메뉴 건너뛰기




Volumn 1655, Issue 1-3, 2004, Pages 332-339

The influence of subunit III of cytochrome c oxidase on the D pathway, the proton exit pathway and mechanism-based inactivation in subunit I

Author keywords

Cytochrome oxidase; Proton pathway; Proton pumping; Suicide inactivation

Indexed keywords

CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE I; CYTOCHROME C OXIDASE III; OXIDOREDUCTASE; OXYGEN; PROTON; UNCLASSIFIED DRUG;

EID: 1942536202     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.06.009     Document Type: Review
Times cited : (63)

References (59)
  • 1
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siècle
    • Saraste M. Oxidative phosphorylation at the fin de siècle. Science. 283:1999;1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 2
    • 0031745229 scopus 로고    scopus 로고
    • Crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution
    • Yoshikawa S., Shinzawa-Itoh K., Tsukihara T. Crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution. J. Bioenerg. Biomembranes. 30:1998;7-14.
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 7-14
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 3
    • 0031935710 scopus 로고    scopus 로고
    • Structure and function of bacterial cytochrome c oxidase
    • Iwata S. Structure and function of bacterial cytochrome c oxidase. J. Biochem. (Tokyo). 123:1998;369-375.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 369-375
    • Iwata, S.1
  • 4
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M., Abramson J., Larsson G., Törnroth S., Brzezinski P., Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:2002;329-339.
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 6
    • 0025026342 scopus 로고
    • Phospholipid vesicles containing bovine heart mitochondrial cytochrome c oxidase and subunit III-deficient enzyme: Analysis of respiratory control and proton translocating activities
    • Wilson K.S., Prochaska L.J. Phospholipid vesicles containing bovine heart mitochondrial cytochrome c oxidase and subunit III-deficient enzyme: analysis of respiratory control and proton translocating activities. Arch. Biochem. Biophys. 282:1990;413-420.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 413-420
    • Wilson, K.S.1    Prochaska, L.J.2
  • 7
    • 0022037634 scopus 로고
    • Cytochrome c oxidase depleted of subunit III: Proton-pumping, respiratory control, and pH dependence of the midpoint potential of cytochrome a
    • Thompson D.A., Gregory L., Ferguson-Miller S. Cytochrome c oxidase depleted of subunit III: proton-pumping, respiratory control, and pH dependence of the midpoint potential of cytochrome a. J. Inorg. Biochem. 23:1985;357-364.
    • (1985) J. Inorg. Biochem. , vol.23 , pp. 357-364
    • Thompson, D.A.1    Gregory, L.2    Ferguson-Miller, S.3
  • 8
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Ädelroth P., Gennis R.B., Brzezinski P. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. Biochemistry. 37:1998;2470-2476.
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ädelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 9
    • 0039840998 scopus 로고    scopus 로고
    • Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • Jünemann S., Meunier B., Gennis R.B., Rich P.R. Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 36:1997;14456-14464.
    • (1997) Biochemistry , vol.36 , pp. 14456-14464
    • Jünemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 10
    • 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
    • Konstantinov A.A., Siletsky S., Mitchell D., Kaulen A., Gennis R.B. 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
  • 11
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström M., Jasaitis A., Backgren C., Puustinen A., Verkhovsky M.I. The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim. Biophys. Acta. 1459:2000;514-520.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 13
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. Biochemistry. 36:1997;13824-13829.
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Ek, M.S.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 14
    • 0032130867 scopus 로고    scopus 로고
    • Proton-controlled electron transfer in cytochrome c oxidase: Functional role of the pathways through Glu 286 and Lys 362
    • Brzezinski P., Ädelroth P. Proton-controlled electron transfer in cytochrome c oxidase: functional role of the pathways through Glu 286 and Lys 362. Acta Physiol. Scand., Suppl. 643:1998;7-16.
    • (1998) Acta Physiol. Scand., Suppl. , vol.643 , pp. 7-16
    • Brzezinski, P.1    Ädelroth, P.2
  • 15
    • 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
  • 16
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • Zaslavsky D., Gennis R.B. Proton pumping by cytochrome oxidase: progress, problems and postulates. Biochim. Biophys. Acta. 1458:2000;164-179.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 17
    • 0038998833 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase: A rejoinder to recent criticism
