메뉴 건너뛰기




Volumn 49, Issue 27, 2010, Pages 5651-5661

Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: Insights into the assembly of CuB of cytochrome c oxidase.

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINUS; CHARGE BALANCES; COPPER BINDING; CYTOCHROME C OXIDASE; RHODOBACTER SPHAEROIDES; SPHAEROIDES; TETRAMERS; TRANSMEMBRANE HELICES;

EID: 77954691094     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1003876     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • Hosler, J. P., Ferguson-Miller, S., and Mills, D. A. (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
  • 2
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Structure, function, and physiology of a redox-driven molecular machine
    • Richter, O. M., and Ludwig, B. (2003) Cytochrome c oxidase: Structure, function, and physiology of a redox-driven molecular machine. Rev. Physiol. Biochem. Pharmacol. 147, 47-74.
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.147 , pp. 47-74
    • Richter, O.M.1    Ludwig, B.2
  • 4
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans twosubunit cytochrome c oxidase complexed with an antibody Fv fragment
    • Ostermeier, C., Harrenga, A., Ermler, U., and Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans twosubunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc. Natl. Acad. Sci. U.S.A. 94, 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
  • 5
    • 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, R. M., and 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. U.S.A. 103, 16117-16122.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 7
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the heme-copper superfamily in archaea: Insights from genomics and structural modeling
    • Hemp, J., and Gennis, R. B. (2008) Diversity of the heme-copper superfamily in archaea: Insights from genomics and structural modeling. Results Probl. Cell Differ. 45, 1-31.
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 8
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia, T., Semo, N., Arrondo, J. L., Goni, F. M., and Freire, E. (1994) Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33, 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
  • 9
    • 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., and Hosler, J. P. (2000) Identification of the structural subunits required for formation of the metal centers in subunit I of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry 39, 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
  • 10
    • 34548842221 scopus 로고    scopus 로고
    • Conserved lipid-binding sites in membrane proteins: A focus on cytochrome c oxidase
    • Qin, L., Sharpe, M. A., Garavito, R. M., and Ferguson-Miller, S. (2007) Conserved lipid-binding sites in membrane proteins: A focus on cytochrome c oxidase. Curr. Opin. Struct. Biol. 17, 444-450.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 444-450
    • Qin, L.1    Sharpe, M.A.2    Garavito, R.M.3    Ferguson-Miller, S.4
  • 11
    • 0026615058 scopus 로고
    • Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast
    • Cao, J., Hosler, J., Shapleigh, J., Revzin, A., and Ferguson-Miller, S. (1992) Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast. J. Biol. Chem. 267, 24273-24278.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24273-24278
    • Cao, J.1    Hosler, J.2    Shapleigh, J.3    Revzin, A.4    Ferguson-Miller, S.5
  • 12
    • 0026615057 scopus 로고
    • Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis
    • Hosler, J. P., Fetter, J., Tecklenburg, M. M., Espe, M., Lerma, C., and Ferguson-Miller, S. (1992) Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis. J. Biol. Chem. 267, 24264-24272.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24264-24272
    • Hosler, J.P.1    Fetter, J.2    Tecklenburg, M.M.3    Espe, M.4    Lerma, C.5    Ferguson-Miller, S.6
  • 13
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the CuB and magnesium centers of cytochrome c oxidase
    • Hiser, L., Di Valentin, M., Hamer, A. G., and Hosler, J. P. (2000) Cox11p is required for stable formation of the CuB and magnesium centers of cytochrome c oxidase. J. Biol. Chem. 275, 619-623.
    • (2000) J. Biol. Chem. , vol.275 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 14
    • 24044459731 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase in the absence of assembly protein Surf1p leads to loss of the active site heme
    • Smith, D., Gray, J., Mitchell, L., Antholine, W. E., and Hosler, J. P. (2005) Assembly of cytochrome c oxidase in the absence of assembly protein Surf1p leads to loss of the active site heme. J. Biol. Chem. 280, 17652-17656.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17652-17656
    • Smith, D.1    Gray, J.2    Mitchell, L.3    Antholine, W.E.4    Hosler, J.P.5
  • 16
    • 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., and Winge, D. R. (2002) Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I) binding protein. J. Biol. Chem. 277, 31237-31242.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 17
    • 4544227787 scopus 로고    scopus 로고
    • Solution structure of Cox11, a novel type of β-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase
    • Banci, L., Bertini, I., Cantini, F., Ciofi-Baffoni, S., Gonnelli, L., and Mangani, S. (2004) Solution structure of Cox11, a novel type of β-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase. J. Biol. Chem. 279, 34833-34839.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34833-34839
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4    Gonnelli, L.5    Mangani, S.6
  • 18
  • 19
    • 34248136477 scopus 로고    scopus 로고
    • Modeling protein-protein complexes involved in the cytochrome c oxidase copper delivery pathway
    • van Dijk, A. D., Ciofi-Baffoni, S., Banci, L., Bertini, I., Boelens, R., and Bonvin, A. M. (2007) Modeling protein-protein complexes involved in the cytochrome c oxidase copper delivery pathway. J. Proteome Res. 6, 1530-1539.
