메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

A highly stable plastidic-type ferredoxin-NADP(H) reductase in the pathogenic bacterium Leptospira interrogans

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 80055026631     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026736     Document Type: Article
Times cited : (15)

References (69)
  • 1
    • 0038368151 scopus 로고    scopus 로고
    • Open questions in ferredoxin-NADP+ reductase catalytic mechanism
    • Carrillo N, Ceccarelli EA, (2003) Open questions in ferredoxin-NADP+ reductase catalytic mechanism. Eur J Biochem 270: 1900-1915.
    • (2003) Eur J Biochem , vol.270 , pp. 1900-1915
    • Carrillo, N.1    Ceccarelli, E.A.2
  • 2
    • 2342565785 scopus 로고    scopus 로고
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
    • Ceccarelli EA, Arakaki AK, Cortez N, Carrillo N, (2004) Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases. Biochim Biophys Acta 1698: 155-165.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 155-165
    • Ceccarelli, E.A.1    Arakaki, A.K.2    Cortez, N.3    Carrillo, N.4
  • 4
    • 68149170544 scopus 로고    scopus 로고
    • Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+
    • Medina M, (2009) Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+. FEBS J 276: 3942-3958.
    • (2009) FEBS J , vol.276 , pp. 3942-3958
    • Medina, M.1
  • 5
    • 35648996897 scopus 로고    scopus 로고
    • Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions
    • Wang A, Zeng Y, Han H, Weeratunga S, Morgan BN, et al. (2007) Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions. Biochemistry 46: 12198-12211.
    • (2007) Biochemistry , vol.46 , pp. 12198-12211
    • Wang, A.1    Zeng, Y.2    Han, H.3    Weeratunga, S.4    Morgan, B.N.5
  • 6
    • 62649102378 scopus 로고    scopus 로고
    • Ferredoxin-NADP+ reductase from Pseudomonas putida functions as a ferric reductase
    • Yeom J, Jeon CO, Madsen EL, Park W, (2009) Ferredoxin-NADP+ reductase from Pseudomonas putida functions as a ferric reductase. J Bacteriol 191: 1472-1479.
    • (2009) J Bacteriol , vol.191 , pp. 1472-1479
    • Yeom, J.1    Jeon, C.O.2    Madsen, E.L.3    Park, W.4
  • 7
    • 77956543070 scopus 로고    scopus 로고
    • Escherichia coli ferredoxin-NADP+ reductase and oxygen-insensitive nitroreductase are capable of functioning as ferric reductase and of driving the Fenton reaction
    • Takeda K, Sato J, Goto K, Fujita T, Watanabe T, et al. (2010) Escherichia coli ferredoxin-NADP+ reductase and oxygen-insensitive nitroreductase are capable of functioning as ferric reductase and of driving the Fenton reaction. Biometals 23: 727-737.
    • (2010) Biometals , vol.23 , pp. 727-737
    • Takeda, K.1    Sato, J.2    Goto, K.3    Fujita, T.4    Watanabe, T.5
  • 8
    • 79952983138 scopus 로고    scopus 로고
    • Swapping FAD Binding Motifs between Plastidic and Bacterial Ferredoxin-NADP(H) Reductases
    • Musumeci MA, Botti H, Buschiazzo A, Ceccarelli EA, (2011) Swapping FAD Binding Motifs between Plastidic and Bacterial Ferredoxin-NADP(H) Reductases. Biochemistry 50: 2111-2122.
    • (2011) Biochemistry , vol.50 , pp. 2111-2122
    • Musumeci, M.A.1    Botti, H.2    Buschiazzo, A.3    Ceccarelli, E.A.4
  • 9
    • 37349085779 scopus 로고    scopus 로고
    • Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+
    • Nascimento AS, Catalano-Dupuy DL, Bernardes A, de Oliveira NM, Santos MA, et al. (2007) Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+. BMC Struct Biol 7: 69.
