
    • Tackett, J.E.1
  • 37
    • 0003430467 scopus 로고    scopus 로고
    • Infrared and Raman spectra of inorganic and coordination compounds: applications in coordination
    • John Wiley & Sons, Inc., New York
    • Nakamoto K. Infrared and Raman spectra of inorganic and coordination compounds: applications in coordination. Organometallic and Bioinorganic Chemistry (1997), John Wiley & Sons, Inc., New York
    • (1997) Organometallic and Bioinorganic Chemistry
    • Nakamoto, K.1
  • 40
    • 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. 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 (2006) 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
  • 42
    • 0035903013 scopus 로고    scopus 로고
    • 2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation
    • 2+ binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation. FEBS Lett. 503 (2001) 142-146
    • (2001) FEBS Lett. , vol.503 , pp. 142-146
    • Kannt, A.1    Ostermann, T.2    Müller, H.3    Ruitenberg, M.4
  • 44
    • 0016759109 scopus 로고
    • A spectral shift in cytochrome a induced by calcium ions
    • Wikström M., and Saari H. A spectral shift in cytochrome a induced by calcium ions. Biochim. Biophys. Acta 408 (1975) 170-179
    • (1975) Biochim. Biophys. Acta , vol.408 , pp. 170-179
    • Wikström, M.1    Saari, H.2
  • 45
  • 48
    • 34547794301 scopus 로고    scopus 로고
    • Possible mechanism of proton transfer through peptide groups in the H-pathway of the bovine cytochrome c oxidase
    • Kamiya K., Boero M., Tateno M., Shiraishi K., and Oshiyama A. Possible mechanism of proton transfer through peptide groups in the H-pathway of the bovine cytochrome c oxidase. J. Am. Chem. Soc. 129 (2007) 9663-9673
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9663-9673
    • Kamiya, K.1    Boero, M.2    Tateno, M.3    Shiraishi, K.4    Oshiyama, A.5
  • 49
    • 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. 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
    • (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
  • 52
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter shaeroides in involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • 3 from Rhodobacter shaeroides in involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. Biochemistry 36 (1997) 13824-13829
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Svensson-Ek, M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 53
    • 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. Effects of mutation of the conserved glutamic acid-286 in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 38 (1999) 5248-5255
    • (1999) Biochemistry , vol.38 , pp. 5248-5255
    • Jünemann, S.1    Meunier, B.2    Fisher, N.3    Rich, P.R.4
  • 54
    • 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. 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
    • (2003) Biochemistry , vol.42 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 55
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Ädelroth P., Gennis R., and Brzezinski P. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. Biochemistry 37 (1998) 2470-2476
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ädelroth, P.1    Gennis, R.2    Brzezinski, P.3
  • 56
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • Wikström M., and Verkhovsky M.I. Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases. Biochim. Biophys. Acta Bioenergetics 1767 (2007) 1200-1214
    • (2007) Biochim. Biophys. Acta Bioenergetics , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 57
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikström M., Verkhovsky M.I., and Hummer G. Water-gated mechanism of proton translocation by cytochrome c oxidase. Biochim. Biophys. Acta 1604 (2003) 61-65
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 59
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt A., Lancaster R.D., and Michel H. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase. Biophysical Journal 74 (1998) 708-721
    • (1998) Biophysical Journal , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, R.D.2    Michel, H.3
  • 62
    • 0032318376 scopus 로고    scopus 로고
    • Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine
    • Gennis R.B. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine. Biochim. Biophys. Acta 1365 (1998) 241-248
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 241-248
    • Gennis, R.B.1
  • 64
    • 0039840998 scopus 로고    scopus 로고
    • Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • Jünemann S., Meunier B., Gennis R.B., and Rich P.R. Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 36 (1997) 14456-14464
    • (1997) Biochemistry , vol.36 , pp. 14456-14464
    • Jünemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 67
    • 33947284329 scopus 로고    scopus 로고
    • An IR study of protonation changes associated with heme-heme electron transfer in bovine cytochrome c oxidase
    • Iwaki M., and Rich P.R. An IR study of protonation changes associated with heme-heme electron transfer in bovine cytochrome c oxidase. J. Am. Chem. Soc. 129 (2007) 2923-2929
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2923-2929
    • Iwaki, M.1    Rich, P.R.2
  • 68
    • 23244466489 scopus 로고    scopus 로고
    • An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase
    • Mills D.A., Geren L., Hiser C., Schmidt B., Durham B., Millett F., and Ferguson-Miller S. An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase. Biochemistry 44 (2005) 10457-10465
    • (2005) Biochemistry , vol.44 , pp. 10457-10465
    • Mills, D.A.1    Geren, L.2    Hiser, C.3    Schmidt, B.4    Durham, B.5    Millett, F.6    Ferguson-Miller, S.7
  • 69
    • 0034673188 scopus 로고    scopus 로고
    • Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis
    • Behr J., Michel H., Mäntele W., and Hellwig P. Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis. Biochemistry 39 (2000) 1356-1363
    • (2000) Biochemistry , vol.39 , pp. 1356-1363
    • Behr, J.1    Michel, H.2    Mäntele, W.3    Hellwig, P.4
  • 70
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy in proteins
    • Barth A. Infrared spectroscopy in proteins. Biochim. Biophys. Acta 1767 (2007) 1073-1101
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 71
    • 3242708681 scopus 로고    scopus 로고