    • (2007) J. Proteome Res. , vol.6 , pp. 1530-1539
    • Van Dijk, A.D.1    Ciofi-Baffoni, S.2    Banci, L.3    Bertini, I.4    Boelens, R.5    Bonvin, A.M.6
  • 20
    • 18944364732 scopus 로고    scopus 로고
    • Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the CuB site formation of cytochrome c oxidase
    • Khalimonchuk, O., Ostermann, K., and Rodel, G. (2005) Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the CuB site formation of cytochrome c oxidase. Curr. Genet. 47, 223-233.
    • (2005) Curr. Genet. , vol.47 , pp. 223-233
    • Khalimonchuk, O.1    Ostermann, K.2    Rodel, G.3
  • 21
    • 46349092291 scopus 로고    scopus 로고
    • Biogenesis of cytochrome c oxidase: In vitro approaches to study cofactor insertion into a bacterial subunit I
    • Greiner, P., Hannappel, A., Werner, C., and Ludwig, B. (2008) Biogenesis of cytochrome c oxidase: In vitro approaches to study cofactor insertion into a bacterial subunit I. Biochim. Biophys. Acta 1777, 904-911.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 904-911
    • Greiner, P.1    Hannappel, A.2    Werner, C.3    Ludwig, B.4
  • 22
    • 33645052707 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p
    • Banting, G. S., and Glerum, D. M. (2006) Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p. Eukaryotic Cell 5, 568-578.
    • (2006) Eukaryotic Cell , vol.5 , pp. 568-578
    • Banting, G.S.1    Glerum, D.M.2
  • 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, 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, 4656-14566
    • (2005) Biochemistry , vol.44 , pp. 4656-14566
    • Mills, D.A.1    Hosler, J.P.2
  • 25
    • 0027178231 scopus 로고
    • Stoichiometry and redox behaviour of metals in cytochrome c oxidase
    • Steffens, G. C., Soulimane, T., Wolff, G., and Buse, G. (1993) Stoichiometry and redox behaviour of metals in cytochrome c oxidase. Eur. J. Biochem. 213, 1149-1157.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1149-1157
    • Steffens, G.C.1    Soulimane, T.2    Wolff, G.3    Buse, G.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., and Hosler, J. P. (1999) Suicide inactivation of cytochrome c oxidase: Catalytic turnover in the absence of subunit III alters the active site. Biochemistry 38, 16236-16245.
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 27
    • 4344560984 scopus 로고    scopus 로고
    • Metalbinding mechanism of Cox17, a copper chaperone for cytochrome c oxidase
    • Palumaa, P., Kangur, L., Voronova, A., and Sillard, R. (2004) Metalbinding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Biochem. J. 382, 307-314.
    • (2004) Biochem. J. , vol.382 , pp. 307-314
    • Palumaa, P.1    Kangur, L.2    Voronova, A.3    Sillard, R.4
  • 29
    • 0030855633 scopus 로고    scopus 로고
    • EPR spectroscopy of Escherichia coli cytochrome bo which lacks CuB
    • Hunter, D. J., Moody, A. J., Rich, P. R., and Ingledew, W. J. (1997) EPR spectroscopy of Escherichia coli cytochrome bo which lacks CuB. FEBS Lett. 412, 43-47.
    • (1997) FEBS Lett. , vol.412 , pp. 43-47
    • Hunter, D.J.1    Moody, A.J.2    Rich, P.R.3    Ingledew, W.J.4
  • 30
    • 67649948826 scopus 로고    scopus 로고
    • Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides
    • Egawa, T., Lee, H. J., Gennis, R. B., Yeh, S. R., and Rousseau, D. L. (2009) Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochim. Biophys. Acta 1787, 1272-1275.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1272-1275
    • Egawa, T.1    Lee, H.J.2    Gennis, R.B.3    Yeh, S.R.4    Rousseau, D.L.5
  • 33
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont, A. K., Huffman, D. L., Lamb, A. L., O'Halloran, T. V., and Rosenzweig, A. C. (2000) Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 7, 766-771.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 34
    • 0035936586 scopus 로고    scopus 로고
    • The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex
    • Heaton, D. N., George, G. N., Garrison, G., and Winge, D. R. (2001) The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry 40, 743-751.
