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Volumn 1817, Issue 4, 2012, Pages 579-589

Structural studies on bovine heart cytochrome c oxidase

Author keywords

Bovine cytochrome c oxidase; Hemoproteins; Membrane proteins; O 2 reduction; Proton pump; X ray structural analyses

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; FORMIC ACID; HEMOPROTEIN; MEMBRANE PROTEIN; OXYGEN; OXYGEN DERIVATIVE; PHOSPHOLIPID; PROPIONIC ACID; PROTON PUMP; TRIACYLGLYCEROL;

EID: 84857923810     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.12.012     Document Type: Review
Times cited : (49)

References (37)
  • 1
    • 0002122748 scopus 로고
    • Isolierung der a-Komponente des Cytochroms und ihre Eigenschaften
    • E. Yakushiji, and K. Okunuki Isolierung der a-Komponente des Cytochroms und ihre Eigenschaften Proc. Imp. Acad. Jpn. 17 1941 38 40
    • (1941) Proc. Imp. Acad. Jpn. , vol.17 , pp. 38-40
    • Yakushiji, E.1    Okunuki, K.2
  • 8
    • 0020055171 scopus 로고
    • Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidase
    • N.C. Robinson Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidase Biochemistry 21 1982 184 188
    • (1982) Biochemistry , vol.21 , pp. 184-188
    • Robinson, N.C.1
  • 9
    • 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 physiological pH
    • G. Gilderson, L. Salomonson, 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 physiological pH Biochemistry 42 2003 7400 7409
    • (2003) Biochemistry , vol.42 , pp. 7400-7409
    • Gilderson, G.1    Salomonson, L.2    Aagaard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 11
    • 32944480421 scopus 로고    scopus 로고
    • Absolute configuration of the hydroxy-farnesylethyl group of heme A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using a novel method applicable at 2.8 Å resolution
    • E. Yamashita, H. Aoyama, M. Yao, K. Muramoto, K. Shinzawa-Itoh, S. Yoshikawa, and T. Tsukihara Absolute configuration of the hydroxy-farnesylethyl group of heme A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using a novel method applicable at 2.8 Å resolution Acta Crystallogr. D61 2005 1373 1377
    • (2005) Acta Crystallogr. , vol.61 D , pp. 1373-1377
    • Yamashita, E.1    Aoyama, H.2    Yao, M.3    Muramoto, K.4    Shinzawa-Itoh, K.5    Yoshikawa, S.6    Tsukihara, T.7
  • 12
    • 27844524873 scopus 로고    scopus 로고
    • Oxygen activation mechanism at the binuclear site of heme-copper oxidase superfamily as revealed by time-resolved resonance Raman spectroscopy
    • T. Kitagawa, and T. Ogura Oxygen activation mechanism at the binuclear site of heme-copper oxidase superfamily as revealed by time-resolved resonance Raman spectroscopy Prog. Inorg. Chem. 45 1997 431 479
    • (1997) Prog. Inorg. Chem. , vol.45 , pp. 431-479
    • Kitagawa, T.1    Ogura, T.2
  • 15
    • 0020490364 scopus 로고
    • B in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures
    • B in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures J. Biol. Chem. 257 1982 1639 1650
    • (1982) J. Biol. Chem. , vol.257 , pp. 1639-1650
    • Fiamingo, F.G.1    Altshuld, R.A.2    Moh, P.P.3    Alben, J.O.4
  • 19
    • 0024286159 scopus 로고
    • The possible role of the closed-open transition in proton pumping by cytochrome c oxidase:The pH dependence of cyanide inhibition
    • P.E. Thornstrom, T. Nilsson, and B.G. Malmstrom The possible role of the closed-open transition in proton pumping by cytochrome c oxidase:The pH dependence of cyanide inhibition Biochim. Biophys. Acta 935 1988 103 108
    • (1988) Biochim. Biophys. Acta , vol.935 , pp. 103-108
    • Thornstrom, P.E.1    Nilsson, T.2    Malmstrom, B.G.3
  • 20
    • 0033585006 scopus 로고    scopus 로고
    • Quantitative reevaluation of the redox active sites of crystalline bovine heart cytochrome c oxidase
    • M. Mochizuki, H. Aoyama, K. Shinzawa-Itoh, T. Usui, T. Tsukihara, and S. Yoshikawa Quantitative reevaluation of the redox active sites of crystalline bovine heart cytochrome c oxidase J. Biol. Chem. 274 1999 33403 33411