    • (2007) BMC Struct Biol , vol.7 , pp. 69
    • Nascimento, A.S.1    Catalano-Dupuy, D.L.2    Bernardes, A.3    de Oliveira, N.M.4    Santos, M.A.5
  • 10
    • 33847093343 scopus 로고    scopus 로고
    • Ferredoxin-NADP+ reductase from Plasmodium falciparum undergoes NADP+-dependent dimerization and inactivation: functional and crystallographic analysis
    • Milani M, Balconi E, Aliverti A, Mastrangelo E, Seeber F, et al. (2007) Ferredoxin-NADP+ reductase from Plasmodium falciparum undergoes NADP+-dependent dimerization and inactivation: functional and crystallographic analysis. J Mol Biol 367: 501-513.
    • (2007) J Mol Biol , vol.367 , pp. 501-513
    • Milani, M.1    Balconi, E.2    Aliverti, A.3    Mastrangelo, E.4    Seeber, F.5
  • 11
    • 34248665846 scopus 로고    scopus 로고
    • Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase from human malaria parasite
    • Kimata-Ariga Y, Kurisu G, Kusunoki M, Aoki S, Sato D, et al. (2007) Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase from human malaria parasite. J Biochem 141: 421-428.
    • (2007) J Biochem , vol.141 , pp. 421-428
    • Kimata-Ariga, Y.1    Kurisu, G.2    Kusunoki, M.3    Aoki, S.4    Sato, D.5
  • 12
    • 27744542867 scopus 로고    scopus 로고
    • Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum
    • Rohrich RC, Englert N, Troschke K, Reichenberg A, Hintz M, et al. (2005) Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum. FEBS Lett 579: 6433-6438.
    • (2005) FEBS Lett , vol.579 , pp. 6433-6438
    • Rohrich, R.C.1    Englert, N.2    Troschke, K.3    Reichenberg, A.4    Hintz, M.5
  • 13
    • 6344292519 scopus 로고    scopus 로고
    • A single in vivo-selected point mutation in the active center of Toxoplasma gondii ferredoxin-NADP+ reductase leads to an inactive enzyme with greatly enhanced affinity for ferredoxin
    • Thomsen-Zieger N, Pandini V, Caprini G, Aliverti A, Cramer J, et al. (2004) A single in vivo-selected point mutation in the active center of Toxoplasma gondii ferredoxin-NADP+ reductase leads to an inactive enzyme with greatly enhanced affinity for ferredoxin. FEBS Lett 576: 375-380.
    • (2004) FEBS Lett , vol.576 , pp. 375-380
    • Thomsen-Zieger, N.1    Pandini, V.2    Caprini, G.3    Aliverti, A.4    Cramer, J.5
  • 15
    • 23844532238 scopus 로고    scopus 로고
    • The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites
    • Seeber F, Aliverti A, Zanetti G, (2005) The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites. Curr Pharm Des 11: 3159-3172.
    • (2005) Curr Pharm Des , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 16
    • 0037844597 scopus 로고    scopus 로고
    • Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa
    • Seeber F, (2003) Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa. Curr Drug Targets Immune Endocr Metabol Disord 3: 99-109.
    • (2003) Curr Drug Targets Immune Endocr Metabol Disord , vol.3 , pp. 99-109
    • Seeber, F.1
  • 17
    • 77954224688 scopus 로고    scopus 로고
    • Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation
    • Rather LJ, Knapp B, Haehnel W, Fuchs G, (2010) Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation. J Biol Chem 285: 20615-20624.
    • (2010) J Biol Chem , vol.285 , pp. 20615-20624
    • Rather, L.J.1    Knapp, B.2    Haehnel, W.3    Fuchs, G.4
  • 18
    • 0035101009 scopus 로고    scopus 로고
    • Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii
    • Mohamed ME, Zaar A, Ebenau-Jehle C, Fuchs G, (2001) Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii. J Bacteriol 183: 1899-1908.