    • (2001) Biochemistry , vol.40 , pp. 743-751
    • Heaton, D.N.1    George, G.N.2    Garrison, G.3    Winge, D.R.4
  • 37
    • 35448929548 scopus 로고    scopus 로고
    • A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase
    • Stasser, J. P., Siluvai, G. S., Barry, A. N., and Blackburn, N. J. (2007) A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase. Biochemistry 46, 11845-11856.
    • (2007) Biochemistry , vol.46 , pp. 11845-11856
    • Stasser, J.P.1    Siluvai, G.S.2    Barry, A.N.3    Blackburn, N.J.4
  • 38
    • 18944396823 scopus 로고    scopus 로고
    • Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding
    • Arnesano, F., Balatri, E., Banci, L., Bertini, I., and Winge, D. R. (2005) Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure 13, 713-722.
    • (2005) Structure , vol.13 , pp. 713-722
    • Arnesano, F.1    Balatri, E.2    Banci, L.3    Bertini, I.4    Winge, D.R.5
  • 39
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb, A. L., Torres, A. S., O'Halloran, T. V., and Rosenzweig, A. C. (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat. Struct. Biol. 8, 751-755.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 40
    • 75749130711 scopus 로고    scopus 로고
    • Formation of the redox cofactor centers during Cox1 maturation in yeast cytochrome oxidase
    • Khalimonchuk, O., Bestwick,M., Meunier, B.,Watts, T. C., andWinge, D. R. (2010) Formation of the redox cofactor centers during Cox1 maturation in yeast cytochrome oxidase. Mol. Cell. Biol. 30, 1004-1017.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1004-1017
    • Khalimonchuk, O.1    Bestwick, M.2    Meunier, B.3    Watts, T.C.4    Winge, D.R.5
  • 41
    • 70350033961 scopus 로고    scopus 로고
    • Surf1, associated with Leigh syndrome in humans, is a heme-binding protein in bacterial oxidase biogenesis
    • Bundschuh, F. A., Hannappel, A., Anderka, O., and Ludwig, B. (2009) Surf1, associated with Leigh syndrome in humans, is a heme-binding protein in bacterial oxidase biogenesis. J. Biol. Chem. 284, 25735-25741.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25735-25741
    • Bundschuh, F.A.1    Hannappel, A.2    Anderka, O.3    Ludwig, B.4
  • 42
    • 6344282706 scopus 로고    scopus 로고
    • Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli
    • Brown, B. M., Wang, Z., Brown, K. R., Cricco, J. A., and Hegg, E. L. (2004) Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli. Biochemistry 43, 13541-13548.
    • (2004) Biochemistry , vol.43 , pp. 13541-13548
    • Brown, B.M.1    Wang, Z.2    Brown, K.R.3    Cricco, J.A.4    Hegg, E.L.5
  • 43
    • 70450177295 scopus 로고    scopus 로고
    • Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain
    • Hussain, F., Rodriguez-Granillo, A., and Wittung-Stafshede, P. (2009) Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain. J. Am. Chem. Soc. 131, 16371-16373.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16371-16373
    • Hussain, F.1    Rodriguez-Granillo, A.2    Wittung-Stafshede, P.3
  • 44
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase
    • Horng, Y. C., Cobine, P. A., Maxfield, A. B., Carr, H. S., and Winge, D. R. (2004) Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase. J. Biol. Chem. 279, 35334-35340.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35334-35340
    • Horng, Y.C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 45
    • 34548689397 scopus 로고    scopus 로고
    • PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
    • Badrick, A. C., Hamilton, A. J., Bernhardt, P. V., Jones, C. E., Kappler, U., Jennings, M. P., and McEwan, A. G. (2007) PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity. FEBS Lett. 581, 4663-4667.
    • (2007) FEBS Lett. , vol.581 , pp. 4663-4667
    • Badrick, A.C.1    Hamilton, A.J.2    Bernhardt, P.V.3    Jones, C.E.4    Kappler, U.5    Jennings, M.P.6    McEwan, A.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.