메뉴 건너뛰기




Volumn 44, Issue 38, 2005, Pages 12767-12774

G204D, a mutation that blocks the proton-conducting D-channel of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ENZYME INHIBITION; FREE ENERGY; MUTAGENS; OXYGEN; PROTONS;

EID: 25444491194     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051141m     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0035853469 scopus 로고    scopus 로고
    • Zinc ions inhibit oxidation of cytochrome c oxidase by oxygen
    • Aagaard, A., and Brzezinski, P. (2001) Zinc Ions Inhibit Oxidation of Cytochrome c Oxidase by Oxygen, FEBS Lett. 494, 157-160.
    • (2001) FEBS Lett. , vol.494 , pp. 157-160
    • Aagaard, A.1    Brzezinski, P.2
  • 2
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller, S., and Babcock, G. T. (1996) Heme/Copper Terminal Oxidases, Chem. Rev. 7, 2889-2907.
    • (1996) Chem. Rev. , vol.7 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 3
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 Years of the elusive proton pump
    • Wikström, M. (2004) Cytochrome c Oxidase: 25 Years of the Elusive Proton Pump, Biochim. Biophys. Acta 1655, 241-247.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikström, M.1
  • 4
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel, H. (1998) The Mechanism of Proton Pumping by Cytochrome c Oxidase, Proc. Natl. Acad. Sci. U.S.A. 95, 12819-12824.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 5
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping - A discussion
    • Michel, H. (1999) Cytochrome c Oxidase: Catalytic Cycle and Mechanisms of Proton Pumping-A Discussion, Biochemistry 38, 15129-15140.
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 6
    • 0028890031 scopus 로고
    • Structure at 2.8 a resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8 A Resolution of Cytochrome c Oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 8
    • 0028913025 scopus 로고
    • 3 ubiquinol oxidase of Escherichia coli: Second site mutations in subunit I that restore proton pumping in the decoupled mutant asp135Asn
    • 3 Ubiquinol Oxidase of Escherichia coli: Second Site Mutations in Subunit I that Restore Proton Pumping in the Decoupled Mutant Asp135Asn, Biochemistry 34, 4428-4433.
    • (1995) Biochemistry , vol.34 , pp. 4428-4433
    • Garcia-Horsman, J.A.1    Puustinen, A.2    Gennis, R.B.3    Wikström, M.4
  • 9
    • 0037015164 scopus 로고    scopus 로고
    • Identification of the entry point of the k-proton-transfer pathway in cytochrome c oxidase
    • Brädén, M., Tomson, F. L., Gennis, R. B., and Brzezinski, P. (2002) Identification of the Entry Point of the K-proton-Transfer Pathway in Cytochrome c Oxidase, Biochemistry 41, 10794-10798.
    • (2002) Biochemistry , vol.41 , pp. 10794-10798
    • Brädén, M.1    Tomson, F.L.2    Gennis, R.B.3    Brzezinski, P.4
  • 10
    • 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., and Verkhovsky, M. I. (2000) The Role of the D- and K-pathways of Proton Transfer in the Function of the Haem-copper Oxidases, Biochim. Biophys. Acta 1459, 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
  • 11
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochrome c oxidase by a second electron leads to proton translocation
    • Rultenberg, M., Kannt, A., Bamberg, E., Fendler, K., and Michel, H. (2002) Reduction of Cytochrome c Oxidase by a Second Electron Leads to Proton Translocation, Nature 417, 99-102.
    • (2002) Nature , vol.417 , pp. 99-102
    • Rultenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 12
    • 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., and Gennis, R. B. (1997) 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, 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
  • 13
    • 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., and Nicholls, P. (1996) Fatty Acids Stimulate Activity and Restore Respiratory Control in a Proton Channel Mutant of Cytochrome c Oxidase, FEBS Lett. 393, 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
  • 14
    • 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, 13824-13829.
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Svensson-Ek, M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 15
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping
    • Pawate, A. S., Morgan, J., Namslauer, A., Mills, D. A., Brzezinski, P., Ferguson-Miller, S., and Gennis, R. B. (2002) A Mutation in Subunit I of Cytochrome Oxidase from Rhodobacter sphaeroides Results in an Increase in Steady-State Activity but Completely Eliminates Proton Pumping, Biochemistry 41, 13417.
    • (2002) Biochemistry , vol.41 , pp. 13417
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.A.4    Brzezinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 16
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • Pfitzner, U., Hoffmeier, K., Harrenga, A., Kannt, A., Michel, H., Bamberg, E., Richter, O.-M. H., and Ludwig, B. (2000) Tracing the D-Pathway in Reconstituted Site-Directed Mutants of Cytochrome c Oxidase from Paracoccus denitrificans, Biochemistry 39, 6756-6762.
    • (2000) Biochemistry , vol.39 , pp. 6756-6762
    • Pfitzner, U.1    Hoffmeier, K.2    Harrenga, A.3    Kannt, A.4    Michel, H.5    Bamberg, E.6    Richter, O.-M.H.7    Ludwig, B.8
  • 17
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • Brzezinski, P., and Larsson, G. (2003) Redox-driven Proton Pumping by Heme-copper Oxidases, Biochim. Biophys. Acta 1605, 1-13.