    • (2001) J Bacteriol , vol.183 , pp. 1899-1908
    • Mohamed, M.E.1    Zaar, A.2    Ebenau-Jehle, C.3    Fuchs, G.4
  • 19
    • 0035937117 scopus 로고    scopus 로고
    • Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP+ reductase and ferredoxin
    • Vollmer M, Thomsen N, Wiek S, Seeber F, (2001) Apicomplexan parasites possess distinct nuclear-encoded, but apicoplast-localized, plant-type ferredoxin-NADP+ reductase and ferredoxin. J Biol Chem 276: 5483-5490.
    • (2001) J Biol Chem , vol.276 , pp. 5483-5490
    • Vollmer, M.1    Thomsen, N.2    Wiek, S.3    Seeber, F.4
  • 20
    • 0033911508 scopus 로고    scopus 로고
    • Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins
    • Onda Y, Matsumura T, Kimata-Ariga Y, Sakakibara H, Sugiyama T, et al. (2000) Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins. Plant Physiol 123: 1037-1045.
    • (2000) Plant Physiol , vol.123 , pp. 1037-1045
    • Onda, Y.1    Matsumura, T.2    Kimata-Ariga, Y.3    Sakakibara, H.4    Sugiyama, T.5
  • 21
    • 77349112000 scopus 로고    scopus 로고
    • The endosymbiotic origin, diversification and fate of plastids
    • Keeling PJ, (2010) The endosymbiotic origin, diversification and fate of plastids. Philos Trans R Soc Lond B Biol Sci 365: 729-748.
    • (2010) Philos Trans R Soc Lond B Biol Sci , vol.365 , pp. 729-748
    • Keeling, P.J.1
  • 22
    • 0033823160 scopus 로고    scopus 로고
    • The phylogeny of proteobacteria: relationships to other eubacterial phyla and eukaryotes
    • Gupta RS, (2000) The phylogeny of proteobacteria: relationships to other eubacterial phyla and eukaryotes. FEMS Microbiol Rev 24: 367-402.
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 367-402
    • Gupta, R.S.1
  • 23
    • 0037073767 scopus 로고    scopus 로고
    • Ferredoxin-NADP+ Reductase and Ferredoxin of the Protozoan Parasite Toxoplasma gondii Interact Productively in Vitro and in Vivo
    • Pandini V, Caprini G, Thomsen N, Aliverti A, Seeber F, et al. (2002) Ferredoxin-NADP+ Reductase and Ferredoxin of the Protozoan Parasite Toxoplasma gondii Interact Productively in Vitro and in Vivo. J Biol Chem 277: 48463-48471.
    • (2002) J Biol Chem , vol.277 , pp. 48463-48471
    • Pandini, V.1    Caprini, G.2    Thomsen, N.3    Aliverti, A.4    Seeber, F.5
  • 24
    • 78751489883 scopus 로고    scopus 로고
    • Identification and characterization of a novel-type ferric siderophore reductase from a gram-positive extremophile
    • Miethke M, Pierik AJ, Peuckert F, Seubert A, Marahiel MA, (2011) Identification and characterization of a novel-type ferric siderophore reductase from a gram-positive extremophile. J Biol Chem 286: 2245-2260.
    • (2011) J Biol Chem , vol.286 , pp. 2245-2260
    • Miethke, M.1    Pierik, A.J.2    Peuckert, F.3    Seubert, A.4    Marahiel, M.A.5
  • 26
    • 45849127235 scopus 로고    scopus 로고
    • Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin
    • Murray GL, Ellis KM, Lo M, Adler B, (2008) Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin. Microbes Infect 10: 791-797.
    • (2008) Microbes Infect , vol.10 , pp. 791-797
    • Murray, G.L.1    Ellis, K.M.2    Lo, M.3    Adler, B.4
  • 27
    • 33645240036 scopus 로고    scopus 로고
    • Roles of the species-specific subdomain and the N-terminal peptide of Toxoplasma gondii ferredoxin-NADP+ reductase in ferredoxin binding
    • Pandini V, Caprini G, Tedeschi G, Seeber F, Zanetti G, et al. (2006) Roles of the species-specific subdomain and the N-terminal peptide of Toxoplasma gondii ferredoxin-NADP+ reductase in ferredoxin binding. Biochemistry 45: 3563-3571.
    • (2006) Biochemistry , vol.45 , pp. 3563-3571
    • Pandini, V.1    Caprini, G.2    Tedeschi, G.3    Seeber, F.4    Zanetti, G.5
  • 28
    • 0039450620 scopus 로고    scopus 로고
    • Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer
    • Martinez-Julvez M, Medina M, Hurley JK, Hafezi R, Brodie TB, et al. (1998) Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Biochemistry 37: 13604-13613.
    • (1998) Biochemistry , vol.37 , pp. 13604-13613
    • Martinez-Julvez, M.1    Medina, M.2    Hurley, J.K.3    Hafezi, R.4    Brodie, T.B.5
  • 29
    • 80055029372 scopus 로고    scopus 로고
    • Searching for the role of the plastidic-type Ferredoxin-NADP(H) reductase in Leptospira interrogans
    • In: Frago S, Gomez-Moreno C, Medina M, editors, Prensas Universitarias de Zaragoza
    • Catalano-Dupuy DL, Ceccarelli EA, (2008) Searching for the role of the plastidic-type Ferredoxin-NADP(H) reductase in Leptospira interrogans. In: Frago S, Gomez-Moreno C, Medina M, editors. Flavins and Flavoproteins Prensas Universitarias de Zaragoza pp. 249-254.
    • (2008) Flavins and Flavoproteins , pp. 249-254
    • Catalano-Dupuy, D.L.1    Ceccarelli, E.A.2
  • 30
    • 0034647447 scopus 로고    scopus 로고
    • Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus
    • Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, et al. (2000) Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. J Mol Biol 300: 587-595.
    • (2000) J Mol Biol , vol.300 , pp. 587-595
    • Yeh, A.P.1    Chatelet, C.2    Soltis, S.M.3    Kuhn, P.4    Meyer, J.5
  • 32
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster
    • Nakamura M, Saeki K, Takahashi Y, (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. J Biochem 126: 10-18.
    • (1999) J Biochem , vol.126 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 34
    • 0033614010 scopus 로고    scopus 로고
    • Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase
    • Jung YS, Roberts VA, Stout CD, Burgess BK, (1999) Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase. J Biol Chem 274: 2978-2987.
    • (1999) J Biol Chem , vol.274 , pp. 2978-2987
    • Jung, Y.S.1    Roberts, V.A.2    Stout, C.D.3    Burgess, B.K.4
  • 35
    • 0033527754 scopus 로고    scopus 로고
    • Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein
    • Jung YS, Gao-Sheridan HS, Christiansen J, Dean DR, Burgess BK, (1999) Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein. J Biol Chem 274: 32402-32410.
    • (1999) J Biol Chem , vol.274 , pp. 32402-32410
    • Jung, Y.S.1    Gao-Sheridan, H.S.2    Christiansen, J.3    Dean, D.R.4    Burgess, B.K.5
  • 36
    • 67651166675 scopus 로고    scopus 로고
    • Guanidine hydrochloride- and urea-induced unfolding of Toxoplasma gondii ferredoxin-NADP+ reductase: stabilization of a functionally inactive holo-intermediate
    • Singh K, Bhakuni V, (2009) Guanidine hydrochloride- and urea-induced unfolding of Toxoplasma gondii ferredoxin-NADP+ reductase: stabilization of a functionally inactive holo-intermediate. J Biochem 145: 721-731.
