메뉴 건너뛰기




Volumn 44, Issue 1, 2005, Pages 97-104

Anabaena flavodoxin as an electron carrier from photosystem I to ferredoxin-NADP+ reductase. Role of flavodoxin residues in protein - Protein interaction and electron transfer

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; ELECTRON TRANSITIONS; HYDROPHOBICITY; MEMBRANES; OPTIMIZATION; PHYSIOLOGY;

EID: 11844266517     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048324d     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I. A., and Stanfield, R. L. (1994) Antibody-antigen interactions: New structures and new conformational changes, Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 2
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W. L., Ultsch, M. H., de Vos, A. M., and Wells, J. A. (2000) Convergent solutions to binding at a protein-protein interface, Science 287, 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 7
    • 12144286291 scopus 로고    scopus 로고
    • + reductase with its substrates: Optimal interaction for efficient electron transfer
    • + reductase with its substrates: Optimal interaction for efficient electron transfer, Photosynth. Res. 79, 113-131.
    • (2004) Photosynth. Res. , vol.79 , pp. 113-131
    • Medina, M.1    Gómez-Moreno, C.2
  • 9
    • 0034280094 scopus 로고    scopus 로고
    • A redox dependent interaction between two electron-transfer partners involved in photosynthesis
    • Morales, R., Charon, M.-H., Kachalova, G., Serre, L., Medina, M., Gómez-Moreno, C., and Frey, M. (2000) A redox dependent interaction between two electron-transfer partners involved in photosynthesis, EMBO Rep. 1, 271-276.
    • (2000) EMBO Rep. , vol.1 , pp. 271-276
    • Morales, R.1    Charon, M.-H.2    Kachalova, G.3    Serre, L.4    Medina, M.5    Gómez-Moreno, C.6    Frey, M.7
  • 12
    • 0027982705 scopus 로고
    • + reductase system from Anabaena: Requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer
    • + reductase system from Anabaena: Requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer, Arch. Biochem. Biophys. 312, 480-486.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 480-486
    • Hurley, J.K.1    Medina, M.2    Gómez-Moreno, C.3    Tollin, G.4
  • 15
    • 0002724653 scopus 로고
    • Ferredoxins, flavodoxins and related proteins: Structure, function and evolution
    • Fay, P., and Van Baalen, C., Eds. Elsevier, Amsterdam
    • Rogers, L. J. (1987) Ferredoxins, flavodoxins and related proteins: Structure, function and evolution, in The Cyanobacteria (Fay, P., and Van Baalen, C., Eds.) pp 35-67, Elsevier, Amsterdam.
    • (1987) The Cyanobacteria , pp. 35-67
    • Rogers, L.J.1
  • 21
    • 0030953444 scopus 로고    scopus 로고
    • Negatively charged Anabaena flavodoxin residues are important for reconstitution of cytochrome P450 17a hydroxylase activity
    • Jenkins, C. M., Genzor, C. G., Fillat, M. F., Waterman, M. R., and Gómez-Moreno, C. (1997) Negatively charged Anabaena flavodoxin residues are important for reconstitution of cytochrome P450 17a hydroxylase activity, J. Biol. Chem. 272, 22509-22513.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22509-22513
    • Jenkins, C.M.1    Genzor, C.G.2    Fillat, M.F.3    Waterman, M.R.4    Gómez-Moreno, C.5
  • 23
    • 11844281093 scopus 로고    scopus 로고
    • Role of the close environment of FMN in Anabaena flavodoxin in the modulation of the flavin reduction potentials and in the energetics of the FMN:apoprotein interaction
    • in press
    • Nogués, I., Mayhew, S. G., Campos, L. A., Sancho, J., Gómez-Moreno, C., and Medina, M. (2004) Role of the close environment of FMN in Anabaena flavodoxin in the modulation of the flavin reduction potentials and in the energetics of the FMN:apoprotein interaction, Biochemistry 43 (in press).
    • (2004) Biochemistry , vol.43
