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Volumn 108, Issue 4, 2011, Pages 1284-1289

Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump

Author keywords

Conformational gating; Membrane protein structure; Proton path mutants; Water chain; X ray reduction

Indexed keywords

CHLORIDE ION; CYTOCHROME C OXIDASE; LYSINE; METHIONINE; PROTON PUMP; WATER;

EID: 79952133576     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1012846108     Document Type: Article
Times cited : (42)

References (40)
  • 1
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller S, Babcock GT (1996) Heme/copper terminal oxidases. Chem Rev 96:2889-2908.
    • (1996) Chem Rev , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 2
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • Hosler JP, Ferguson-Miller S, Mills DA (2006) Energy transduction: Proton transfer through the respiratory complexes. Annu Rev Biochem 75:165-187.
    • (2006) Annu Rev Biochem , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 3
    • 67049086176 scopus 로고    scopus 로고
    • Redox-dependent conformational changes in cytochrome C oxidase suggest a gating mechanism for proton uptake
    • Qin L, et al. (2009) Redox-dependent conformational changes in cytochrome C oxidase suggest a gating mechanism for proton uptake. Biochemistry 48:5121-5130.
    • (2009) Biochemistry , vol.48 , pp. 5121-5130
    • Qin, L.1
  • 4
    • 34548479264 scopus 로고    scopus 로고
    • Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases
    • Hemp J, et al. (2007) Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases. Biochemistry 46:9963-9972.
    • (2007) Biochemistry , vol.46 , pp. 9963-9972
    • Hemp, J.1
  • 6
    • 33745635337 scopus 로고    scopus 로고
    • Reaction mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa S, et al. (2006) Reaction mechanism of bovine heart cytochrome c oxidase. Biochim Biophys Acta 1757:395-400.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 395-400
    • Yoshikawa, S.1
  • 7
    • 34247180567 scopus 로고    scopus 로고
    • The proton pumping pathway of bovine heart cytochrome c oxidase
    • Shimokata K, et al. (2007) The proton pumping pathway of bovine heart cytochrome c oxidase. Proc Natl Acad Sci USA 104:4200-4205.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4200-4205
    • Shimokata, K.1
  • 8
    • 0028941458 scopus 로고
    • Possible proton relay pathways in cytochrome c oxidase
    • Fetter JR, et al. (1995) Possible proton relay pathways in cytochrome c oxidase. Proc Natl Acad Sci USA 92:1604-1608.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1604-1608
    • Fetter, J.R.1
  • 9
    • 9444278512 scopus 로고    scopus 로고
    • Polar residues in helix VIII of subunit I of cytochrome c oxidase influence the activity and the structure of the active site
    • Hosler JP, et al. (1996) Polar residues in helix VIII of subunit I of cytochrome c oxidase influence the activity and the structure of the active site. Biochemistry 35:10776-10783.
    • (1996) Biochemistry , vol.35 , pp. 10776-10783
    • Hosler, J.P.1
  • 10
    • 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, et al. (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
  • 11
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson-Miller S (2006) Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 103:16117-16122.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 12
    • 66349128958 scopus 로고    scopus 로고
    • High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: New insights into the active site and the proton transfer pathways
    • Koepke J, et al. (2009) High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: New insights into the active site and the proton transfer pathways. Biochim Biophys Acta 1787:635-645.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 635-645
    • Koepke, J.1
  • 13
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikstrom M, Jasaitis A, Backgren C, Puustinen A, Verkhovsky MI (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
    • Wikstrom, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 14
    • 33947280355 scopus 로고    scopus 로고
    • Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: Identification of a protonated water cluster
    • Xu J, Sharpe MA, Qin L, Ferguson-Miller S, Voth GA (2007) Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: Identification of a protonated water cluster. J Am Chem Soc 129:2910-2913.
