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Volumn 7, Issue 4, 1997, Pages 574-579

Beef heart cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; HEART ENZYME; PROTON PUMP;

EID: 0030805957     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80124-8     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • 2 reduction with those of [4] will be helpful for considering this intriguing enzyme reaction.
    • 2 reduction with those of [4] will be helpful for considering this intriguing enzyme reaction.
    • (1996) Chem Rev , vol.96 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 2
    • 0001179635 scopus 로고
    • Cytochrome c oxidase as a redox-linked proton pump
    • Malmström BG. Cytochrome c oxidase as a redox-linked proton pump. Chem Rev. 90:1990;1247-1260.
    • (1990) Chem Rev , vol.90 , pp. 1247-1260
    • Malmström, B.G.1
  • 3
    • 0001022291 scopus 로고
    • Über eisen, den sauerstoffübertragenden bestandteil des atmungsfermentes
    • Iron and oxygen transporters of the respiratory system
    • Warburg O. Über eisen, den sauerstoffübertragenden bestandteil des atmungsfermentes. Iron and oxygen transporters of the respiratory system Biochem Z. 152:1924;479-494.
    • (1924) Biochem Z , vol.152 , pp. 479-494
    • Warburg, O.1
  • 4
    • 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
    • 2 reduction mechanism. It includes a well-written introduction of the principles and practice of time-resolved resonance Raman spectroscopy, which is suitable for biochemists not familiar to this technique.
    • 2 reduction mechanism. It includes a well-written introduction of the principles and practice of time-resolved resonance Raman spectroscopy, which is suitable for biochemists not familiar to this technique.
    • (1997) Progr Inorg Chem , vol.45 , pp. 431-479
    • Kitagawa, T.1    Ogura, T.2
  • 7
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, 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
  • 10
    • 0027178231 scopus 로고
    • Stoichiometry and redox behavior of metals in cytochrome-c oxidase
    • Steffens GCM, Soulinane T, Wolff G, Buse G. Stoichiometry and redox behavior of metals in cytochrome-c oxidase. Eur J Biochem. 213:1993;1149-1157.
    • (1993) Eur J Biochem , vol.213 , pp. 1149-1157
    • Steffens, G.C.M.1    Soulinane, T.2    Wolff, G.3    Buse, G.4
  • 11
    • 0024267905 scopus 로고
    • The cupric site in nitrous oxide reductase contains a mixed-valence [Cu(II), Cu(I)] binuclear center: A multifrequency electron paramagnetic resonance investigation
    • Kroneck PMH, Antholine WA, Riester J, Zumft WG. The cupric site in nitrous oxide reductase contains a mixed-valence [Cu(II), Cu(I)] binuclear center: a multifrequency electron paramagnetic resonance investigation. FEBS Lett. 242:1988;70-74.
    • (1988) FEBS Lett , vol.242 , pp. 70-74
    • Kroneck, P.M.H.1    Antholine, W.A.2    Riester, J.3    Zumft, W.G.4
  • 13
    • 0029558330 scopus 로고
    • Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center
    • Wimanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc Natl Acad Sci USA. 92:1995;11955-11959.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11955-11959
    • Wimanns, M.1    Lappalainen, P.2    Kelly, M.3    Sauer-Eriksson, E.4    Saraste, M.5
  • 14
    • 0027406438 scopus 로고
    • Tissue-specific regulation of bovine heart cytochrome-c oxidase activity by ADP via interaction with subunit VIa
    • Anthony G, Reimann A, Kadenbach B. Tissue-specific regulation of bovine heart cytochrome-c oxidase activity by ADP via interaction with subunit VIa. Proc Natl Acad Sci USA. 90:1993;1652-1656.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1652-1656
    • Anthony, G.1    Reimann, A.2    Kadenbach, B.3
  • 15
    • 0029670481 scopus 로고    scopus 로고
    • - stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios
    • - stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios. FEBS Lett. 382:1996;121-124.