    • Wikström M. Proton translocation by cytochrome c oxidase: a rejoinder to recent criticism. Biochemistry. 39:2000;3515-3519.
    • (2000) Biochemistry , vol.39 , pp. 3515-3519
    • Wikström, M.1
  • 18
    • 0034640452 scopus 로고    scopus 로고
    • Mechanism of proton translocation by cytochrome c oxidase: A new four-stroke histidine cycle
    • Wikström M. Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle. Biochim. Biophys. Acta. 1458:2000;188-198.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 188-198
    • Wikström, M.1
  • 19
    • 0037056048 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle
    • Wikström M., Verkhovsky M.I. Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle. Biochim. Biophys. Acta. 1555:2002;128-132.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 128-132
    • Wikström, M.1    Verkhovsky, M.I.2
  • 21
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen A., Wikström M. Proton exit from the heme-copper oxidase of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 96:1999;35-37.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 22
    • 0030590493 scopus 로고    scopus 로고
    • Fatty acids stimulate activity and restore respiratory control in a proton channel mutant of cytochrome c oxidase
    • Fetter J., Sharpe M., Qian J., Mills D., Ferguson-Miller S., Nicholls P. Fatty acids stimulate activity and restore respiratory control in a proton channel mutant of cytochrome c oxidase. FEBS Lett. 393:1996;155-160.
    • (1996) FEBS Lett. , vol.393 , pp. 155-160
    • Fetter, J.1    Sharpe, M.2    Qian, J.3    Mills, D.4    Ferguson-Miller, S.5    Nicholls, P.6
  • 23
  • 24
    • 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 physiologic pH
    • Gilderson G., Salomonsson L., Aagaard A., Gray J., Brzezinski P., Hosler J. Subunit III of cytochrome c oxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH. Biochemistry. 42:2003;7400-7409.
    • (2003) Biochemistry , vol.42 , pp. 7400-7409
    • Gilderson, G.1    Salomonsson, L.2    Aagaard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 25
    • 0037790647 scopus 로고    scopus 로고
    • A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase
    • Mills D., Tan Z., Ferguson-Miller S., Hosler J. A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase. Biochemistry. 42:2003;7410-7417.
    • (2003) Biochemistry , vol.42 , pp. 7410-7417
    • Mills, D.1    Tan, Z.2    Ferguson-Miller, S.3    Hosler, J.4
  • 26
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochrome c oxidase: Catalytic turnover in the absence of subunit III alters the active site
    • Bratton M.R., Pressler M.A., Hosler J.P. Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry. 38:1999;16236-16245.
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 27
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia T., Semo N., Arrondo J.L., Goni F.M., Freire E. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry. 33:1994;9731-9740.
    • (1994) Biochemistry , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.3    Goni, F.M.4    Freire, E.5
  • 28
    • 0024845389 scopus 로고
    • Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase
    • Haltia T., Finel M., Harms N., Nakari T., Raitio M., Wikström M., Saraste M. Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase. EMBO J. 8:1989;3571-3579.
    • (1989) EMBO J. , vol.8 , pp. 3571-3579
    • Haltia, T.1    Finel, M.2    Harms, N.3    Nakari, T.4    Raitio, M.5    Wikström, M.6    Saraste, M.7
  • 29
    • 0034711013 scopus 로고    scopus 로고
    • Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides
    • Bratton M.R., Hiser L., Antholine W.E., Hoganson C., Hosler J.P. Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry. 39:2000;12989-12995.
    • (2000) Biochemistry , vol.39 , pp. 12989-12995
    • Bratton, M.R.1    Hiser, L.2    Antholine, W.E.3    Hoganson, C.4    Hosler, J.P.5
  • 32
    • 0034669607 scopus 로고    scopus 로고
    • Respiratory pathways of Rhodobacter sphaeroides 2.4.1(T): Identification and characterization of genes encoding quinol oxidases
    • Mouncey N.J., Gak E., Choudhary M., Oh J., Kaplan S. Respiratory pathways of Rhodobacter sphaeroides 2.4.1(T): identification and characterization of genes encoding quinol oxidases. FEMS Microbiol. Lett. 192:2000;205-210.
    • (2000) FEMS Microbiol. Lett. , vol.192 , pp. 205-210
    • Mouncey, N.J.1    Gak, E.2    Choudhary, M.3    Oh, J.4    Kaplan, S.5
  • 33
    • 0035861943 scopus 로고    scopus 로고
    • Different suicide inactivation processes for the peroxidase and cyclooxygenase activities of prostaglandin endoperoxide H synthase-1
    • Song I., Ball T.M., Smith W.L. Different suicide inactivation processes for the peroxidase and cyclooxygenase activities of prostaglandin endoperoxide H synthase-1. Biochem. Biophys. Res. Commun. 289:2001;869-875.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 869-875
    • Song, I.1    Ball, T.M.2    Smith, W.L.3
  • 34
    • 0032516915 scopus 로고    scopus 로고
    • A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities
    • Su C., Sahlin M., Oliw E.H. A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities. J. Biol. Chem. 273:1998;20744-20751.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20744-20751
    • Su, C.1    Sahlin, M.2    Oliw, E.H.3
  • 39
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier C., Harrenga A., Ermler U., Michel H. Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc. Natl. Acad. Sci. U. S. A. 94:1997;10547-10553.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 41
    • 0033741298 scopus 로고    scopus 로고
    • X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa S., Shinzawa-Itoh K., Tsukihara T. X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase. J. Inorg. Biochem. 82:2000;1-7.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 1-7
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 43
    • 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
  • 44
    • 0037163087 scopus 로고    scopus 로고
    • Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein
    • Carr H.S., George G.N., Winge D.R. Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein. J. Biol. Chem. 277:2002;31237-31242.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 46
    • 0019887782 scopus 로고
    • The effects of copper depletion on cytochrome c oxidase
    • Weintraub S.T., Wharton D.C. The effects of copper depletion on cytochrome c oxidase. J. Biol. Chem. 256:1981;1669-1676.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1669-1676
    • Weintraub, S.T.1    Wharton, D.C.2
  • 47
    • 0032514726 scopus 로고    scopus 로고
    • The post-translational modification in cytochrome c 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 c 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
  • 48
    • 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
    • Namslauer A., Aagaard A., Katsonouri A., Brzezinski P. 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.
    • (2003) Biochemistry , vol.42 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 49
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochrome c oxidase
    • Brzezinski P., Ädelroth P. Pathways of proton transfer in cytochrome c oxidase. J. Bioenerg. Biomembranes. 30:1998;99-107.
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 99-107
    • Brzezinski, P.1    Ädelroth, P.2
  • 50
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase
    • Ädelroth P., Karpefors M., Gilderson G., Tomson F.L., Gennis R.B., Brzezinski P. Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase. Biochim. Biophys. Acta. 1459:2000;533-539.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 533-539
    • Ädelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 51
    • 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
    • Smirnova I.A., Ädelroth P., Gennis R.B., Brzezinski P. 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
  • 53
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • [see comments]
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. [see comments] Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 54
    • 0020967882 scopus 로고
    • Hydrogen bonded chain mechanisms for proton conduction and proton pumping
    • Nagle J.F., Tristram-Nagle S. Hydrogen bonded chain mechanisms for proton conduction and proton pumping. J. Membr. Biol. 74:1983;1-14.
    • (1983) J. Membr. Biol. , vol.74 , pp. 1-14
    • Nagle, J.F.1    Tristram-Nagle, S.2
  • 55
    • 0037056047 scopus 로고    scopus 로고
    • Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase
    • Mills D.A., Ferguson-Miller S. Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase. Biochim. Biophys. Acta. 1555:2002;96-100.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 96-100
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 56
    • 0028241769 scopus 로고
    • Proton uptake by cytochrome c oxidase on reduction and on ligand binding
    • Mitchell R., Rich P.R. Proton uptake by cytochrome c oxidase on reduction and on ligand binding. Biochim. Biophys. Acta. 1186:1994;19-26.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 19-26
    • Mitchell, R.1    Rich, P.R.2
  • 57
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • Verkhovsky M.I., Morgan J.E., Wikström M. Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons. Biochemistry. 34:1995;7483-7491.
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 58
    • 0034643829 scopus 로고    scopus 로고
    • Localized control of proton transfer through the D-pathway in cytochrome c oxidase: Application of the proton-inventory technique
    • Karpefors M., Ädelroth P., Brzezinski P. Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique. Biochemistry. 39:2000;6850-6856.
    • (2000) Biochemistry , vol.39 , pp. 6850-6856
    • Karpefors, M.1    Ädelroth, P.2    Brzezinski, P.3
  • 59
    • 0027491552 scopus 로고
    • Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
    • Thomas J.W., Puustinen A., Alben J.O., Gennis R.B., Wikström M. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Biochemistry. 32:1993;10923-10928.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.