메뉴 건너뛰기




Volumn 43, Issue 29, 2004, Pages 9477-9486

ATR-FTIR spectroscopy studies of iron-sulfur protein and cytochrome c 1 in the Rhodobacter capsulatus cytochrome bc1 complex

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CRYSTAL STRUCTURE; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MATHEMATICAL MODELS;

EID: 3242733822     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049211x     Document Type: Article
Times cited : (22)

References (61)
  • 8
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell, P. (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems, J. Theor. Biol. 62, 327-367.
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 11
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • Osyczka, A., Moser, C. C., Daldal, F., and Dutton, P. L. (2004) Reversible redox energy coupling in electron transfer chains, Nature 427, 607-612.
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 16
    • 0024276081 scopus 로고
    • Characterisation of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase
    • Brandt, U., Schägger, H., and von Jagow, G. (1988) Characterisation of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase, Eur. J. Biochem. 173, 499-506.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 499-506
    • Brandt, U.1    Schägger, H.2    Von Jagow, G.3
  • 18
    • 0030001519 scopus 로고    scopus 로고
    • 1 complex by proton-gated charge-transfer
    • 1 complex by proton-gated charge-transfer, FEBS Lett. 387, 1-6.
    • (1996) FEBS Lett. , vol.387 , pp. 1-6
    • Brandt, U.1
  • 19
    • 0021968919 scopus 로고
    • Light-induced Fourier transform infrared (FTIR) spectroscopic investigations of the primary oxidation in bacterial photosynthesis
    • Mäntele, W., Nabedryk, E., Tavitian, B. A., Kreutz, W., and Breton, J. (1985) Light-induced Fourier transform infrared (FTIR) spectroscopic investigations of the primary oxidation in bacterial photosynthesis, FEBS Lett. 187, 227-232.
    • (1985) FEBS Lett. , vol.187 , pp. 227-232
    • Mäntele, W.1    Nabedryk, E.2    Tavitian, B.A.3    Kreutz, W.4    Breton, J.5
  • 20
    • 0001607553 scopus 로고
    • Light-induced Fourier transform infrared (FTIR) spectroscopic investigations of primary reactions in photosystem I and photosystem II
    • Tabitian, B. A., Nabedryk, E., Mäntele, W., and Breton, J. (1986) Light-induced Fourier transform infrared (FTIR) spectroscopic investigations of primary reactions in photosystem I and photosystem II, FEBS Lett. 201, 151-157.
    • (1986) FEBS Lett. , vol.201 , pp. 151-157
    • Tabitian, B.A.1    Nabedryk, E.2    Mäntele, W.3    Breton, J.4
  • 21
    • 0025115245 scopus 로고
    • Redox-linked conformational changes in proteins detected by a combination of IR spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c
    • Moss, D., Nabedryk, E., Breton, J., and Mäntele, W. (1990) Redox-linked conformational changes in proteins detected by a combination of IR spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c, Eur. J. Biochem. 187, 565-572.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mäntele, W.4
  • 22
    • 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
  • 23
    • 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
  • 24
    • 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. (1996) Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases, FEBS Lett. 397, 303-307.
    • (1996) FEBS Lett. , vol.397 , pp. 303-307
    • Lübben, M.1    Gerwert, K.2
  • 25
    • 0032876120 scopus 로고    scopus 로고
    • Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy
    • Yamazaki, Y., Kandori, H., and Mogi, T. (1999) Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy, J. Biochem. 126, 194-199.
    • (1999) J. Biochem. , vol.126 , pp. 194-199
    • Yamazaki, Y.1    Kandori, H.2    Mogi, T.3
  • 27
    • 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. (1999) 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, 83-86.
    • (1999) FEBS Lett. , vol.458 , pp. 83-86
    • Hellwig, P.1    Soulimane, T.2    Buse, G.3    Mäntele, W.4
  • 28
    • 0034609560 scopus 로고    scopus 로고
    • FT-IR spectroscopic characterization of NADH: Ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain
    • Hellwig, P., Scheide, D., Bungert, S., Mäntele, W., and Friedrich, T. (2000) FT-IR spectroscopic characterization of NADH: ubiquinone oxidoreductase (complex I) from Escherichia coli: oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain, Biochemistry 39, 10884-10891.
    • (2000) Biochemistry , vol.39 , pp. 10884-10891
    • Hellwig, P.1    Scheide, D.2    Bungert, S.3    Mäntele, W.4    Friedrich, T.5
  • 29
    • 0026454816 scopus 로고
    • 559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: Photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds
    • 559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: Photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds, Biochemistry 31, 11460-11471.
    • (1992) Biochemistry , vol.31 , pp. 11460-11471
    • Berthomieu, C.1    Boussac, A.2    Mäntele, W.3    Breton, J.4    Nabedryk, E.5
  • 31
    • 0142126718 scopus 로고    scopus 로고
    • 1 complex from Paracoccus denitrificans: Evidence for protonation reactions coupled to quinone binding
    • 1 complex from Paracoccus denitrificans: Evidence for protonation reactions coupled to quinone binding, Biochemistry 42, 12391-12399.
    • (2003) Biochemistry , vol.42 , pp. 12391-12399
    • Ritter, M.1    Anderka, O.2    Ludwig, B.3    Mäntele, W.4    Hellwig, P.5
  • 32
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh, E., Raussens, V., and Ruysschaert, J.-M. (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes, Biochim. Biophys. Acta 1422, 105-185.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 34
    • 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
  • 35
    • 0027190929 scopus 로고
    • Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: Evidence for specific protein structural changes upon desensitization
    • Baenziger, J. E., Miller, K. W., and Rothschild, K. J. (1993) Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: evidence for specific protein structural changes upon desensitization, Biochemistry 32, 5448-5454.
    • (1993) Biochemistry , vol.32 , pp. 5448-5454
    • Baenziger, J.E.1    Miller, K.W.2    Rothschild, K.J.3
  • 36
    • 0037154106 scopus 로고    scopus 로고
    • Attenuated total reflection Fourier transform infrared studies of redox changes in bovine cytochrome c oxidase: Resolution of the redox Fourier transform infrared difference spectrum of heme a3
    • Rich, P. R., and Breton, J. (2002) Attenuated total reflection Fourier transform infrared studies of redox changes in bovine cytochrome c oxidase: Resolution of the redox Fourier transform infrared difference spectrum of heme a3, Biochemistry 41, 967-973.
    • (2002) Biochemistry , vol.41 , pp. 967-973
    • Rich, P.R.1    Breton, J.2
  • 37
    • 0035823117 scopus 로고    scopus 로고
    • Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy
    • Nyquist, R. M., Heitbrink, D., Bolwien, C., Wells, T. A., Gennis, R., and Heberle, J. (2001) Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy, FEBS Lett. 505, 63-67.
    • (2001) FEBS Lett. , vol.505 , pp. 63-67
    • Nyquist, R.M.1    Heitbrink, D.2    Bolwien, C.3    Wells, T.A.4    Gennis, R.5    Heberle, J.6
  • 39
    • 0035992560 scopus 로고    scopus 로고
    • Attenuated total reflection Fourier transform infrared spectroscopy of redox transitions in photosynthetic reaction centers: Comparison of perfusion- and light-induced difference spectra
    • Iwaki, M., Andrianambinintsoa, S., Rich, P. R., and Breton, J. (2002) Attenuated total reflection Fourier transform infrared spectroscopy of redox transitions in photosynthetic reaction centers: comparison of perfusion- and light-induced difference spectra, Spectrochim. Acta Part A 58, 1523-1533.
    • (2002) Spectrochim. Acta Part A , vol.58 , pp. 1523-1533
    • Iwaki, M.1    Andrianambinintsoa, S.2    Rich, P.R.3    Breton, J.4
  • 42
    • 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
  • 43
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P. K., and Long, F. A. (1960) Use of glass electrodes to measure acidities in deuterium oxide, J. Phys. Chem. 64, 188-190.
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 44
    • 0031972563 scopus 로고    scopus 로고
    • Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups
    • Rath, P., DeGrip, W. J., and Rothschild, K. J. (1998) Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups, Biophys. J. 74, 192-198.
    • (1998) Biophys. J. , vol.74 , pp. 192-198
    • Rath, P.1    DeGrip, W.J.2    Rothschild, K.J.3
  • 45
