메뉴 건너뛰기




Volumn 50, Issue 12, 2011, Pages 2111-2122

Swapping FAD binding motifs between plastidic and bacterial ferredoxin-NADP(H) reductases

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MOTIF; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CATALYTIC RATES; CRYSTALLOGRAPHIC STRUCTURE; CYTOCHROME C; DIAPHORASE; DIFFERENTIAL EFFECT; FLAVODOXIN; FUNCTIONAL OUTPUTS; REDUCTASE ACTIVITY; STRUCTURAL DETERMINANTS; STRUCTURAL ELEMENTS; TURNOVER RATE;

EID: 79952983138     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101772a     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 2342565785 scopus 로고    scopus 로고
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
    • DOI 10.1016/j.bbapap.2003.12.005, PII S1570963903003923
    • Ceccarelli, E. A., Arakaki, A. K., Cortez, N., and Carrillo, N. (2004) Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases Biochim. Biophys. Acta 1698, 155-165 (Pubitemid 38591470)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1698 , Issue.2 , pp. 155-165
    • Ceccarelli, E.A.1    Arakaki, A.K.2    Cortez, N.3    Carrillo, N.4
  • 5
    • 0031585989 scopus 로고    scopus 로고
    • The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution
    • DOI 10.1006/jmbi.1997.0957
    • Ingelman, M., Bianchi, V., and Eklund, H. (1997) The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution J. Mol. Biol. 268, 147-157 (Pubitemid 27192685)
    • (1997) Journal of Molecular Biology , vol.268 , Issue.1 , pp. 147-157
    • Ingelman, M.1    Bianchi, V.2    Eklund, H.3
  • 7
  • 8
    • 9744250924 scopus 로고    scopus 로고
    • Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide
    • DOI 10.1111/j.1432-1033.2004.04430.x
    • Catalano Dupuy, D. L., Rial, D. V., and Ceccarelli, E. A. (2004) Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide Eur. J. Biochem. 271, 4582-4593 (Pubitemid 39585213)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.22 , pp. 4582-4593
    • Catalano Dupuy, D.L.1    Rial, D.V.2    Ceccarelli, E.A.3
  • 9
    • 40349108840 scopus 로고    scopus 로고
    • Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site
    • DOI 10.1111/j.1742-4658.2008.06298.x
    • Musumeci, M. A., Arakaki, A. K., Rial, D. V., Catalano-Dupuy, D. L., and Ceccarelli, E. A. (2008) Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site FEBS J. 275, 1350-1366 (Pubitemid 351342228)
    • (2008) FEBS Journal , vol.275 , Issue.6 , pp. 1350-1366
    • Musumeci, M.A.1    Arakaki, A.K.2    Rial, D.V.3    Catalano-Dupuy, D.L.4    Ceccarelli, E.A.5
  • 10
    • 0032868231 scopus 로고    scopus 로고
    • Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster
    • Nakamura, M., Saeki, K., and 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 (Pubitemid 29355387)
    • (1999) Journal of Biochemistry , vol.126 , Issue.1 , pp. 10-18
    • Nakamura, M.1    Saeki, K.2    Takahashi, Y.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 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
    • DOI 10.1021/bi061152v
    • Catalano-Dupuy, D. L., Orecchia, M., Rial, D. V., and Ceccarelli, E. A. (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 (Pubitemid 44788758)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13899-13909
    • Catalano-Dupuy, D.L.1    Orecchia, M.2    Rial, D.V.3    Ceccarelli, E.A.4
  • 15
    • 34548643897 scopus 로고    scopus 로고
    • Effects of serine-to-cysteine mutations on β-lactamase folding
    • DOI 10.1529/biophysj.106.103804
    • Santos, J., Risso, V. A., Sica, M. P., and Ermacora, M. R. (2007) Effects of serine-to-cysteine mutations on β-lactamase folding Biophys. J. 93, 1707-1718 (Pubitemid 47403311)
    • (2007) Biophysical Journal , vol.93 , Issue.5 , pp. 1707-1718
    • Santos, J.1    Risso, V.A.2    Sica, M.P.3    Ermacora, M.R.4
  • 17
    • 0020185002 scopus 로고
    • + reductase. Studies on the resolution process and characterization of the FAD reconstituted holoenzyme
    • + reductase. Studies on the resolution process and characterization of the FAD reconstituted holoenzyme Eur. J. Biochem. 126, 453-458
    • (1982) Eur. J. Biochem. , vol.126 , pp. 453-458
    • Zanetti, G.1    Cidaria, D.2    Curti, B.3
  • 20
    • 0033776369 scopus 로고    scopus 로고
    • Modelling prior distributions of atoms for macromolecular refinement and completion
    • Roversi, P., Blanc, E., Vonrhein, C., Evans, G., and Bricogne, G. (2000) Modelling prior distributions of atoms for macromolecular refinement and completion Acta Crystallogr. D56, 1316-1323
    • (2000) Acta Crystallogr. , vol.56 , pp. 1316-1323
    • Roversi, P.1    Blanc, E.2    Vonrhein, C.3    Evans, G.4    Bricogne, G.5
  • 23
    • 67649170613 scopus 로고    scopus 로고
    • Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductases
    • Paladini, D. H., Musumeci, M. A., Carrillo, N., and Ceccarelli, E. A. (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
  • 34
    • 2442637815 scopus 로고    scopus 로고
    • Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin
    • DOI 10.1021/bi049858h
    • Nogues, I., Tejero, J., Hurley, J. K., Paladini, D., Frago, S., Tollin, G., Mayhew, S. G., Gomez-Moreno, C., Ceccarelli, E. A., Carrillo, N., and Medina, M. (2004) Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin Biochemistry 43, 6127-6137 (Pubitemid 38669481)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 6127-6137
    • Nogues, I.1    Tejero, J.2    Hurley, J.K.3    Paladini, D.4    Frago, S.5    Tollin, G.6    Mayhew, S.G.7    Gomez-Moreno, C.8    Ceccarelli, E.A.9    Carrillo, N.10    Medina, M.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.