    • (2007) J Am Chem Soc , vol.129 , pp. 2910-2913
    • Xu, J.1    Sharpe, M.A.2    Qin, L.3    Ferguson-Miller, S.4    Voth, G.A.5
  • 15
    • 2642586355 scopus 로고    scopus 로고
    • Quantum molecular dynamics simulation of proton transfer in cytochrome c oxidase
    • Cukier RI (2004) Quantum molecular dynamics simulation of proton transfer in cytochrome c oxidase. Biochim Biophys Acta 1656:189-202.
    • (2004) Biochim Biophys Acta , vol.1656 , pp. 189-202
    • Cukier, R.I.1
  • 16
    • 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 AS, et al. (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 41:13417-13423.
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1
  • 18
    • 63449091255 scopus 로고    scopus 로고
    • Functional hydration and conformational gating of proton uptake in cytochrome c oxidase
    • Henry RM, Yu CH, Rodinger T, Pomes R (2009) Functional hydration and conformational gating of proton uptake in cytochrome c oxidase. J Mol Biol 387:1165-1185.
    • (2009) J Mol Biol , vol.387 , pp. 1165-1185
    • Henry, R.M.1    Yu, C.H.2    Rodinger, T.3    Pomes, R.4
  • 19
    • 33751569076 scopus 로고    scopus 로고
    • Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump
    • Han D, et al. (2006) Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump. Biochemistry 45:14064-14074.
    • (2006) Biochemistry , vol.45 , pp. 14064-14074
    • Han, D.1
  • 20
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • Pfitzner U, et al. (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
  • 21
    • 77952825869 scopus 로고    scopus 로고
    • Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping
    • Zhu J, Han H, Pawate A, Gennis RB (2010) Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping. Biochemistry 49:4476-4482.
    • (2010) Biochemistry , vol.49 , pp. 4476-4482
    • Zhu, J.1    Han, H.2    Pawate, A.3    Gennis, R.B.4
  • 22
    • 0030033422 scopus 로고    scopus 로고
    • Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor
    • Yao N, Ledvina PS, Choudhary A, Quiocho FA (1996) Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor. Biochemistry 35:2079-2085.
    • (1996) Biochemistry , vol.35 , pp. 2079-2085
    • Yao, N.1    Ledvina, P.S.2    Choudhary, A.3    Quiocho, F.A.4
  • 23
    • 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 DA, Hosler JP (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
  • 24
    • 11144304570 scopus 로고    scopus 로고
    • A molecular dynamics study of water chain formation in the proton conduction K channel of cytochrome c oxidase
    • Cukier RI (2005) A molecular dynamics study of water chain formation in the proton conduction K channel of cytochrome c oxidase. Biochim Biophys Acta 1706:134-146.
    • (2005) Biochim Biophys Acta , vol.1706 , pp. 134-146
    • Cukier, R.I.1
  • 25
    • 0037015164 scopus 로고    scopus 로고
    • The entry point of the K-protontransfer pathway in cytochrome c oxidase
    • Branden M, Tomson F, Gennis RB, Brzezinski P (2002) The entry point of the K-protontransfer pathway in cytochrome c oxidase. Biochemistry 41:10794-10798.
    • (2002) Biochemistry , vol.41 , pp. 10794-10798
    • Branden, M.1    Tomson, F.2    Gennis, R.B.3    Brzezinski, P.4
  • 26
    • 12544249247 scopus 로고    scopus 로고
    • Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase
    • Richter OM, et al. (2005) Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase. FEBS J 272:404-412.
    • (2005) FEBS J , vol.272 , pp. 404-412
    • Richter, O.M.1
  • 27
    • 57049130390 scopus 로고    scopus 로고
    • A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
    • Sharpe MA, Ferguson-Miller S (2008) A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases. J Bioenerg Biomembr 40:541-549.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 541-549
    • Sharpe, M.A.1    Ferguson-Miller, S.2
  • 28
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Adelroth P, Gennis RB, Brzezinski P (1998) Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. Biochemistry 37:2470-2476.
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Adelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 29
    • 0032478167 scopus 로고    scopus 로고
    • Substitution of lysine-362 in a putative proton-conducting channel in the cytochrome c oxidase from Rhodobacter sphaeroides blocks turnover with O2 but not with H2O2
