메뉴 건너뛰기




Volumn 80, Issue 10, 1998, Pages 813-820

Apoflavodoxin: Structure, stability, and FMN binding

Author keywords

Flavodoxin; