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Volumn 3, Issue JAN, 2013, Pages

Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein

Author keywords

Copper metallochaperone; Cytochrome c oxidase; Morphological development; Sco protein; Streptomyces; Thiol disulphide reductase activity

Indexed keywords

BACTERIAL PROTEIN; COPPER; CYTOCHROME C OXIDASE;

EID: 84877761743     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.120163     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 33746865723 scopus 로고    scopus 로고
    • Streptomyces inside-out: A new perspective on the bacteria that provide us with antibiotics
    • DOI 10.1098/rstb.2005.1758
    • Chater KF. 2006 Streptomyces inside-out: a new perspective on the bacteria that provide us with antibiotics. Phil. Trans. R. Soc. B 361, 761-768.(doi:10.1098/rstb.2005.1758) (Pubitemid 44858918)
    • (2006) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.361 , Issue.1469 , pp. 761-768
    • Chater, K.F.1
  • 2
    • 0030867564 scopus 로고    scopus 로고
    • Stimulatory effect of copper on antibiotic production and morphological differentiation in Streptomyces tanashiensis
    • Ueda K, Tomaru Y, Endoh K, Beppu T. 1997 Stimulatory effect of copper on antibiotic production and morphological differentiation in Streptomyces tanashiensis. J. Antibiot. (Tokyo) 50, 693-695. (doi:10.7164/antibiotics.50.693) (Pubitemid 27401707)
    • (1997) Journal of Antibiotics , vol.50 , Issue.8 , pp. 693-695
    • Ueda, K.1    Tomaru, Y.2    Endoh, K.3    Beppu, T.4
  • 4
    • 84862011712 scopus 로고    scopus 로고
    • Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces
    • doi:10.1111/j.1751-7915.2011.00319.x
    • Fujimoto M, Yamada A, Kurosawa J, Kawata A, Beppu T, Takano H, Ueda K. 2012 Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces. Microbial Biotechnol. 5, 477-488. (doi:10.1111/j.1751-7915. 2011.00319.x)
    • (2012) Microbial Biotechnol. , vol.5 , pp. 477-488
    • Fujimoto, M.1    Yamada, A.2    Kurosawa, J.3    Kawata, A.4    Beppu, T.5    Takano, H.6    Ueda, K.7
  • 5
    • 0025889035 scopus 로고
    • Genetic manipulation of Streptomyces: Integrating vectors and gene replacement
    • doi:10.1016/0076-6879(91)04023-H
    • Kieser T, Hopwood DA. 1991 Genetic manipulation of Streptomyces: integrating vectors and gene replacement. Methods Enzymol. 204, 430-458. (doi:10.1016/0076-6879(91)04023-H)
    • (1991) Methods Enzymol. , vol.204 , pp. 430-458
    • Kieser, T.1    Hopwood, D.A.2
  • 6
    • 38649097521 scopus 로고    scopus 로고
    • Occurrence of copper proteins through the three domains of life: A bioinformatic approach
    • DOI 10.1021/pr070480u
    • Andreini C, Banci L, Bertini I, Rosato A. 2008 Occurrence of copper proteins through the three domains of life: a bioinformatic approach. J. Proteome Res. 7, 209-216. (doi:10.1021/pr070480u) (Pubitemid 351171133)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 209-216
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 7
    • 77951990361 scopus 로고    scopus 로고
    • Copper mining in Streptomyces: Enzymes, natural products and development
    • doi:10.1039/B804465C
    • Worrall JAR, Vijgenboom E. 2010 Copper mining in Streptomyces: enzymes, natural products and development. Nat. Prod. Rep. 27, 742-756. (doi:10.1039/B804465C)
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 742-756
    • Worrall, J.A.R.1    Vijgenboom, E.2
  • 8
    • 84861206687 scopus 로고    scopus 로고
    • Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR)
    • doi:10.1074/jbc.M112.352740
    • Dwarakanath S, Chaplin AK, Hough MA, Rigali S, Vijgenboom E, Worrall JAR. 2012 Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR). J. Biol. Chem. 287, 17 833-17 847. (doi:10.1074/jbc.M112.352740)
    • (2012) J. Biol. Chem. , vol.287 , pp. 17833-17847
    • Dwarakanath, S.1    Chaplin, A.K.2    Hough, M.A.3    Rigali, S.4    Vijgenboom, E.5    Worrall, J.A.R.6
  • 10
    • 14344266861 scopus 로고    scopus 로고
    • Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins
    • DOI 10.1021/bi0480537
    • Ye Q, Imriskova-Sosova I, Hill BC, Jia Z. 2005 Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins. Biochemistry 44, 2934-2942. (doi:10.1021/bi0480537) (Pubitemid 40293668)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2934-2942
    • Ye, Q.1    Imriskova-Sosova, I.2    Hill, B.C.3    Jia, Z.4
  • 12
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.34.20531
    • Glerum DM, Shtanko A, Tzagoloff A. 1996 SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271, 20 531-20 535. (doi:10.1074/jbc.271.34.20531) (Pubitemid 26281827)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20531-20535
    • Moira Glerum, D.1    Shtanko, A.2    Tzagoloff, A.3
  • 13
    • 0033025125 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase
    • DOI 10.1007/s002940050438
    • Rentzsch A, Krummeck-Weiss G, Hofer A, Bartuschka A, Ostermann K, Rodel G. 1999 Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Curr. Genet. 35, 103-108. (doi:10.1007/s002940050438) (Pubitemid 29141252)
    • (1999) Current Genetics , vol.35 , Issue.2 , pp. 103-108
    • Rentzsch, A.1    Krummeck-Weiss, G.2    Hofer, A.3    Bartuschka, A.4    Ostermann, K.5    Rodel, G.6
  • 14
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a Protein Essential for Cytochrome c Oxidase Function Is a Cu(I)-binding Protein
    • DOI 10.1074/jbc.M107077200
    • Nittis T, George GN, Winge DR. 2001 Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J. Biol. Chem. 276, 42 520-42 526. (doi:10.1074/jbc.M107077200) (Pubitemid 37371166)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 15
    • 0034666433 scopus 로고    scopus 로고
    • Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis
    • doi:10.1074/jbc.M002741200
    • Mattatall NR, Jazairi J, Hill BC. 2000 Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J. Biol. Chem. 275, 28 802-28 809. (doi:10.1074/jbc. M002741200)
    • (2000) J. Biol. Chem. , vol.275 , pp. 28802-28809
    • Mattatall, N.R.1    Jazairi, J.2    Hill, B.C.3
  • 16
    • 28444449850 scopus 로고    scopus 로고
    • Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a homologue of the yeast mitochondrial protein Sco1p
    • DOI 10.1021/ja0529539
    • Andruzzi L, Nakano M, Nilges MJ, Blackburn NJ. 2005 Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a homologue of the yeast mitochondrial protein Sco1p. J. Am. Chem. Soc. 127, 16 548-16 558. (doi:10.1021/ja0529539) (Pubitemid 41740407)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.47 , pp. 16548-16558
    • Andruzzi, L.1    Nakano, M.2    Nilges, M.J.3    Blackburn, N.J.4
  • 17
    • 79959306944 scopus 로고    scopus 로고
    • Seeking the determinants of the elusive functions of Sco proteins
    • doi:10.1111/j.1742-4658.2011.08141.x
    • Banci L, Bertini I, Cavallaro G, Ciofi-Baffoni S. 2011 Seeking the determinants of the elusive functions of Sco proteins. FEBS J. 278, 2244-2262. (doi:10.1111/j.1742-4658.2011.08141.x)
    • (2011) FEBS J. , vol.278 , pp. 2244-2262
    • Banci, L.1    Bertini, I.2    Cavallaro, G.3    Ciofi-Baffoni, S.4
  • 20
    • 17644415027 scopus 로고    scopus 로고
    • Crystal structure of human SCO1: Implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein
    • DOI 10.1074/jbc.M410705200
    • Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA. 2005 Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase 'assembly' protein. J. Biol. Chem. 280, 15 202-15 211. (doi:10.1074/jbc.M410705200) (Pubitemid 40562876)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15202-15211
    • Williams, J.C.1    Sue, C.2    Banting, G.B.3    Yang, H.4    Glerum, D.M.5    Hendrickson, W.A.6    Schon, E.A.7
  • 22
    • 0242541974 scopus 로고    scopus 로고
    • Solution structure of Sco1: A thioredoxin-like protein involved in cytochrome c oxidase assembly
    • DOI 10.1016/j.str.2003.10.004
    • Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S. 2003 Solution structure of Sco1: a thioredoxin-like protein involved in cytochrome c oxidase assembly. Structure 11, 1431-1443. (doi:10.1016/j.str.2003.10.004) (Pubitemid 37412425)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1431-1443
    • Balatri, E.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5
  • 23
    • 29344435547 scopus 로고    scopus 로고
    • Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase
    • DOI 10.1021/bi051343i
    • Imriskova-Sosova I, Andrews D, Yam K, Davidson D, Yachnin B, Hill BC. 2005 Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase. Biochemistry 44, 16 949-16 956. (doi:10.1021/bi051343i) (Pubitemid 43007223)
    • (2005) Biochemistry , vol.44 , Issue.51 , pp. 16949-16956
    • Imriskova-Sosova, I.1    Andrews, D.2    Yam, K.3    Davidson, D.4    Yachnin, B.5    Hill, B.C.6
  • 24
    • 34548689397 scopus 로고    scopus 로고
    • PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
    • DOI 10.1016/j.febslet.2007.08.058, PII S0014579307009404
    • Badrick AC, Hamilton AJ, Bernhardt PV, Jones CE, Kappler U, Jennings MP, McEwan AG. 2007 PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity. FEBS Lett. 581, 4663-4667. (doi:10.1016/j.febslet.2007.08.058) (Pubitemid 47418791)
    • (2007) FEBS Letters , vol.581 , Issue.24 , 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
  • 26
    • 43349095381 scopus 로고    scopus 로고
    • Functional expression of the Cre recombinase in actinomycetes
    • doi:10.1007/s00253-008-1382-9
    • Fedoryshyn M, Welle E, Bechthold A, Luzhetskyy A. 2008 Functional expression of the Cre recombinase in actinomycetes. Appl. Microbiol. Biotechnol. 78, 1065-1070. (doi:10.1007/s00253-008-1382-9)
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 1065-1070
    • Fedoryshyn, M.1    Welle, E.2    Bechthold, A.3    Luzhetskyy, A.4
  • 27
    • 0024419124 scopus 로고
    • Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus)
    • Vara J, Lewandowska-Skarbek M, Wang YG, Donadio S, Hutchinson CR. 1989 Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus). J. Bacteriol. 171, 5872-5881. (Pubitemid 19266910)
    • (1989) Journal of Bacteriology , vol.171 , Issue.11 , pp. 5872-5881
    • Vara, J.1    Lewandowska-Skarbek, M.2    Wang, Y.-G.3    Donadio, S.4    Hutchinson, C.R.5
  • 28
    • 0033763852 scopus 로고    scopus 로고
    • Application of redD, the transcriptional activator gene of the undecylprodigiosin biosynthetic pathway, as a reporter for transcriptional activity in Streptomyces coelicolor A3(2) and Streptomyces lividans
    • van Wezel GP, White J, Hoogvliet G, Bibb MJ. 2000 Application of redD, the transcriptional activator gene of the undecylprodigiosin biosynthetic pathway, as a reporter for transcriptional activity in Streptomyces coelicolor A3(2) and Streptomyces lividans. J. Mol. Microbiol. Biotechnol. 2, 551-556.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 551-556
    • Van Wezel, G.P.1    White, J.2    Hoogvliet, G.3    Bibb, M.J.4
  • 29
    • 0020505048 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase
    • Green GN, Gennis RB. 1983 Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. J. Bacteriol. 154, 1269-1275. (Pubitemid 13099040)
    • (1983) Journal of Bacteriology , vol.154 , Issue.3 , pp. 1269-1275
    • Green, G.N.1    Gennis, R.B.2
  • 30
    • 0024729626 scopus 로고
    • Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis
    • Mueller JP, Taber HW. 1989 Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis. J. Bacteriol. 171, 4967-4978.
    • (1989) J. Bacteriol. , vol.171 , pp. 4967-4978
    • Mueller, J.P.1    Taber, H.W.2
  • 31
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • DOI 10.1093/nar/gkg563
    • Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A. 2003 ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31, 3784-3788. (doi:10.1093/nar/gkg563) (Pubitemid 37442246)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 32
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • DOI 10.1093/nar/gkh371
    • Whitmore L, Wallace BA. 2004 DichroWeb, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673. (doi:10.1093/nar/gkh371) (Pubitemid 38997420)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISSUE
    • Whitmore, L.1    Wallace, B.A.2
  • 33
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • doi:10.1002/bip.20853
    • Whitmore L, Wallace BA. 2008 Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89, 392-400. (doi:10.1002/bip.20853)
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 34
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton LA, Johnson Jr WC. 1986 Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155, 155-167. (doi:10.1016/0003-2697(86)90241-1) (Pubitemid 16034476)
    • (1986) Analytical Biochemistry , vol.155 , Issue.1 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 35
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • doi:10.1016/0003-2697(87)90135-7
    • Manavalan P, Johnson Jr WC. 1987 Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76-85. (doi:10.1016/0003-2697(87)90135-7)
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 36
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • DOI 10.1006/abio.2000.4879
    • Sreerama N, Venyaminov SY, Woody RW. 2000 Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochemistry 287, 243-251. (doi:10.1006/abio.2000.4879) (Pubitemid 32006233)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Yu.2    Woody, R.W.3
  • 37
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • doi:10.1021/bi00504a006
    • Provencher SW, Glockner J. 1981 Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33-37. (doi:10.1021/ bi00504a006)
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama N, Woody RW. 2000 Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260. (doi:10.1006/abio.2000.4880) (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • DOI 10.1093/bioinformatics/btl327
    • Lees JG, Miles AJ, Wien F, Wallace BA. 2006 A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22, 1955-1962. (doi:10.1093/bioinformatics/btl327) (Pubitemid 44283007)
    • (2006) Bioinformatics , vol.22 , Issue.16 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 40
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. 1979 Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632. (Pubitemid 10248727)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.19 , pp. 9627-9632
    • Holmgren, A.1
  • 41
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • doi:10.1016/0003-9861(59)90090-6
    • Ellman GL. 1959 Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77. (doi:10.1016/0003-9861(59)90090-6)
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 42
    • 77950794316 scopus 로고    scopus 로고
    • Anatomy of a red copper center: Spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-torsob Ala variants
    • doi:10.1021/ja910759v
    • Siluvai GS, Mayfield M, Nilges MJ, Debeer George S, Blackburn NJ. 2010 Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-torsob Ala variants. J. Am. Chem. Soc. 132, 5215-5226. (doi:10.1021/ja910759v)
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5215-5226
    • Siluvai, G.S.1    Mayfield, M.2    Nilges, M.J.3    Debeer George, S.4    Blackburn, N.J.5
  • 43
    • 66349133626 scopus 로고    scopus 로고
    • Probing the kinetics and thermodynamics of copper(II) binding to Bacillus subtilis Sco, a protein involved in the assembly of the Cu(A) center of cytochrome c oxidase
    • doi:10.1021/bi802288m
    • Cawthorn TR, Poulsen BE, Davidson DE, Andrews D, Hill BC. 2009 Probing the kinetics and thermodynamics of copper(II) binding to Bacillus subtilis Sco, a protein involved in the assembly of the Cu(A) center of cytochrome c oxidase. Biochemistry 48, 4448-4454. (doi:10.1021/bi802288m)
    • (2009) Biochemistry , vol.48 , pp. 4448-4454
    • Cawthorn, T.R.1    Poulsen, B.E.2    Davidson, D.E.3    Andrews, D.4    Hill, B.C.5
  • 44
    • 0024287742 scopus 로고
    • Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers
    • Calabrese L, Carbonaro M, Musci G. 1988 Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers. J. Biol. Chem. 263, 6480-6483.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6480-6483
    • Calabrese, L.1    Carbonaro, M.2    Musci, G.3
  • 46
    • 0001165206 scopus 로고
    • Solvent effects on hyperfine coupling constants in electron paramagnetic resonance spectra
    • doi:10.1021/ja01075a011
    • Ludwig P, Layloff T, Adams RN. 1964 Solvent effects on hyperfine coupling constants in electron paramagnetic resonance spectra. J. Am. Chem. Soc. 86, 4568-4573. (doi:10.1021/ja01075a011)
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 4568-4573
    • Ludwig, P.1    Layloff, T.2    Adams, R.N.3
  • 48
    • 0035873518 scopus 로고    scopus 로고
    • Crystal structure of a novel red copper protein from Nitrosomonas europaea
    • DOI 10.1021/bi0102611
    • Lieberman RL, Arciero DM, Hooper AB, Rosenzweig AC. 2001 Crystal structure of a novel red copper protein from Nitrosomonas europaea. Biochemistry 40, 5674-5681. (doi:10.1021/bi0102611) (Pubitemid 32440871)
    • (2001) Biochemistry , vol.40 , Issue.19 , pp. 5674-5681
    • Lieberman, R.L.1    Arciero, D.M.2    Hooper, A.B.3    Rosenzweig, A.C.4
  • 49
    • 14944379569 scopus 로고    scopus 로고
    • Spectroscopic and density functional studies of the red copper site in nitrosocyanin: Role of the protein in determining active site geometric and electronic structure
    • DOI 10.1021/ja044412+
    • Basumallick L, Sarangi R, DeBeer George S, Elmore B, Hooper AB, Hedman B, Hodgson KO, Solomon EI. 2005 Spectroscopic and density functional studies of the red copper site in nitrosocyanin: role of the protein in determining active site geometric and electronic structure. J. Am. Chem. Soc. 127, 3531-3544. (doi:10.1021/ja044412+) (Pubitemid 40372236)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.10 , pp. 3531-3544
    • Basumallick, L.1    Sarangi, R.2    DeBeer George, S.3    Elmore, B.4    Hooper, A.B.5    Hedman, B.6    Hodgson, K.O.7    Solomon, E.I.8
  • 50
    • 73149111478 scopus 로고    scopus 로고
    • H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco
    • doi:10.1021/bi901480g
    • Siluvai GS, Nakano MM, Mayfield M, Nilges MJ, Blackburn NJ. 2009 H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco. Biochemistry 48, 12 133-12 144. (doi:10.1021/bi901480g)
    • (2009) Biochemistry , vol.48 , pp. 12133-12144
    • Siluvai, G.S.1    Nakano, M.M.2    Mayfield, M.3    Nilges, M.J.4    Blackburn, N.J.5
  • 51
    • 77951571462 scopus 로고    scopus 로고
    • Copper metallochaperones
    • doi:10.1146/annurev-biochem-030409-143539
    • Robinson NJ, Winge DR. 2010 Copper metallochaperones. Annu. Rev. Biochem. 79, 537-562. (doi:10.1146/annurev-biochem-030409-143539)
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 537-562
    • Robinson, N.J.1    Winge, D.R.2
  • 52
    • 84860653311 scopus 로고    scopus 로고
    • The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases
    • doi:10.1016/j.bbabio.2012.01.003
    • Thompson AK, Gray J, Liu A, Hosler JP. 2012 The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases. Biochim. Biophys. Acta 1817, 955-964. (doi:10.1016/j.bbabio.2012.01.003)
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 955-964
    • Thompson, A.K.1    Gray, J.2    Liu, A.3    Hosler, J.P.4
  • 54
    • 79952575573 scopus 로고    scopus 로고
    • Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze-quench EPR study
    • doi:10.1016/j.febslet.2011.02.014
    • Bennett B, Hill BC. 2011 Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze-quench EPR study. FEBS Lett. 585, 861-864. (doi:10.1016/j.febslet.2011.02.014)
    • (2011) FEBS Lett. , vol.585 , pp. 861-864
    • Bennett, B.1    Hill, B.C.2


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