메뉴 건너뛰기




Volumn 69, Issue 1, 1999, Pages 22-26

Dynamics of flavin in flavocytochrome b2: A fluorescence study

Author keywords

[No Author keywords available]

Indexed keywords

PICHIA ANOMALA;

EID: 0002858893     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1999.tb05301.x     Document Type: Article
Times cited : (7)

References (41)
  • 2
    • 0017708488 scopus 로고
    • Complexes entre les l(+) lactate: Cytochrome c oxidoréductases extraites des levures saccharomyces cerevisiae ou hansenula anomala et le cytochrome c de coeur de cheval
    • Prats, M. (1977) Complexes entre les L(+) lactate: cytochrome c oxidoréductases extraites des levures Saccharomyces cerevisiae ou Hansenula anomala et le cytochrome c de coeur de cheval. Biochimíe 59, 621-626.
    • (1977) Biochimíe , vol.59 , pp. 621-626
    • Prats, M.1
  • 5
    • 0027478161 scopus 로고
    • A study of the interaction between two proteins, one containing a flavin mononucleotide
    • Albani, J. (1993) A study of the interaction between two proteins, one containing a flavin mononucleotide. J. Biochem. Biophys. Methods 26, 105-112.
    • (1993) J. Biochem. Biophys. Methods , vol.26 , pp. 105-112
    • Albani, J.1
  • 7
    • 0022369577 scopus 로고
    • Fluorescence studies on the interaction between two cytochromes extracted from the yeast Hansenula anomala
    • Albani, J. (1985) Fluorescence studies on the interaction between two cytochromes extracted from the yeast Hansenula anomala. Arch. Biochem. Biophys. 243, 292-297.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 292-297
    • Albani, J.1
  • 9
    • 0022782928 scopus 로고
    • 2: Determination with singly modified carboxydinitrophenyl cytochromes c
    • 2: determination with singly modified carboxydinitrophenyl cytochromes c. J. Biochem. 100, 543-551.
    • (1986) J. Biochem. , vol.100 , pp. 543-551
    • Matsushima, A.1    Yoshimura, T.2    Aki, K.3
  • 10
    • 0023374726 scopus 로고
    • 2 and cytochrome c. Rapid kinetic characterization of the electron-transfer parameters with ionic-strength-dependence
    • 2 and cytochrome c. Rapid kinetic characterization of the electron-transfer parameters with ionic-strength-dependence. Biochem. J. 245, 159-165.
    • (1987) Biochem. J. , vol.245 , pp. 159-165
    • Capeillère-Blandin, C.1    Albani, J.2
  • 15
    • 0015212898 scopus 로고
    • 2). Relative orientations of the prosthetic heme and flavin
    • 2). Relative orientations of the prosthetic heme and flavin. Biochemistry 10, 2664-2669.
    • (1971) Biochemistry , vol.10 , pp. 2664-2669
    • Risler, J.L.1
  • 17
    • 0024960684 scopus 로고
    • Flavin and heme structures in lactate : Cytochrome c oxidoreductase: A resonance raman study
    • Desbois, A., M. Tegoni, M. Gervais and M. Lutz (1989) Flavin and heme structures in lactate : cytochrome c oxidoreductase: a resonance raman study. Biochemistry 28, 8011-8022.
    • (1989) Biochemistry , vol.28 , pp. 8011-8022
    • Desbois, A.1    Tegoni, M.2    Gervais, M.3    Lutz, M.4
  • 19
    • 0000130805 scopus 로고
    • Thermal coefficient of the frictional resistance to rotation in simple fluorophores determined by fluorescence polarization
    • Weber, G., S. F. Scarlata and M. Rholam (1984) Thermal coefficient of the frictional resistance to rotation in simple fluorophores determined by fluorescence polarization. Biochemistry 23, 6785-6788.
    • (1984) Biochemistry , vol.23 , pp. 6785-6788
    • Weber, G.1    Scarlata, S.F.2    Rholam, M.3
  • 21
    • 0013508985 scopus 로고    scopus 로고
    • Role of the carbohydrate moiety and of a-L-fucose in the stabilization and the dynamics of the Lens culinaris agglutinin-glycoprotein complex. A fluorescence study
    • Albani, J. R., H. Debray, M. Vincent and J. Gallay (1997) Role of the carbohydrate moiety and of a-L-fucose in the stabilization and the dynamics of the Lens culinaris agglutinin-glycoprotein complex. A fluorescence study. J. Fluoresc. 7, 293-298.
    • (1997) J. Fluoresc. , vol.7 , pp. 293-298
    • Albani, J.R.1    Debray, H.2    Vincent, M.3    Gallay, J.4
  • 22
    • 0030888292 scopus 로고    scopus 로고
    • Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri
    • Visser, A. J. W. G., A. Van Hoek, N. V. Visser, Y. Lee and S. Ghisla (1997) Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri. Photochem. Photobiol. 65, 570-575.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 570-575
    • Visser, A.J.W.G.1    Van Hoek, A.2    Visser, N.V.3    Lee, Y.4    Ghisla, S.5
  • 23
    • 0004409031 scopus 로고    scopus 로고
    • 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra
    • 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra. J. Fluoresc. 8, 213-224.
    • (1998) J. Fluoresc. , vol.8 , pp. 213-224
    • Albani, J.R.1
  • 24
    • 0027130836 scopus 로고
    • Flavin dynamics in oxidized Clostridium beijerinckii flavodoxin as assessed by time-resolved polarized fluorescence
