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Volumn 1655, Issue 1-3, 2004, Pages 347-352

Time-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: Implications for O2 input and H 2O/H+ output channels

Author keywords

CcO; Cytochrome c oxidase; Fourier transform infrared; FTIR; MCT; Mercury cadmium telluride; Resonance Raman; RR; Time resolved Fourier transform infrared; TR FTIR

Indexed keywords

CYTOCHROME C OXIDASE; HEME OXYGENASE; OXYGEN; WATER;

EID: 1942504432     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.06.004     Document Type: Review
Times cited : (28)

References (28)
  • 2
    • 0025132493 scopus 로고
    • Ferryl and hydroxy intermediates in the reaction of oxygen with reduced cytochrome c oxidase
    • Han S., Ching Y.-C., Rousseau D.L. Ferryl and hydroxy intermediates in the reaction of oxygen with reduced cytochrome c oxidase. Nature. 348:1990;89-90.
    • (1990) Nature , vol.348 , pp. 89-90
    • Han, S.1    Ching, Y.-C.2    Rousseau, D.L.3
  • 3
    • 0034695481 scopus 로고    scopus 로고
    • Time dependence of the catalytic intermediates in cytochrome c oxidase
    • Han S., Takahashi S., Rousseau D.L. Time dependence of the catalytic intermediates in cytochrome c oxidase. J. Biol. Chem. 275:1999;1910-1919.
    • (1999) J. Biol. Chem. , vol.275 , pp. 1910-1919
    • Han, S.1    Takahashi, S.2    Rousseau, D.L.3
  • 4
    • 0029998277 scopus 로고    scopus 로고
    • Time-resolved resonance Raman evidence for tight coupling between electron transfer and proton pumping of cytochrome c oxidase upon the change from the Fe(V) oxidation level to the Fe(IV) oxidation level
    • Ogura T., Hirota S., Proshlyakov D.A., Shinzawa-Itoh K., Yoshikawa S., Kitagawa T. Time-resolved resonance Raman evidence for tight coupling between electron transfer and proton pumping of cytochrome c oxidase upon the change from the Fe(V) oxidation level to the Fe(IV) oxidation level. J. Am. Chem. Soc. 118:1996;5443-5449.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5443-5449
    • Ogura, T.1    Hirota, S.2    Proshlyakov, D.A.3    Shinzawa-Itoh, K.4    Yoshikawa, S.5    Kitagawa, T.6
  • 5
    • 0035977608 scopus 로고    scopus 로고
    • Presence of the heme-oxo intermediate in oxygenation of carbon monoxide by cytochrome c oxidase revealed by resonance Raman spectroscopy
    • Kim Y., Shinzawa-Itoh K., Yoshikawa S., Kitagawa T. Presence of the heme-oxo intermediate in oxygenation of carbon monoxide by cytochrome c oxidase revealed by resonance Raman spectroscopy. J. Am. Chem. Soc. 123:2001;757-758.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 757-758
    • Kim, Y.1    Shinzawa-Itoh, K.2    Yoshikawa, S.3    Kitagawa, T.4
  • 6
    • 0001158908 scopus 로고
    • Time-resolved Raman detection of ν(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase
    • C. Varotsis, W.H. Woodruff, G.T. Babcock, Time-resolved Raman detection of ν(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase, J. Am. Chem. Soc. 111 (1989) 6439-6440, 112 (1990) 1297.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6439-6440
    • Varotsis, C.1    Woodruff, W.H.2    Babcock, G.T.3
  • 7
    • 0025217226 scopus 로고
    • C. Varotsis, W.H. Woodruff, G.T. Babcock, Time-resolved Raman detection of ν(Fe-O) in an early intermediate in the reduction of oxygen by cytochrome oxidase, J. Am. Chem. Soc. 111 (1989) 6439-6440, 112 (1990) 1297.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1297
  • 10
    • 0028857206 scopus 로고
    • Photolytic activity of early intermediates in dioxygen activation and reduction by cytochrome oxidase
    • Varotsis C., Babcock G.T. Photolytic activity of early intermediates in dioxygen activation and reduction by cytochrome oxidase. J. Am. Chem. Soc. 117:1995;11260-11269.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11260-11269
    • Varotsis, C.1    Babcock, G.T.2
  • 12
    • 0037134420 scopus 로고    scopus 로고
    • The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase
    • Pinakoulaki E., Pfitzner U., Ludwig B., Varotsis C. The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase. J. Biol. Chem. 277:2002;13563-13568.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13563-13568
    • Pinakoulaki, E.1    Pfitzner, U.2    Ludwig, B.3    Varotsis, C.4
  • 13
    • 0032514726 scopus 로고    scopus 로고
    • The post-translational modification in cytochrome oxidase is required to establish a functional environment of the catalytic site
    • Das T.K., Pecoraro C., Tomson F.L., Gennis R.B., Rousseau D.L. The post-translational modification in cytochrome oxidase is required to establish a functional environment of the catalytic site. Biochemistry. 37:1998;14471-14476.
    • (1998) Biochemistry , vol.37 , pp. 14471-14476
    • Das, T.K.1    Pecoraro, C.2    Tomson, F.L.3    Gennis, R.B.4    Rousseau, D.L.5
  • 16
    • 0033576974 scopus 로고    scopus 로고
    • Infrared evidence for CuB ligation of photodissociated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein
    • Iwase T., Varotsis C., Shinzawa-Itoh K., Yoshikawa S., Kitagawa T. Infrared evidence for CuB ligation of photodissociated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein. J. Am. Chem. Soc. 121:1999;1415-1416.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1415-1416
    • Iwase, T.1    Varotsis, C.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 18
    • 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    Bowlwien, C.3    Brzezinski, P.4    Heberle, J.5
  • 19
    • 0035967511 scopus 로고    scopus 로고
    • FTIR studies of the CO and cyanide adducts of fully reduced bovine cytochrome c oxidase
    • Rich P.R., Breton J. FTIR studies of the CO and cyanide adducts 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
  • 24
    • 0027308712 scopus 로고
    • Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation
    • Woodruff W.H. Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation. J. Bioenerg. Biomembranes. 25:1993;177-188.
    • (1993) J. Bioenerg. Biomembranes , vol.25 , pp. 177-188
    • Woodruff, W.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.