    • Nogués, I.1    Mayhew, S.G.2    Campos, L.A.3    Sancho, J.4    Gómez-Moreno, C.5    Medina, M.6
  • 25
    • 0035793715 scopus 로고    scopus 로고
    • Native hydrogen bonds in a molten globule of the apoflavodoxin thermal intermediate
    • Irún, M. P., García-Mira, M. M., Sanchez-Ruiz, J. M., and Sancho, J. (2001) Native hydrogen bonds in a molten globule of the apoflavodoxin thermal intermediate, J. Mol. Biol. 306, 877-888.
    • (2001) J. Mol. Biol. , vol.306 , pp. 877-888
    • Irún, M.P.1    García-Mira, M.M.2    Sanchez-Ruiz, J.M.3    Sancho, J.4
  • 26
    • 0343431368 scopus 로고    scopus 로고
    • Stabilization of apoflavodoxin by replacing hydrogen bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln
    • Irún, M. P., Maldonado, S., and Sancho, J. (2001) Stabilization of apoflavodoxin by replacing hydrogen bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln, Protein Eng. 14, 173-181.
    • (2001) Protein Eng. , vol.14 , pp. 173-181
    • Irún, M.P.1    Maldonado, S.2    Sancho, J.3
  • 29
    • 84985110491 scopus 로고
    • Near infrared absorption spectra of the chlorophyll a cations and triplet states in vitro and in vivo
    • Mathis, P., and Sétif, P. (1981) Near infrared absorption spectra of the chlorophyll a cations and triplet states in vitro and in vivo, Isr. J. Chem. 21, 316-320.
    • (1981) Isr. J. Chem. , vol.21 , pp. 316-320
    • Mathis, P.1    Sétif, P.2
  • 30
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in β-vulgaris
    • Arnon, D. I. (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in β-vulgaris, Plant Physiol. 24, 1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 32
    • 0027319734 scopus 로고
    • Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin
    • Meyer, T. E., Zhao, Z. G., Cusanovich, M. A., and Tollin, G. (1993) Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin, Biochemistry 32, 4552-4559.
    • (1993) Biochemistry , vol.32 , pp. 4552-4559
    • Meyer, T.E.1    Zhao, Z.G.2    Cusanovich, M.A.3    Tollin, G.4
  • 33
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 35
    • 0033198021 scopus 로고    scopus 로고
    • A molecular dynamics simulation of the flavin mononucleotide-RNA aptamer complex
    • Schneider, C., and Suhnel, J. (1999) A molecular dynamics simulation of the flavin mononucleotide-RNA aptamer complex, Biopolymers 50, 287-302.
    • (1999) Biopolymers , vol.50 , pp. 287-302
    • Schneider, C.1    Suhnel, J.2
  • 36
    • 0035976018 scopus 로고    scopus 로고
    • Ferredoxin and flavodoxin reduction by photosystem I
    • Sétif, P. (2001) Ferredoxin and flavodoxin reduction by photosystem I, Biochim. Biophys. Acta 1507, 161-179.
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 161-179
    • Sétif, P.1
  • 37
    • 0026451050 scopus 로고
    • A laser flash absorption spectroscopy study of Anabaena sp. PCC 7119 flavodoxin photoreduction by photosystem I particles from spinach
    • Medina, M., Hervás, M., Navarro, J. A., de la Rosa, M. A., Gómez-Moreno, C., and Tollin, G. (1992) A laser flash absorption spectroscopy study of Anabaena sp. PCC 7119 flavodoxin photoreduction by photosystem I particles from spinach, FEBS Lett. 313, 239-242.
    • (1992) FEBS Lett. , vol.313 , pp. 239-242
    • Medina, M.1    Hervás, M.2    Navarro, J.A.3    De La Rosa, M.A.4    Gómez-Moreno, C.5    Tollin, G.6
  • 38
    • 0030021986 scopus 로고    scopus 로고
    • Laser flash absorption spectroscopy study of flavodoxin reduction by photosystem 1 in Synechococcus sp. PCC 7002
    • Mühlenhoff, U., and Sétif, P. (1996) Laser flash absorption spectroscopy study of flavodoxin reduction by photosystem 1 in Synechococcus sp. PCC 7002. Biochemistry 35, 1367-1374.
    • (1996) Biochemistry , vol.35 , pp. 1367-1374
    • Mühlenhoff, U.1    Sétif, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.