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Volumn 1807, Issue 9, 2011, Pages 1162-1169

Time-resolved single-turnover of caa3 oxidase from Thermus thermophilus. Fifth electron of the fully reduced enzyme converts OH into EH state

Author keywords

Catalytic cycle intermediates; Cytochrome c oxidase; Electron transfer; Thermus thermophilus

Indexed keywords

CAA3 OXIDASE; COPPER; CYTOCHROME C OXIDASE; UNCLASSIFIED DRUG;

EID: 80955180551     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.05.006     Document Type: Article
Times cited : (14)

References (71)
  • 1
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • S. Ferguson-Miller, and G.T. Babcock Heme/copper terminal oxidases Chem. Rev. 7 1996 2889 2907 (Pubitemid 126641120)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 2
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M.K. Wikström Proton pump coupled to cytochrome c oxidase in mitochondria Nature 266 1977 271 273 (Pubitemid 8071433)
    • (1977) Nature , vol.266 , Issue.5599 , pp. 271-273
    • Wikstrom, M.K.F.1
  • 3
    • 0020984324 scopus 로고
    • 2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature
    • 2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature Biochem. J. 215 1983 659 667
    • (1983) Biochem. J. , vol.215 , pp. 659-667
    • Hill, B.C.1    Greenwood, C.2
  • 4
    • 0024408677 scopus 로고
    • The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen
    • DOI 10.1016/S0005-2728(89)80087-8
    • M. Oliveberg, P. Brzezinski, and B.G. Malmström The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen Biochim. Biophys. Acta 977 1989 322 328 (Pubitemid 20004624)
    • (1989) Biochimica et Biophysica Acta - Bioenergetics , vol.977 , Issue.3 , pp. 322-328
    • Oliveberg, M.1    Brzezinski, P.2    Malmstrom, B.G.3
  • 5
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • M.I. Verkhovsky, J.E. Morgan, and M. Wikström Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase Biochemistry 33 1994 3079 3086 (Pubitemid 24103371)
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikstrom, M.3
  • 7
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • DOI 10.1021/bi961634e
    • J.E. Morgan, M.I. Verkhovsky, and M. Wikström Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase Biochemistry 35 1996 12235 12240 (Pubitemid 26331244)
    • (1996) Biochemistry , vol.35 , Issue.38 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikstrom, M.3
  • 8
    • 0032558999 scopus 로고    scopus 로고
    • Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen
    • DOI 10.1021/bi981092w
    • A. Sucheta, I. Szundi, and O. Einarsdottir Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen Biochemistry 37 1998 17905 17914 (Pubitemid 29023946)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17905-17914
    • Sucheta, A.1    Szundi, I.2    Einarsdottir, O.3
  • 9
    • 0021763113 scopus 로고
    • The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature
    • B.C. Hill, and C. Greenwood The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature Biochem. J. 218 1984 913 921
    • (1984) Biochem. J. , vol.218 , pp. 913-921
    • Hill, B.C.1    Greenwood, C.2
  • 10
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation
    • I.A. Smirnova, P. Ädelroth, R.B. Gennis, and P. Brzezinski Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation Biochemistry 38 1999 6826 6833
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 11
    • 0037452497 scopus 로고    scopus 로고
    • Intramolecular proton-transfer reactions in a membrane-bound proton pump: The effect of pH on the peroxy to ferryl transition in cytochrome c oxidase
    • DOI 10.1021/bi026524o
    • A. Namslauer, A. Aagaard, A. Katsonouri, and P. Brzezinski Intramolecular proton-transfer reactions in a membrane-bound proton pump: the effect of pH on the peroxy to ferryl transition in cytochrome c oxidase Biochemistry 42 2003 1488 1498 (Pubitemid 36205955)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 12
    • 36049009410 scopus 로고    scopus 로고
    • Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans
    • DOI 10.1021/bi701614w