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 18
    • 0346734127 scopus 로고    scopus 로고
    • Redox-coupled proton translocation in biological systems: Proton shuttling in cytochrome c oxidase
    • Namslauer, A., Pawate, A., Gennis, R. B., and Brzezinski, P. (2003) Redox-Coupled Proton Translocation in Biological Systems: Proton Shuttling in Cytochrome c Oxidase, Proc. Natl. Acad. Sci. U.S.A. 100, 15543-15547.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15543-15547
    • Namslauer, A.1    Pawate, A.2    Gennis, R.B.3    Brzezinski, P.4
  • 19
    • 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. A., Tan, Z., Ferguson-Miller, S., and Hosler, J. P. (2003) 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, 7410-7417.
    • (2003) Biochemistry , vol.42 , pp. 7410-7417
    • Mills, D.A.1    Tan, Z.2    Ferguson-Miller, S.3    Hosler, J.P.4
  • 21
    • 0035852838 scopus 로고    scopus 로고
    • C-Terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the c-terminus in cytochrome c binding, and improves the assay for proton pumping
    • Riser, C., Mills, D. A., Schall, M., and Ferguson-Miller, S. (2001) C-Terminal Truncation and Histidine-tagging of Cytochrome c Oxidase Subunit II Reveals the Native Processing Site, Shows Involvement of the C-terminus in Cytochrome c Binding, and Improves the Assay for Proton Pumping, Biochemistry 40, 1606-1615.
    • (2001) Biochemistry , vol.40 , pp. 1606-1615
    • Riser, C.1    Mills, D.A.2    Schall, M.3    Ferguson-Miller, S.4
  • 22
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • Jasaitis, A., Verkhovsky, M. I., Morgan, J. E., Verkhovskaya, M. L., and Wikström, M. (1999) Assignment and Charge Translocation Stoichiometries of the Major Electrogenic Phases in the Reaction of Cytochrome c Oxidase with Dioxygen, Biochemistry 38, 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
  • 23
    • 0030949437 scopus 로고    scopus 로고
    • Bio-beads: An efficient strategy for two-dimensional crystallization of membrane proteins
    • Rigaud, J.-L., Mosser, G., Lacapere, J.-J., Olofsson, A., Levy, D., and Ranck, J.-L. (1997) Bio-Beads: An Efficient Strategy for Two-Dimensional Crystallization of Membrane Proteins, J. Struct. Biol. 118, 226-235.
    • (1997) J. Struct. Biol. , vol.118 , pp. 226-235
    • Rigaud, J.-L.1    Mosser, G.2    Lacapere, J.-J.3    Olofsson, A.4    Levy, D.5    Ranck, J.-L.6
  • 24
    • 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., and Wikström, M. (1995) Control of Electron Delivery to the Oxygen Reduction Site of Cytochrome c Oxidase: A Role for Protons, Biochemistry 34, 7483-7491.
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 25
    • 0037452542 scopus 로고    scopus 로고
    • Substitutions for glutamate 101 in subunit II of Cytochrome c oxidase from Rhodobacter sphaeroides result in blocking the proton-conducting K-channel
    • Tomson, F. L., Morgan, J. E., Gu, G., Barquera, B., Vygodina, T. V., and Gennis, R. B. (2003) Substitutions for glutamate 101 in subunit II of Cytochrome c oxidase from Rhodobacter sphaeroides result in blocking the proton-conducting K-channel, Biochemistry 42, 1711-1717.
    • (2003) Biochemistry , vol.42 , pp. 1711-1717
    • Tomson, F.L.1    Morgan, J.E.2    Gu, G.3    Barquera, B.4    Vygodina, T.V.5    Gennis, R.B.6
  • 27
    • 15444369621 scopus 로고    scopus 로고
    • Slow proton transfer through the pathways for pumped protons in cytochrome c oxidase induces suicide inactivation of the enzyme
    • Mills, D. A., and Hosler, J. P. (2005) Slow Proton Transfer Through the Pathways for Pumped Protons in Cytochrome c Oxidase Induces Suicide Inactivation of the Enzyme, Biochemistry 44, 4656-4666.
    • (2005) Biochemistry , vol.44 , pp. 4656-4666
    • Mills, D.A.1    Hosler, J.P.2
  • 28
    • 1942536202 scopus 로고    scopus 로고
    • The influence of subunit III of cytochrome c oxidase on the D pathway, the proton exit pathway and mechanism-based inactivation in subunit I
    • Hosler, J. P. (2004) The Influence of Subunit III of Cytochrome c Oxidase on the D Pathway, the Proton Exit pathway and Mechanism-based Inactivation in Subunit I, Biochim. Biophys. Acta 1655, 332-339.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 332-339
    • Hosler, J.P.1
  • 29
    • 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., Tornroth, S., Brzezinski, P., and Iwata, S. (2002) The X-ray Crystal Structures of Wild-type and EQ(I-286) Mutant Cytochrome c Oxidases from Rhodobacter sphaeroides, J. Mol. Biol. 321, 329-339.
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 30
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxoFerryl formation
    • Smirnova, I. A., Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1999) Aspartate-132 in Cytochrome c Oxidase from Rhodobacter sphaeroides is Involved in a Two-step Proton Transfer during OxoFerryl Formation, Biochemistry 38, 6826-6833.
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 31
    • 0038408885 scopus 로고    scopus 로고
    • Subunit III of cytochrome c oxidase of Rhodobacter spaheroides is required to maintain rapid proton uptake through the D pathway at physiologic pH
    • Gilderson, G., Salomonsson, L., Aagaard, A., Gray, J., Brzezinski, P., and Hosler, J. (2003) Subunit III of Cytochrome c Oxidase of Rhodobacter spaheroides is Required to Maintain Rapid Proton Uptake through the D Pathway at Physiologic pH, Biochemistry 42, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.