    • (1996) FEBS Lett , vol.382 , pp. 121-124
    • Frank, V.1    Kadenbach, B.2
  • 17
    • 0040546072 scopus 로고
    • The iron-sulfur proteins: An overview
    • H. Matsubara, Y. Katsube, Wada K. Berlin: Springer-Verlag
    • Jensen LH. The iron-sulfur proteins: an overview. Matsubara H, Katsube Y, Wada K. Iron-Sulfur Protein Research. 1986;3-21 Springer-Verlag, Berlin.
    • (1986) Iron-Sulfur Protein Research , pp. 3-21
    • Jensen, L.H.1
  • 19
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • Calhoun MW, Thomas JW, Gennis RB. 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
  • 20
    • 0027993918 scopus 로고
    • Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase
    • Hill BC. Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase. J Biol Chem. 269:1994;2419-2425.
    • (1994) J Biol Chem , vol.269 , pp. 2419-2425
    • Hill, B.C.1
  • 22
    • 85023498412 scopus 로고
    • Time-resolved resonance Raman investigation of cytochrome oxidase catalysis: Observation of a new oxygen-isotope sensitive Raman band
    • Ogura T, Takahashi S, Shinzawa-Itoh K, Yoshikawa S, Kitagawa T. Time-resolved resonance Raman investigation of cytochrome oxidase catalysis: observation of a new oxygen-isotope sensitive Raman band. Bull Chem Soc Jpn. 64:1991;2901-2907.
    • (1991) Bull Chem Soc Jpn , vol.64 , pp. 2901-2907
    • Ogura, T.1    Takahashi, S.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 24
    • 0004009372 scopus 로고
    • Chemistry of the transition elements, copper
    • edn 4 New York: John Wiley Sons
    • Cotton FA, Wilkinson G. Chemistry of the transition elements, copper. edn 4 Advanced Inorganic Chemistry. 1980;798-821 John Wiley Sons, New York.
    • (1980) Advanced Inorganic Chemistry , pp. 798-821
    • Cotton, F.A.1    Wilkinson, G.2
  • 25
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • Verkhovsky MI, Morgan JE, Wikström M. Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. Biochemistry. 33:1994;3079-3086.
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 26
    • 0000659133 scopus 로고
    • Resonance Raman spectra of highly oxidized metalloporphyrins and heme proteins
    • Kitagawa T, Mizutani Y. Resonance Raman spectra of highly oxidized metalloporphyrins and heme proteins. Coordination Chem Rev. 135/136:1994;685-735.
    • (1994) Coordination Chem Rev , vol.135-136 , pp. 685-735
    • Kitagawa, T.1    Mizutani, Y.2
  • 29
    • 0030220806 scopus 로고    scopus 로고
    • Cytochrome c oxidase
    • of special interest. A summary of the crystal structure of the bacterial enzyme and a discussion of the reaction mechanism.
    • Ostermeier C, Iwata S, Michel H. Cytochrome c oxidase. of special interest Curr Opin Struct Biol. 6:1996;460-466 A summary of the crystal structure of the bacterial enzyme and a discussion of the reaction mechanism.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 460-466
    • Ostermeier, C.1    Iwata, S.2    Michel, H.3
  • 30
    • 0029150334 scopus 로고
    • Purpose of proton pathways
    • Williams RJP. Purpose of proton pathways. Nature. 376:1995;643.
    • (1995) Nature , vol.376 , pp. 643
    • Williams, R.J.P.1
  • 31
    • 0029884379 scopus 로고    scopus 로고
    • Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy
    • of special interest. This is the first report showing redox-linked conformational and/or protonation changes of the carboxyl group of glutamate or aspartate. This finding may promote the real-time measurement of proton pump behavior.
    • Hellwig P, Rost B, Kaiser U, Ostermeier C, Michel H, Mäntele W. Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy. of special interest FEBS Lett. 385:1996;53-57 This is the first report showing redox-linked conformational and/or protonation changes of the carboxyl group of glutamate or aspartate. This finding may promote the real-time measurement of proton pump behavior.
    • (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
  • 32
    • 0029897391 scopus 로고    scopus 로고
    • Redox-linked conformational changes in cytochrome c oxidase
    • Wittung P, Malmström BG. Redox-linked conformational changes in cytochrome c oxidase. FEBS Lett. 388:1996;47-49.
    • (1996) FEBS Lett , vol.388 , pp. 47-49
    • Wittung, P.1    Malmström, B.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.