    • E.A. Gorbikova, N.P. Belevich, M. Wikström, and M.I. Verkhovsky Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans Biochemistry 46 2007 13141 13148 (Pubitemid 350086232)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13141-13148
    • Gorbikova, E.A.1    Belevich, N.P.2    Wikstrom, M.3    Verkhovsky, M.I.4
  • 13
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel 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
  • 14
    • 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.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.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 15
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • DOI 10.1074/jbc.M407549200
    • S.A. Siletsky, A.S. Pawate, K. Weiss, R.B. Gennis, and A.A. Konstantinov Transmembrane charge separation during the ferryl-oxo - > oxidized transition in a nonpumping mutant of cytochrome c oxidase J. Biol. Chem. 279 2004 52558 52565 (Pubitemid 39656632)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2    Weiss, K.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 16
    • 77950646226 scopus 로고    scopus 로고
    • Partial steps of charge translocation in the nonpumping N139L mutant of Rhodobacter sphaeroides cytochrome c oxidase with a blocked D-Channel
    • S.A. Siletsky, J. Zhu, R.B. Gennis, and A.A. Konstantinov Partial steps of charge translocation in the nonpumping N139L mutant of Rhodobacter sphaeroides cytochrome c oxidase with a blocked D-Channel Biochemistry 49 2010 3060 3073
    • (2010) Biochemistry , vol.49 , pp. 3060-3073
    • Siletsky, S.A.1    Zhu, J.2    Gennis, R.B.3    Konstantinov, A.A.4
  • 22
    • 33750036104 scopus 로고    scopus 로고
    • Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and 'activated' by reoxidation
    • DOI 10.1074/jbc.M605955200
    • D. Jancura, V. Berka, M. Antalik, J. Bagelova, R.B. Gennis, G. Palmer, and M. Fabian Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and "activated" by reoxidation J. Biol. Chem. 281 2006 30319 30325 (Pubitemid 44582085)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30319-30325
    • Jancura, D.1    Berka, V.2    Antalik, M.3    Bagelova, J.4    Gennis, R.B.5    Palmer, G.6    Fabian, M.7
  • 23
    • 1942504686 scopus 로고    scopus 로고
    • Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: A comparison between the three families
    • DOI 10.1016/j.bbabio.2003.06.003, PII S0005272803001993
    • M.M. Pereira, and M. Teixeira Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: a comparison between the three families Biochim. Biophys. Acta 1655 2004 340 346 (Pubitemid 38526197)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 340-346
    • Pereira, M.M.1    Teixeira, M.2
  • 28
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochrome c oxidase by a second electron leads to proton translocation
    • DOI 10.1038/416099a
    • M. Ruitenberg, A. Kannt, E. Bamberg, K. Fendler, and H. Michel Reduction of cytochrome c oxidase by a second electron leads to proton translocation Nature 417 2002 99 102 (Pubitemid 34498824)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 99-102
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 32
    • 0001232127 scopus 로고
    • Purification and characterisation of cytochrome c oxidase from Thermus thermophilus HB8
    • K. Hon-nami, and T. Oshima Purification and characterisation of cytochrome c oxidase from Thermus thermophilus HB8 Biochemistry 23 1984 454 460
    • (1984) Biochemistry , vol.23 , pp. 454-460
    • Hon-Nami, K.1    Oshima, T.2
  • 34
    • 0024523241 scopus 로고
    • 3' of Thermus thermophilus. How old is cytochrome oxidase?
    • DOI 10.1111/j.1432-1033.1989.tb14720.x
    • G. Buse, S. Hensel, and J.A. Fee Evidence for cytochrome oxidase subunit I and a cytochrome c-subunit II fused protein in the cytochrome ′c1aa3′ of Thermus thermophilus. How old is cytochrome oxidase? Eur. J. Biochem. 181 1989 261 268 (Pubitemid 19120226)
    • (1989) European Journal of Biochemistry , vol.181 , Issue.1 , pp. 261-268
    • Buse, G.1    Hensel, S.2    Fee, J.A.3
  • 36
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • A. Jasaitis, M.I. Verkhovsky, J.E. Morgan, M.L. Verkhovskaya, and M. Wikström Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen Biochemistry 38 1999 2697 2706
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikström, M.5
  • 40
    • 0035340281 scopus 로고    scopus 로고
    • Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans
    • A. Jasaitis, C. Backgren, J.E. Morgan, A. Puustinen, M.I. Verkhovsky, and M. Wikström Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans Biochemistry 40 2001 5269 5274 (Pubitemid 32374010)
    • (2001) Biochemistry , vol.40 , Issue.17 , pp. 5269-5274
    • Jasaitis, A.1    Backgren, C.2    Morgan, J.E.3    Puustinen, A.4    Verkhovsky, M.I.5    Wikstrom, M.6
  • 41
    • 0034732967 scopus 로고    scopus 로고
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans
    • DOI 10.1021/bi000123w
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans Biochemistry 39 2000 6365 6372 (Pubitemid 30347141)
    • (2000) Biochemistry , vol.39 , Issue.21 , pp. 6365-6372
    • Riistama, S.1    Puustinen, A.2    Verkhovsky, M.I.3    Morgan, J.E.4    Wikstrom, M.5
  • 42
    • 0020488548 scopus 로고
    • Evidence for modulation of the heme absorptions of cytochrome c oxidase by metal-metal interactions
    • D.F. Blair, D.F. Bocian, G.T. Babcock, and S.I. Chan Evidence for modulation of the heme absorptions of cytochrome c oxidase by metal-metal interactions Biochemistry 21 1982 6928 6935
    • (1982) Biochemistry , vol.21 , pp. 6928-6935
    • Blair, D.F.1    Bocian, D.F.2    Babcock, G.T.3    Chan, S.I.4
  • 43
    • 0026671804 scopus 로고
    • The dioxygen cycle. Spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction
    • M. Wikström, and J.E. Morgan 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
  • 44
    • 0028851789 scopus 로고
    • The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F
    • M. Fabian, and G. Palmer 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
  • 47
    • 0032126255 scopus 로고    scopus 로고
    • Quantitation and characterization of cytochrome c oxidase in complex systems
    • DOI 10.1006/abio.1998.2704
    • B. Meunier, and P.R. Rich Quantitation and characterization of cytochrome c oxidase in complex systems Anal. Biochem. 260 1998 237 243 (Pubitemid 28322124)
    • (1998) Analytical Biochemistry , vol.260 , Issue.2 , pp. 237-243
    • Meunier, B.1    Rich, P.R.2
  • 50
    • 0027933876 scopus 로고
    • Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O
    • M. Lubben, and K. Morand Novel prenylated hemes as cofactors of cytochrome oxidases. Archaea have modified hemes A and O J. Biol. Chem. 269 1994 21473 21479
    • (1994) J. Biol. Chem. , vol.269 , pp. 21473-21479
    • Lubben, M.1    Morand, K.2
  • 51
    • 0022966751 scopus 로고
    • Kinetic investigations of the reactions of cytochrome c oxidase with hydrogen peroxide
    • DOI 10.1016/0005-2728(86)90059-9
    • A.C. Gorren, H. Dekker, and R. Wever Kinetic investigations of the reactions of cytochrome c oxidase with hydrogen peroxide Biochim. Biophys. Acta 852 1986 81 92 (Pubitemid 17182250)
    • (1986) Biochimica et Biophysica Acta - Bioenergetics , vol.852 , Issue.1 , pp. 81-92
    • Gorren, A.C.F.1    Dekker, H.2    Wever, R.3
  • 52
    • 0001805270 scopus 로고    scopus 로고
    • The reactions of hydrogen peroxide with bovine cytochrome c oxidase
    • DOI 10.1016/S0005-2728(99)00105-X, PII S000527289900105X
    • S. Junemann, P. Heathcote, and P.R. Rich The reactions of hydrogen peroxide with bovine cytochrome c oxidase Biochim. Biophys. Acta 1456 2000 56 66 (Pubitemid 30009738)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1456 , Issue.1 , pp. 56-66
    • Junemann, S.1    Heathcote, P.2    Rich, P.3
  • 53
    • 0030577351 scopus 로고    scopus 로고
    • 2: Evidence for the formation of an oxyferryl species by two distinct routes
    • DOI 10.1016/S0014-5793(96)01253-7, PII S0014579396012537
    • 2: evidence for the formation of an oxyferryl species by two distinct routes FEBS Lett. 399 1996 21 25 (Pubitemid 27007943)
    • (1996) FEBS Letters , vol.399 , Issue.1-2 , pp. 21-25
    • Brittain, T.1    Little, R.H.2    Greenwood, C.3    Watmough, N.J.4
  • 54
  • 55
    • 0035859920 scopus 로고    scopus 로고
    • Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide
    • DOI 10.1021/bi010115v
    • C. Pecoraro, R.B. Gennis, T.V. Vygodina, and A.A. Konstantinov Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide Biochemistry 40 2001 9695 9708 (Pubitemid 32757909)
    • (2001) Biochemistry , vol.40 , Issue.32 , pp. 9695-9708
    • Pecoraro, C.1    Gennis, R.B.2    Vygodina, T.V.3    Konstantinov, A.A.4
  • 56
    • 0039840998 scopus 로고    scopus 로고
    • Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • DOI 10.1021/bi971458p
    • S. Junemann, B. Meunier, R.B. Gennis, and P.R. Rich Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides Biochemistry 36 1997 14456 14464 (Pubitemid 27509938)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14456-14464
    • Junemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 57
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Q.H. Gibson, and C. Greenwood Reactions of cytochrome oxidase with oxygen and carbon monoxide Biochem. J. 86 1963 541 554
    • (1963) Biochem. J. , vol.86 , pp. 541-554
    • Gibson, Q.H.1    Greenwood, C.2
  • 58
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme
    • DOI 10.1016/S0005-2728(98)00142-X, PII S000527289800142X
    • P. Ädelroth, M. Ek, and P. Brzezinski 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 (Pubitemid 28451587)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1367 , Issue.1-3 , pp. 107-117
    • Adelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 60
    • 0016537919 scopus 로고
    • Low temperature trapping method for cytochrome oxidase oxygen intermediates
    • B. Chance, N. Graham, and V. Legallais Low temperature trapping method for cytochrome oxidase oxygen intermediates Anal. Biochem. 67 1975 552 579
    • (1975) Anal. Biochem. , vol.67 , pp. 552-579
    • Chance, B.1    Graham, N.2    Legallais, V.3
  • 63
    • 0027308712 scopus 로고
    • Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation
    • W.H. Woodruff Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation J. Bioenerg. Biomembr. 25 1993 177 188 (Pubitemid 23133525)
    • (1993) Journal of Bioenergetics and Biomembranes , vol.25 , Issue.2 , pp. 177-188
    • Woodruff, W.H.1
  • 65
    • 29244472486 scopus 로고    scopus 로고
    • An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans
    • DOI 10.1021/bi0511336
    • C. Ribacka, M.I. Verkhovsky, I. Belevich, D.A. Bloch, A. Puustinen, and M. Wikström An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans Biochemistry 44 2005 16502 16512 (Pubitemid 41832033)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16502-16512
    • Ribacka, C.1    Verkhovsky, M.I.2    Belevich, I.3    Bloch, D.A.4    Puustinen, A.5    Wikstrom, M.6
  • 66
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505 2001 185 208 (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 68
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • DOI 10.1021/bi9629079
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen Biochemistry 36 1997 13824 13829 (Pubitemid 27494888)
    • (1997) Biochemistry , vol.36 , Issue.45 , pp. 13824-13829
    • Adelroth, P.1    Svensson Ek, M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 69
    • 32344451238 scopus 로고    scopus 로고
    • A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus
    • DOI 10.1016/j.febslet.2006.01.055, PII S0014579306001086
    • 3 reductase from Rhodothermus marinus FEBS Lett. 580 2006 1350 1354 (Pubitemid 43221999)
    • (2006) FEBS Letters , vol.580 , Issue.5 , pp. 1350-1354
    • Pereira, M.M.1    Sousa, F.L.2    Teixeira, M.3    Nyquist, R.M.4    Heberle, J.5
  • 71
    • 0000816133 scopus 로고
    • The oxidation-reduction potential of the copper signal in pigeon heart mitochondria
    • M. Erecinska, B. Chance, and D.F. Wilson The oxidation-reduction potential of the copper signal in pigeon heart mitochondria FEBS Lett. 16 1971 284 286
    • (1971) FEBS Lett. , vol.16 , pp. 284-286
    • Erecinska, M.1    Chance, B.2    Wilson, D.F.3


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