    • (2009) J Biochem , vol.145 , pp. 721-731
    • Singh, K.1    Bhakuni, V.2
  • 37
    • 18444410750 scopus 로고    scopus 로고
    • Guanidinium chloride- and urea-induced unfolding of FprA, a mycobacterium NADPH-ferredoxin reductase: stabilization of an apo-protein by GdmCl
    • Shukla N, Bhatt AN, Aliverti A, Zanetti G, Bhakuni V, (2005) Guanidinium chloride- and urea-induced unfolding of FprA, a mycobacterium NADPH-ferredoxin reductase: stabilization of an apo-protein by GdmCl. FEBS J 272: 2216-2224.
    • (2005) FEBS J , vol.272 , pp. 2216-2224
    • Shukla, N.1    Bhatt, A.N.2    Aliverti, A.3    Zanetti, G.4    Bhakuni, V.5
  • 38
    • 0028824766 scopus 로고
    • Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase
    • Calcaterra NB, Pico GA, Orellano EG, Ottado J, Carrillo N, et al. (1995) Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase. Biochemistry 34: 12842-12848.
    • (1995) Biochemistry , vol.34 , pp. 12842-12848
    • Calcaterra, N.B.1    Pico, G.A.2    Orellano, E.G.3    Ottado, J.4    Carrillo, N.5
  • 39
    • 34247103661 scopus 로고    scopus 로고
    • Cores and pH-dependent dynamics of ferredoxin-NADP+ reductase revealed by hydrogen/deuterium exchange
    • Lee YH, Tamura K, Maeda M, Hoshino M, Sakurai K, et al. (2007) Cores and pH-dependent dynamics of ferredoxin-NADP+ reductase revealed by hydrogen/deuterium exchange. J Biol Chem 282: 5959-5967.
    • (2007) J Biol Chem , vol.282 , pp. 5959-5967
    • Lee, Y.H.1    Tamura, K.2    Maeda, M.3    Hoshino, M.4    Sakurai, K.5
  • 40
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov PL, (1996) Intermediate states in protein folding. J Mol Biol 258: 707-725.
    • (1996) J Mol Biol , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 41
    • 4043167104 scopus 로고    scopus 로고
    • Structural Aspects of Plant Ferredoxin: NADP(+) Oxidoreductases
    • Karplus PA, Faber HR, (2004) Structural Aspects of Plant Ferredoxin: NADP(+) Oxidoreductases. Photosynth Res 81: 303-315.
    • (2004) Photosynth Res , vol.81 , pp. 303-315
    • Karplus, P.A.1    Faber, H.R.2
  • 42
    • 77954758295 scopus 로고    scopus 로고
    • Role of specific residues in coenzyme binding, charge-transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase
    • Peregrina JR, Sanchez-Azqueta A, Herguedas B, Martinez-Julvez M, Medina M, (2010) Role of specific residues in coenzyme binding, charge-transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase. Biochim Biophys Acta 1797: 1638-1646.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1638-1646
    • Peregrina, J.R.1    Sanchez-Azqueta, A.2    Herguedas, B.3    Martinez-Julvez, M.4    Medina, M.5
  • 43
    • 0036305947 scopus 로고    scopus 로고
    • Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+
    • Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, et al. (2002) Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+. J Mol Biol 319: 1133-1142.
    • (2002) J Mol Biol , vol.319 , pp. 1133-1142
    • Hermoso, J.A.1    Mayoral, T.2    Faro, M.3    Gomez-Moreno, C.4    Sanz-Aparicio, J.5
  • 44
    • 67649170613 scopus 로고    scopus 로고
    • Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductases
    • Paladini DH, Musumeci MA, Carrillo N, Ceccarelli EA, (2009) Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductases. Biochemistry 48: 5760-5768.
    • (2009) Biochemistry , vol.48 , pp. 5760-5768
    • Paladini, D.H.1    Musumeci, M.A.2    Carrillo, N.3    Ceccarelli, E.A.4
  • 45
    • 1242306548 scopus 로고    scopus 로고
    • Domain exchange between isoforms of ferredoxin-NADP(+) reductase produces a functional enzyme
    • Aliverti A, Pandini V, Zanetti G, (2004) Domain exchange between isoforms of ferredoxin-NADP(+) reductase produces a functional enzyme. Biochim Biophys Acta 1696: 93-101.