    • Leenders, R., A. Van Hoek, M. Van Iersel, C. Veeger and A. J. W. G. Visser (1993) Flavin dynamics in oxidized Clostridium beijerinckii flavodoxin as assessed by time-resolved polarized fluorescence. Eur. J. Biochem. 218, 977-984.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 977-984
    • Leenders, R.1    Van Hoek, A.2    Van Iersel, M.3    Veeger, C.4    Visser, A.J.W.G.5
  • 27
    • 0014703185 scopus 로고
    • 2). 2. Revised heme extinction coefficients and minimal molecular weight
    • 2). 2. Revised heme extinction coefficients and minimal molecular weight. Eur. J. Biochem. 12, 158-164.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 158-164
    • Pajot, P.1    Groudinsky, O.2
  • 28
    • 0000597110 scopus 로고
    • Cytochrome c from vertebrate and invertebrate sources
    • Margoliash, E. and O. F. Walasek (1967) Cytochrome c from vertebrate and invertebrate sources. Methods Enzymol. 10, 339-348.
    • (1967) Methods Enzymol. , vol.10 , pp. 339-348
    • Margoliash, E.1    Walasek, O.F.2
  • 29
    • 0000171230 scopus 로고
    • A new method for preparing flavin-adenine dinucleotide
    • Whitby, L. G. (1953) A new method for preparing flavin-adenine dinucleotide. Biochem. J. 54, 437-442.
    • (1953) Biochem. J. , vol.54 , pp. 437-442
    • Whitby, L.G.1
  • 31
    • 76949127690 scopus 로고
    • Polarization of the fluorescence of macromolecules
    • Weber, G. (1952) Polarization of the fluorescence of macromolecules. Biochem. J. 51, 145-155.
    • (1952) Biochem. J. , vol.51 , pp. 145-155
    • Weber, G.1
  • 33
    • 0028961326 scopus 로고
    • Fluorescence study of the three tryptophan residues of the pore-forming domain of colicin A using multifrequency phase fluorometry
    • Vos, R., J. Izard, D. Baty and Y. Engelborghs (1995) Fluorescence study of the three tryptophan residues of the pore-forming domain of colicin A using multifrequency phase fluorometry. Biochemistry 34, 1734-1743.
    • (1995) Biochemistry , vol.34 , pp. 1734-1743
    • Vos, R.1    Izard, J.2    Baty, D.3    Engelborghs, Y.4
  • 34
    • 0030293924 scopus 로고
    • Fluorescence study of the conformational properties of recombinant tick anticoagulant peptide (Ornithodorus moubata) using multifrequency phase fluorometry
    • Sillen, A., R. Vos and Y. Engelborghs (1995) Fluorescence study of the conformational properties of recombinant tick anticoagulant peptide (Ornithodorus moubata) using multifrequency phase fluorometry. Photochem. Photobiol. 64, 785-791.
    • (1995) Photochem. Photobiol. , vol.64 , pp. 785-791
    • Sillen, A.1    Vos, R.2    Engelborghs, Y.3
  • 35
    • 0031049050 scopus 로고    scopus 로고
    • The role of time-dependent measurements in elucidating static versus dynamic quenching processes
    • Webber, S. E. (1997) The role of time-dependent measurements in elucidating static versus dynamic quenching processes. Photochem. Photobiol. 65, 33-38.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 33-38
    • Webber, S.E.1
  • 36
    • 0042468424 scopus 로고
    • Demonstration of picosecond fluorescence lifetimes of FMN in Desulfovibrio flavodoxins
    • Visser, A. I. W. G., A. Van Hoek, T. Kulinski and J. Le Gall (1987) Demonstration of picosecond fluorescence lifetimes of FMN in Desulfovibrio flavodoxins. FEBS Lett. 224, 406-410.
    • (1987) FEBS Lett. , vol.224 , pp. 406-410
    • Visser, A.I.W.G.1    Van Hoek, A.2    Kulinski, T.3    Le Gall, J.4
  • 37
    • 0026023225 scopus 로고
    • Atomic structure of ferrodoxin-NADP-reductase: Prototype for a structurally novel flavoenzyme family
    • Karplus, P. A., M. J. Daniels and J. R. Herriott (1991) Atomic structure of ferrodoxin-NADP-reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 38
    • 0026335998 scopus 로고
    • Properties of lipoamide dehydrogenase altered by site-directed mutagenesis as a key residue (1184Y) in the pyridine nucleotide binding domain
    • Maeda-Yorita, K., G. C. Russell, J. R. Guest, V. Massey and J. Wiliams (1991) Properties of lipoamide dehydrogenase altered by site-directed mutagenesis as a key residue (1184Y) in the pyridine nucleotide binding domain. Biochemistry 30, 11788-11795.
    • (1991) Biochemistry , vol.30 , pp. 11788-11795
    • Maeda-Yorita, K.1    Russell, G.C.2    Guest, J.R.3    Massey, V.4    Wiliams, J.5
  • 39
    • 0031953365 scopus 로고    scopus 로고
    • Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase
    • Van den Berg, P. A. W., A. Van Hoek, C. D. Walentas, R. N. Perham and A. J. W. G. Visser (1998) Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase. Biophys. J. 74, 2046-2058.
    • (1998) Biophys. J. , vol.74 , pp. 2046-2058
    • Van Den Berg, P.A.W.1    Van Hoek, A.2    Walentas, C.D.3    Perham, R.N.4    Visser, A.J.W.G.5
  • 40
  • 41
    • 0041466695 scopus 로고
    • 2
    • (Edited by B. Curti, S. Ronchi and G. Zanetti), Walter de Gruyter, New York
    • 2. In Flavins and Flavoproteins (Edited by B. Curti, S. Ronchi and G. Zanetti), pp. 797-800. Walter de Gruyter, New York.
    • (1990) Flavins and Flavoproteins , pp. 797-800
    • Gervais, M.1    Tegoni, M.2    Risler, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.