    • 0018787864 scopus 로고
    • Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties
    • Takamiya, K., and Dutton, P. L. (1979) Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties, Biochim. Biophys. Acta 546, 1-16.
    • (1979) Biochim. Biophys. Acta , vol.546 , pp. 1-16
    • Takamiya, K.1    Dutton, P.L.2
  • 46
    • 0014843976 scopus 로고
    • The reaction of antimycin with a cytochrome b preparation active in reconstitution of the respiratory chain
    • Berden, J. A., and Slater, E. C. (1970) The reaction of antimycin with a cytochrome b preparation active in reconstitution of the respiratory chain, Biochim. Biophys. Acta 216, 237-249.
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 237-249
    • Berden, J.A.1    Slater, E.C.2
  • 47
    • 0019206273 scopus 로고
    • The interrelation of the two c-type cytochromes in Rhodopseudomonas sphaeroides photosynthesis
    • Wood, P. M. (1980) The interrelation of the two c-type cytochromes in Rhodopseudomonas sphaeroides photosynthesis, Biochem. J. 192, 761-764.
    • (1980) Biochem. J. , vol.192 , pp. 761-764
    • Wood, P.M.1
  • 49
    • 0001059223 scopus 로고
    • Electrochemical and infrared-spectroscopic characterization of redox reactions of p-quinones
    • Bauscher, M., and Mäntele, W. (1992) Electrochemical and infrared-spectroscopic characterization of redox reactions of p-quinones, J. Phys. Chem. 96, 11101-11108.
    • (1992) J. Phys. Chem. , vol.96 , pp. 11101-11108
    • Bauscher, M.1    Mäntele, W.2
  • 50
    • 0001465954 scopus 로고
    • FTIR spectroscopy of UV-generated quinone radicals: Evidence for an intramolecular hydrogen atom transfer in ubiquinone, naphthoquinone, and plastoquinone
    • Burie, J.-R., Boussac, A., Boullais, C., Berger, G., Mattioli, T., Mioskowski, C., Nabedryk, E., and Breton, J. (1995) FTIR spectroscopy of UV-generated quinone radicals: Evidence for an intramolecular hydrogen atom transfer in ubiquinone, naphthoquinone, and plastoquinone, J. Phys. Chem. 99, 4059-4070.
    • (1995) J. Phys. Chem. , vol.99 , pp. 4059-4070
    • Burie, J.-R.1    Boussac, A.2    Boullais, C.3    Berger, G.4    Mattioli, T.5    Mioskowski, C.6    Nabedryk, E.7    Breton, J.8
  • 51
    • 0025054951 scopus 로고
    • Investigation of models for photosynthetic electron acceptors: Infrared spectroelectrochemistry of ubiquinone and its anions
    • Bauscher, M., Nabedryk, E., Bagley, K., Breton, J., and Mäntele, W. (1990) Investigation of models for photosynthetic electron acceptors: Infrared spectroelectrochemistry of ubiquinone and its anions, FEBS Lett. 261, 191-195.
    • (1990) FEBS Lett. , vol.261 , pp. 191-195
    • Bauscher, M.1    Nabedryk, E.2    Bagley, K.3    Breton, J.4    Mäntele, W.5
  • 53
    • 0038670109 scopus 로고    scopus 로고
    • (Amesz, J., and Hoff, A. J., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Mäntele, W. (1996) in Biophysical Techniques in Photosynthesis (Amesz, J., and Hoff, A. J., Eds.) pp 137-160, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Biophysical Techniques in Photosynthesis , pp. 137-160
    • Mäntele, W.1
  • 54
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth, A. (2000) The infrared absorption of amino acid side chains, Prog. Biophys. Mol. Biol. 74, 141-173.
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 56
    • 0037061931 scopus 로고    scopus 로고
    • Ab initio density functional theory calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes
    • Hasegawa, K., Ono, T.-A., and Noguchi, T. (2002) Ab initio density functional theory calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes, J. Phys. Chem. A 106, 3377-3390.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 3377-3390
    • Hasegawa, K.1    Ono, T.-A.2    Noguchi, T.3
  • 57
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L. R., Muga, A., Castresana, J., and Goñi, F. M. (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy, Prog. Biophys. Mol. Biol. 59, 23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 59
    • 0035799313 scopus 로고    scopus 로고
    • B pocket studied by Fourier transform infrared spectroscopy
    • B pocket studied by Fourier transform infrared spectroscopy, Biochemistry 40, 4044-4052.
    • (2001) Biochemistry , vol.40 , pp. 4044-4052
    • Berthomieu, C.1    Hienerwadel, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.