    • (2004) Biochim Biophys Acta , vol.1696 , pp. 93-101
    • Aliverti, A.1    Pandini, V.2    Zanetti, G.3
  • 46
    • 44349139540 scopus 로고    scopus 로고
    • Toxoplasma gondii ferredoxin-NADP(+) reductase: Role of ionic interactions in stabilization of native conformation and structural cooperativity
    • Singh K, Bhakuni V, (2008) Toxoplasma gondii ferredoxin-NADP(+) reductase: Role of ionic interactions in stabilization of native conformation and structural cooperativity. Proteins 71: 1879-1888.
    • (2008) Proteins , vol.71 , pp. 1879-1888
    • Singh, K.1    Bhakuni, V.2
  • 47
    • 0037053356 scopus 로고    scopus 로고
    • Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP+ reductase with residual NADP+ binding domain
    • Maeda M, Hamada D, Hoshino M, Onda Y, Hase T, et al. (2002) Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP+ reductase with residual NADP+ binding domain. J Biol Chem 277: 17101-17107.
    • (2002) J Biol Chem , vol.277 , pp. 17101-17107
    • Maeda, M.1    Hamada, D.2    Hoshino, M.3    Onda, Y.4    Hase, T.5
  • 49
    • 77954365306 scopus 로고    scopus 로고
    • Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3
    • Liang X, Arunima A, Zhao Y, Bhaskaran R, Shende A, et al. (2010) Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3. Biophys J 99: 273-283.
    • (2010) Biophys J , vol.99 , pp. 273-283
    • Liang, X.1    Arunima, A.2    Zhao, Y.3    Bhaskaran, R.4    Shende, A.5
  • 50
    • 0005489171 scopus 로고
    • Studies on Leptospira icterohaemorrhagiae; survival in water and sewage; destruction in water by halogen compounds, synthetic detergents, and heat
    • Chang SL, Buckingham M, Taylor MP, (1948) Studies on Leptospira icterohaemorrhagiae; survival in water and sewage; destruction in water by halogen compounds, synthetic detergents, and heat. J Infect Dis 82: 256-266.
    • (1948) J Infect Dis , vol.82 , pp. 256-266
    • Chang, S.L.1    Buckingham, M.2    Taylor, M.P.3
  • 51
    • 73949084950 scopus 로고    scopus 로고
    • Leptospira and leptospirosis
    • Adler B, de la Pena MA, (2010) Leptospira and leptospirosis. Vet Microbiol 140: 287-296.
    • (2010) Vet Microbiol , vol.140 , pp. 287-296
    • Adler, B.1    de la Pena, M.A.2
  • 52
    • 2942720914 scopus 로고    scopus 로고
    • Cell aggregation: a mechanism of pathogenic Leptospira to survive in fresh water
    • Trueba G, Zapata S, Madrid K, Cullen P, Haake D, (2004) Cell aggregation: a mechanism of pathogenic Leptospira to survive in fresh water. Int Microbiol 7: 35-40.
    • (2004) Int Microbiol , vol.7 , pp. 35-40
    • Trueba, G.1    Zapata, S.2    Madrid, K.3    Cullen, P.4    Haake, D.5
  • 53
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer M, Knani M, Simonin P, Sutter B, Sahm H, (1993) Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem J 295 (Pt 2): 517-524.
    • (1993) Biochem J , vol.295 , Issue.Pt 2 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 54
    • 20144366218 scopus 로고    scopus 로고
    • Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1
    • Okada K, Hase T, (2005) Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J Biol Chem 280: 20672-20679.
    • (2005) J Biol Chem , vol.280 , pp. 20672-20679
    • Okada, K.1    Hase, T.2
  • 55
    • 0037464546 scopus 로고    scopus 로고
    • Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing
    • Ren SX, Fu G, Jiang XG, Zeng R, Miao YG, et al. (2003) Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 422: 888-893.
    • (2003) Nature , vol.422 , pp. 888-893
    • Ren, S.X.1    Fu, G.2    Jiang, X.G.3    Zeng, R.4    Miao, Y.G.5
  • 56
    • 33646818699 scopus 로고    scopus 로고
    • Antibiotic resistance in bacteria and its future for novel antibiotic development
    • Yoneyama H, Katsumata R, (2006) Antibiotic resistance in bacteria and its future for novel antibiotic development. Biosci Biotechnol Biochem 70: 1060-1075.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1060-1075
    • Yoneyama, H.1    Katsumata, R.2
  • 57
    • 34547603801 scopus 로고    scopus 로고
    • Evolution of function in the "two dinucleotide binding domains" flavoproteins
    • Ojha S, Meng EC, Babbitt PC, (2007) Evolution of function in the "two dinucleotide binding domains" flavoproteins. PLoS Comput Biol 3: e121.
    • (2007) PLoS Comput Biol , vol.3
    • Ojha, S.1    Meng, E.C.2    Babbitt, P.C.3
  • 58
    • 77958593629 scopus 로고    scopus 로고
    • A bacteria-specific 2[4Fe-4S] ferredoxin is essential in Pseudomonas aeruginosa
    • Elsen S, Efthymiou G, Peteinatos P, Diallinas G, Kyritsis P, et al. (2010) A bacteria-specific 2[4Fe-4S] ferredoxin is essential in Pseudomonas aeruginosa. BMC Microbiol 10: 271.
    • (2010) BMC Microbiol , vol.10 , pp. 271
    • Elsen, S.1    Efthymiou, G.2    Peteinatos, P.3    Diallinas, G.4    Kyritsis, P.5
  • 59
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J, (2000) Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17: 540-552.
    • (2000) Mol Biol Evol , vol.17 , pp. 540-552
    • Castresana, J.1
  • 60
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J, (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 61
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP, (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 62
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM, (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 65
    • 33751237715 scopus 로고    scopus 로고
    • Reduction of the pea ferredoxin-NADP(H) reductase catalytic efficiency by the structuring of a carboxyl-terminal artificial metal binding site
    • Catalano-Dupuy DL, Orecchia M, Rial DV, Ceccarelli EA, (2006) Reduction of the pea ferredoxin-NADP(H) reductase catalytic efficiency by the structuring of a carboxyl-terminal artificial metal binding site. Biochemistry 45: 13899-13909.
    • (2006) Biochemistry , vol.45 , pp. 13899-13909
    • Catalano-Dupuy, D.L.1    Orecchia, M.2    Rial, D.V.3    Ceccarelli, E.A.4
  • 66
    • 0017187522 scopus 로고
    • A lysyl residue at the NADP+ binding site of ferredoxin-NADP+ reductase
    • Zanetti G, (1976) A lysyl residue at the NADP+ binding site of ferredoxin-NADP+ reductase. Biochim Biophys Acta 445: 14-24.
    • (1976) Biochim Biophys Acta , vol.445 , pp. 14-24
    • Zanetti, G.1
  • 67
    • 34548643897 scopus 로고    scopus 로고
    • Effects of serine-to-cysteine mutations on beta-lactamase folding
    • Santos J, Risso VA, Sica MP, Ermacora MR, (2007) Effects of serine-to-cysteine mutations on beta-lactamase folding. Biophys J 93: 1707-1718.
    • (2007) Biophys J , vol.93 , pp. 1707-1718
    • Santos, J.1    Risso, V.A.2    Sica, M.P.3    Ermacora, M.R.4
  • 68
    • 0002693020 scopus 로고
    • Physical basis of the folded conformation of proteins
    • W. H. Freeman andCompany
    • Privalov PL, (1992) Physical basis of the folded conformation of proteins. Protein Folding W. H. Freeman andCompany pp. 83-126.
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 69
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.