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Volumn 1555, Issue 1-3, 2002, Pages 116-121

ATR-FTIR difference spectroscopy of the PM intermediate of bovine cytochrome c oxidase

Author keywords

Cytochrome c oxidase; FTIR spectroscopy; Intermediate

Indexed keywords

BUFFER; CARBON DIOXIDE; CHEMICAL COMPOUND; CYTOCHROME C OXIDASE; DETERGENT; HEME DERIVATIVE; OXYGEN; PROTEIN;

EID: 0037056003     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(02)00265-7     Document Type: Article
Times cited : (35)

References (49)
  • 2
    • 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
  • 3
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock G.T., 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
  • 4
    • 0039242661 scopus 로고
    • Energy-dependent reversal of the cytochrome oxidase reaction
    • Wikström M. Energy-dependent reversal of the cytochrome oxidase reaction. Proc. Natl. Acad. Sci. USA. 78:1981;4051-4054.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4051-4054
    • Wikström, M.1
  • 5
    • 0026671804 scopus 로고
    • The dioxygen cycle. Spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction
    • Wikström M., Morgan J.E. The dioxygen cycle. Spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction. J. Biol. Chem. 267:1992;10266-10273.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10266-10273
    • Wikström, M.1    Morgan, J.E.2
  • 6
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • Morgan J.E., Verkhovsky M.I., Wikström M. Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase. Biochemistry. 35:1996;12235-12240.
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 7
    • 0031031990 scopus 로고    scopus 로고
    • Mechanism of cytochrome c oxidase-catalysed reduction of dioxygen to water: Evidence for peroxy and ferryl intermediates at room temperature
    • Sucheta A., Georgiadis K.E., Einarsdóttir O. Mechanism of cytochrome c oxidase-catalysed reduction of dioxygen to water: evidence for peroxy and ferryl intermediates at room temperature. Biochemistry. 36:1997;554-565.
    • (1997) Biochemistry , vol.36 , pp. 554-565
    • Sucheta, A.1    Georgiadis, K.E.2    Einarsdóttir, O.3
  • 11
    • 0029926483 scopus 로고    scopus 로고
    • Redox transitions between oxygen intermediates in cytochrome-c oxidase
    • Verkhovsky M.I., Morgan J.E., Wikström M. Redox transitions between oxygen intermediates in cytochrome-c oxidase. Proc. Natl. Acad. Sci. USA. 93:1996;12235-12239.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12235-12239
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 12
    • 0028263983 scopus 로고
    • Cytochrome bo from Escherichia coli: Reaction of the oxidized enzyme with hydrogen peroxide
    • Watmough N.J., Cheesman M.R., Greenwood C., Thomson A.J. Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide. Biochem. J. 300:1994;469-475.
    • (1994) Biochem. J. , vol.300 , pp. 469-475
    • Watmough, N.J.1    Cheesman, M.R.2    Greenwood, C.3    Thomson, A.J.4
  • 13
    • 0028139015 scopus 로고
    • Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide
    • Proshlyakov D.A., Ogura T., Shinzawa-Itoh K., Yoshikawa S., Appelman E.H., Kitagawa T. Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide. J. Biol. Chem. 269:1994;29385-29388.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29385-29388
    • Proshlyakov, D.A.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Appelman, E.H.5    Kitagawa, T.6
  • 14
    • 0030047099 scopus 로고    scopus 로고
    • Microcirculating system for simultaneous determination of Raman and absorption spectra of enzymatic reaction intermediates and its application to the reaction of cytochrome c oxidase with hydrogen peroxide
    • Proshlyakov D.A., Ogura T., Shinzawa-Itoh K., Yoshikawa S., Kitagawa T. Microcirculating system for simultaneous determination of Raman and absorption spectra of enzymatic reaction intermediates and its application to the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry. 35:1996;76-82.
    • (1996) Biochemistry , vol.35 , pp. 76-82
    • Proshlyakov, D.A.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 16
    • 0033539479 scopus 로고    scopus 로고
    • Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase
    • Fabian M., Wong W.W., Gennis R.B., Palmer G. Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proc. Natl. Acad. Sci. USA. 96:1999;13114-13117.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13114-13117
    • Fabian, M.1    Wong, W.W.2    Gennis, R.B.3    Palmer, G.4
  • 17
    • 0028851789 scopus 로고
    • The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F
    • Fabian M., Palmer G. The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F. Biochemistry. 34:1995;13802-13810.
    • (1995) Biochemistry , vol.34 , pp. 13802-13810
    • Fabian, M.1    Palmer, G.2
  • 18
    • 0033545832 scopus 로고    scopus 로고
    • Redox state of peroxy and ferryl intermediates in cytochrome c oxidase catalysis
    • Fabian M., Palmer G. Redox state of peroxy and ferryl intermediates in cytochrome c oxidase catalysis. Biochemistry. 38:1999;6270-6275.
    • (1999) Biochemistry , vol.38 , pp. 6270-6275
    • Fabian, M.1    Palmer, G.2
  • 19
    • 0016709349 scopus 로고
    • Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen
    • Chance B., Saronio C., Leigh J.S. Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen. J. Biol. Chem. 250:1975;9226-9237.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9226-9237
    • Chance, B.1    Saronio, C.2    Leigh, J.S.3
  • 20
    • 0019878443 scopus 로고
    • 3 with oxygen and carbon monoxide. The role of the 607 nm complex
    • 3 with oxygen and carbon monoxide. The role of the 607 nm complex. Biochim. Biophys. Acta. 634:1981;256-265.
    • (1981) Biochim. Biophys. Acta , vol.634 , pp. 256-265
    • Nicholls, P.1    Chanady, G.A.2
  • 21
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • Verkhovsky M.I., Morgan J.E., 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
  • 22
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: Investigation of the oxygen reaction in the R. sphaeroides enzyme
    • Ädelroth P., Ek M., Brzezinski P. Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme. Biochim. Biophys. Acta. 1367:1998;107-117.
    • (1998) Biochim. Biophys. Acta , vol.1367 , pp. 107-117
    • Ädelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 23
    • 0032558999 scopus 로고    scopus 로고
    • Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen
    • Sucheta A., Szundi I., Einarsdóttir O. Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry. 37:1998;17905-17914.
    • (1998) Biochemistry , vol.37 , pp. 17905-17914
    • Sucheta, A.1    Szundi, I.2    Einarsdóttir, O.3
  • 24
    • 0034727649 scopus 로고    scopus 로고
    • Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer
    • Karpefors M., Ädelroth P., Namslauer A., Zhen Y., Brzezinski P. Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer. Biochemistry. 39:2000;14664-14669.
    • (2000) Biochemistry , vol.39 , pp. 14664-14669
    • Karpefors, M.1    Ädelroth, P.2    Namslauer, A.3    Zhen, Y.4    Brzezinski, P.5
  • 28
    • 0036648089 scopus 로고    scopus 로고
    • Radicals associated with the catalytic intermediates of bovine cytochrome c oxidase
    • Rich P.R., Rigby S.E.J., Heathcote P. Radicals associated with the catalytic intermediates of bovine cytochrome c oxidase. Biochim. Biophys. Acta. 1554:2002;137-146.
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 137-146
    • Rich, P.R.1    Rigby, S.E.J.2    Heathcote, P.3
  • 29
    • 0025772795 scopus 로고
    • Characterisation of 'fast' and 'slow' forms of bovine heart cytochrome-c oxidase
    • Moody A.J., Cooper C.E., Rich P.R. Characterisation of 'fast' and 'slow' forms of bovine heart cytochrome-c oxidase. Biochim. Biophys. Acta. 1059:1991;189-207.
    • (1991) Biochim. Biophys. Acta , vol.1059 , pp. 189-207
    • Moody, A.J.1    Cooper, C.E.2    Rich, P.R.3
  • 31
    • 0035967511 scopus 로고    scopus 로고
    • FTIR studies of the CO and cyanide compounds of fully reduced bovine cytochrome c oxidase
    • Rich P.R., 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
  • 32
    • 0023787959 scopus 로고
    • The site and mechanism of dioxygen reduction in bovine heart cytochrome c oxidase
    • Einarsdóttir O., Choc M.G., Weldon S., Caughey W.S. The site and mechanism of dioxygen reduction in bovine heart cytochrome c oxidase. J. Biol. Chem. 263:1988;13641-13654.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13641-13654
    • Einarsdóttir, O.1    Choc, M.G.2    Weldon, S.3    Caughey, W.S.4
  • 34
    • 0029657964 scopus 로고    scopus 로고
    • B binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy
    • B binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy. Biophys. J. 71:1996;1036-1047.
    • (1996) Biophys. J. , vol.71 , pp. 1036-1047
    • Park, S.1    Pan, L.P.2    Chan, S.I.3    Alben, J.O.4
  • 35
    • 0030573678 scopus 로고    scopus 로고
    • 'As prepared' forms of fully oxidised haem/Cu terminal oxidases
    • Moody A.J. 'As prepared' forms of fully oxidised haem/Cu terminal oxidases. Biochim. Biophys. Acta. 1276:1996;6-20.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 6-20
    • Moody, A.J.1
  • 37
    • 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., 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
  • 38
    • 0025823074 scopus 로고
    • Vibrational structure of the formyl group on heme a. Implications on the properties of cytochrome c oxidase
    • Han S., Ching Y., Hammes S.L., Rousseau D.L. Vibrational structure of the formyl group on heme a. Implications on the properties of cytochrome c oxidase. Biophys. J. 60:1991;45-52.
    • (1991) Biophys. J. , vol.60 , pp. 45-52
    • Han, S.1    Ching, Y.2    Hammes, S.L.3    Rousseau, D.L.4
  • 39
    • 0001173024 scopus 로고
    • Resonance Raman and electronic spectra of heme a complexes of cytochrome oxidase
    • Choi S., Lee J.J., Wei Y.H., Spiro T.G. Resonance Raman and electronic spectra of heme a complexes of cytochrome oxidase. J. Am. Chem. Soc. 105:1983;3692-3707.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3692-3707
    • Choi, S.1    Lee, J.J.2    Wei, Y.H.3    Spiro, T.G.4
  • 44
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping - A discussion
    • Michel H. Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping - a discussion. Biochemistry. 38:1999;15129-15140.
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 45
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • Proshlyakov D.A., Pressler M.A., DeMaso C., Leykam J.F., DeWitt D.L., Babcock G.T. Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244. Science. 290:2000;1588-1591.
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    DeMaso, C.3    Leykam, J.F.4    DeWitt, D.L.5    Babcock, G.T.6
  • 46
    • 0034612367 scopus 로고    scopus 로고
    • Resonance Raman studies of oxo intermediates in the reaction of pulsed cytochrome bo with hydrogen peroxide
    • Uchida T., Mogi T., Kitagawa T. Resonance Raman studies of oxo intermediates in the reaction of pulsed cytochrome bo with hydrogen peroxide. Biochemistry. 39:2000;6669-6678.
    • (2000) Biochemistry , vol.39 , pp. 6669-6678
    • Uchida, T.1    Mogi, T.2    Kitagawa, T.3
  • 47
    • 0037094081 scopus 로고    scopus 로고
    • Spectroscopic properties of tyrosyl radicals in dipeptides
    • Ayala I., Rangel K., York D., Barry B.A. Spectroscopic properties of tyrosyl radicals in dipeptides. J. Am. Chem. Soc. 124:2002;5496-5505.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5496-5505
    • Ayala, I.1    Rangel, K.2    York, D.3    Barry, B.A.4
  • 49
    • 0037061951 scopus 로고    scopus 로고
    • 244 of bovine cytochrome c oxidase in its neutral, deprotonated anoionic, and deprotonated neutral radical forms: Effects of covalent binding between tyrosine and histidine
    • 244 of bovine cytochrome c oxidase in its neutral, deprotonated anoionic, and deprotonated neutral radical forms: effects of covalent binding between tyrosine and histidine. J. Phys. Chem. A. 106:2002;3436-3444.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 3436-3444
    • Aki, M.1    Ogura, T.2    Naruta, Y.3    Le, T.H.4    Sato, T.5    Kitagawa, T.6


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