    • The molecular mechanism of membrane proteins probed by evanescent infrared waves
    • Nyquist R.M., Ataka K., and Heberle J. The molecular mechanism of membrane proteins probed by evanescent infrared waves. ChemBioChem. 3 (2004) 431-436
    • (2004) ChemBioChem. , vol.3 , pp. 431-436
    • Nyquist, R.M.1    Ataka, K.2    Heberle, J.3
  • 72
    • 34249706283 scopus 로고    scopus 로고
    • Methods to probe protein transitions with ATR infrared spectroscopy
    • Rich P.R., and Iwaki M. Methods to probe protein transitions with ATR infrared spectroscopy. Mol. Biosys. 3 (2007) 365-550
    • (2007) Mol. Biosys. , vol.3 , pp. 365-550
    • Rich, P.R.1    Iwaki, M.2
  • 73
    • 0035967511 scopus 로고    scopus 로고
    • FTIR studies of the CO and cyanide compounds of fully reduced bovine cytochrome c oxidase
    • Rich P.R., and Breton J. FTIR studies of the CO and cyanide compounds of fully reduced bovine cytochrome c oxidase. Biochemistry 40 (2001) 6441-6449
    • (2001) Biochemistry , vol.40 , pp. 6441-6449
    • Rich, P.R.1    Breton, J.2
  • 75
    • 0019484649 scopus 로고
    • Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex
    • Alben J.O., Moh P.P., Fiamingo F.G., and Altschuld R.A. Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex. Proc. Natl. Acad. Sci. U.S.A. 78 (1981) 234-237
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 234-237
    • Alben, J.O.1    Moh, P.P.2    Fiamingo, F.G.3    Altschuld, R.A.4
  • 76
    • 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. 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 (1999) 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
  • 77
    • 0036219767 scopus 로고    scopus 로고
    • B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation
    • 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 (2002) 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
  • 79
    • 0037176910 scopus 로고    scopus 로고
    • Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and cytochrome bo3 from Escherichia coli
    • Bailey J.A., Tomson F.L., Mecklenburg S.L., MacDonald G.M., Katsonouri A., Puustinen A., Gennis R.B., Woodruff W.H., and Dyer R.B. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and cytochrome bo3 from Escherichia coli. Biochemistry 41 (2002) 2675-2683
    • (2002) Biochemistry , vol.41 , pp. 2675-2683
    • Bailey, J.A.1    Tomson, F.L.2    Mecklenburg, S.L.3    MacDonald, G.M.4    Katsonouri, A.5    Puustinen, A.6    Gennis, R.B.7    Woodruff, W.H.8    Dyer, R.B.9
  • 80
    • 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. Ligand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan Fourier transform infrared study. J. Am. Chem. Soc. 125 (2003) 14728-14732
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14728-14732
    • Koutsoupakis, C.1    Soulimane, T.2    Varotsis, C.3
  • 81
    • 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. Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy. FEBS Lett. 385 (1996) 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
  • 82
    • 0030592721 scopus 로고    scopus 로고
    • Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases
    • Lübben M., and Gerwert K. Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases. FEBS Lett. 397 (1996) 303-307
    • (1996) FEBS Lett. , vol.397 , pp. 303-307
    • Lübben, M.1    Gerwert, K.2
  • 83
    • 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. Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy. Biochemistry 37 (1998) 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
  • 84
    • 0032819266 scopus 로고    scopus 로고
    • Similarities and dissimilarities in the structure-function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy
    • Hellwig P., Soulimane T., Buse G., and Mäntele W. Similarities and dissimilarities in the structure-function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy. FEBS Lett. 458 (1999) 83-86
    • (1999) FEBS Lett. , vol.458 , pp. 83-86
    • Hellwig, P.1    Soulimane, T.2    Buse, G.3    Mäntele, W.4
  • 86
    • 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. Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy. Biochemistry 45 (2006) 5641-5649
    • (2006) Biochemistry , vol.45 , pp. 5641-5649
    • Gorbikova, E.A.1    Vuorilehto, K.2    Wikström, M.3    Verkhovsky, M.I.4
  • 88
    • 0034744058 scopus 로고    scopus 로고
    • Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from P. denitrificans. The reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear centre
    • Hellwig P., Rost B., and Mäntele W. Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from P. denitrificans. The reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear centre. Spectrochim. Acta A 57 (2001) 1123-1131
    • (2001) Spectrochim. Acta A , vol.57 , pp. 1123-1131
    • Hellwig, P.1    Rost, B.2    Mäntele, W.3
  • 90
    • 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 (2003) 8809-8817
    • (2003) Biochemistry , vol.42 , pp. 8809-8817
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 93
    • 33748481558 scopus 로고    scopus 로고
    • M intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidines
    • M intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidines. Biochemistry 45 (2006) 10873-10885
    • (2006) Biochemistry , vol.45 , pp. 10873-10885
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 95
    • 36049009410 scopus 로고    scopus 로고
    • Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans
    • Gorbikova E.A., Belevich N.P., Wikström M., and Verkhovsky M.I. Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 46 (2007) 13141-13148
    • (2007) Biochemistry , vol.46 , pp. 13141-13148
    • Gorbikova, E.A.1    Belevich, N.P.2    Wikström, M.3    Verkhovsky, M.I.4
  • 96
    • 33745605230 scopus 로고    scopus 로고
    • Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral?
    • Song Y., Michonova-Alexova E., and Gunner M.R. Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral?. Biochemistry 45 (2006) 7959-7975
    • (2006) Biochemistry , vol.45 , pp. 7959-7975
    • Song, Y.1    Michonova-Alexova, E.2    Gunner, M.R.3
  • 97
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • Siegbahn P.E.M., Blomberg M.R.A., and Blomberg M.L. 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


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