    • (1999) J. Biol. Chem. , vol.274 , pp. 33403-33411
    • Mochizuki, M.1    Aoyama, H.2    Shinzawa-Itoh, K.3    Usui, T.4    Tsukihara, T.5    Yoshikawa, S.6
  • 22
    • 77954423532 scopus 로고    scopus 로고
    • A resonance Raman band assignable to the O-O stretching mode in the resting oxidized state of bovine heart cytochrome c oxidase
    • M. Sakaguchi, K. Shinzawa-Itoh, S. Yoshikawa, and T. Ogura A resonance Raman band assignable to the O-O stretching mode in the resting oxidized state of bovine heart cytochrome c oxidase J. Bioenerg. Biomembr. 42 2010 241 243
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 241-243
    • Sakaguchi, M.1    Shinzawa-Itoh, K.2    Yoshikawa, S.3    Ogura, T.4
  • 23
    • 0035918563 scopus 로고    scopus 로고
    • Cyanide stimulated dissociation of chloride from the catalytic center of oxidized cytochrome c oxidase
    • M. Fabian, L. Skultety, C. Brunel, and G. Palmer Cyanide stimulated dissociation of chloride from the catalytic center of oxidized cytochrome c oxidase Biochemistry 40 2001 6061 6069
    • (2001) Biochemistry , vol.40 , pp. 6061-6069
    • Fabian, M.1    Skultety, L.2    Brunel, C.3    Palmer, G.4
  • 26
    • 0000540212 scopus 로고
    • Proton exchange in amides: Surprise from single systems
    • C.L. Perrin Proton exchange in amides: surprise from single systems Acc. Chem. Res. 22 1989 268 275
    • (1989) Acc. Chem. Res. , vol.22 , pp. 268-275
    • Perrin, C.L.1
  • 27
    • 34547794301 scopus 로고    scopus 로고
    • Possible mechanism of proton transfer through peptide groups in the H-pathway of the bovine cytochrome c oxidase
    • K. Kamiya, M. Boero, M. Tateno, K. Shiraishi, and A. Oshiyama 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
  • 28
    • 0024522067 scopus 로고
    • Cytochrome c oxidase: Evidence for interaction of water molecules with cytochrome a
    • M. Sasaroli, Y.-C. Ching, S. Dasgupta, and D.L. Rousseau Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a Biochemistry 28 1989 3128 3132
    • (1989) Biochemistry , vol.28 , pp. 3128-3132
    • Sasaroli, M.1    Ching, Y.-C.2    Dasgupta, S.3    Rousseau, D.L.4
  • 30
    • 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. 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.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 32
    • 0035903013 scopus 로고    scopus 로고
    • 2 + binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfers and proton translocation
    • 2 + binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfers and proton translocation FEBS Lett. 503 2001 142 146
    • (2001) FEBS Lett. , vol.503 , pp. 142-146
    • Kannt, A.1    Ostermann, T.2    Muller, H.3    Ruitenberg, M.4
  • 33
    • 79960519978 scopus 로고    scopus 로고
    • Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side
    • P.L. Martino, G. Capitanio, N. Capitanio, and S. Papa Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side Biochim. Biophys. Acta 1807 2011 1075 1082
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1075-1082
    • Martino, P.L.1    Capitanio, G.2    Capitanio, N.3    Papa, S.4
  • 34
    • 0029150334 scopus 로고
    • Puropose of proton pathways
    • R.J.P. Williams Puropose of proton pathways Nature 376 1995 643
    • (1995) Nature , vol.376 , pp. 643
    • Williams, R.J.P.1
  • 35
    • 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
    • A.S. Pawate, J. Morgan, A. Namslauer, D. Mills, P. Brzenzinski, 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
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.4    Brzenzinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 36
    • 70349493006 scopus 로고    scopus 로고
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping Proc. Natl. Acad. Sci. U. S. A. 106 2009 16169 16173
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16169-16173
    • Chang, H.Y.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.