    • Zaslavsky D, Gennis R (1998) Substitution of lysine-362 in a putative proton-conducting channel in the cytochrome c oxidase from Rhodobacter sphaeroides blocks turnover with O2 but not with H2O2. Biochemistry 37:3062-3067.
    • (1998) Biochemistry , vol.37 , pp. 3062-3067
    • Zaslavsky, D.1    Gennis, R.2
  • 30
    • 42449087250 scopus 로고    scopus 로고
    • Charge transfer in the K proton pathway linked to electron transfer to the catalytic site in cytochrome c oxidase
    • Lepp H, Svahn E, Faxen K, Brzezinski P (2008) Charge transfer in the K proton pathway linked to electron transfer to the catalytic site in cytochrome c oxidase. Biochemistry 47:4929-4935.
    • (2008) Biochemistry , vol.47 , pp. 4929-4935
    • Lepp, H.1    Svahn, E.2    Faxen, K.3    Brzezinski, P.4
  • 31
    • 56249146306 scopus 로고    scopus 로고
    • A D pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate
    • Durr KL, et al. (2008) A D pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate. J Mol Biol 384:865-877.
    • (2008) J Mol Biol , vol.384 , pp. 865-877
    • Durr, K.L.1
  • 32
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • Harrenga A, Michel H (1999) The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J Biol Chem 274:33296-33299.
    • (1999) J Biol Chem , vol.274 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 33
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase
    • Yoshikawa S, et al. (1998) Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science 280:1723-1729.
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1
  • 34
    • 61449123035 scopus 로고    scopus 로고
    • Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: Structure of the reduced form of the enzyme
    • Liu B, et al. (2009) Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: Structure of the reduced form of the enzyme. Biochemistry 48:820-826.
    • (2009) Biochemistry , vol.48 , pp. 820-826
    • Liu, B.1
  • 35
    • 33846085666 scopus 로고    scopus 로고
    • Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry
    • Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM (2007) Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. J Synchrotron Radiat 14:92-98.
    • (2007) J Synchrotron Radiat , vol.14 , pp. 92-98
    • Pearson, A.R.1    Pahl, R.2    Kovaleva, E.G.3    Davidson, V.L.4    Wilmot, C.M.5
  • 36
    • 60549100318 scopus 로고    scopus 로고
    • A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump
    • Aoyama H, et al. (2009) A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump. Proc Natl Acad Sci USA 106:2165-2169.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2165-2169
    • Aoyama, H.1
  • 37
    • 77952331283 scopus 로고    scopus 로고
    • Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate
    • Muramoto K, et al. (2010) Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate. Proc Natl Acad Sci USA 107:7740-7745.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7740-7745
    • Muramoto, K.1
  • 38
    • 33748895869 scopus 로고    scopus 로고
    • Combined DFTand electrostatics study of the proton pumping mechanism in cytochrome c oxidase
    • Quenneville J, Popovic DM, Stuchebrukhov AA (2006) Combined DFTand electrostatics study of the proton pumping mechanism in cytochrome c oxidase. Biochim Biophys Acta 1757:1035-1046.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1035-1046
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 39
    • 38049091274 scopus 로고    scopus 로고
    • Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant
    • Busenlehner LS, Branden G, Namslauer I, Brzezinski P, Armstrong RN (2008) Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant. Biochemistry 47:73-83.
    • (2008) Biochemistry , vol.47 , pp. 73-83
    • Busenlehner, L.S.1    Branden, G.2    Namslauer, I.3    Brzezinski, P.4    Armstrong, R.N.5
  • 40
    • 33750282788 scopus 로고    scopus 로고
    • Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase
    • Busenlehner LS, Salomonsson L, Brzezinski P, Armstrong RN (2006) Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase. Proc Natl Acad Sci USA 103:15398-15403.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15398-15403
    • Busenlehner, L.S.1    Salomonsson, L.2    Brzezinski, P.3    Armstrong, R.N.4


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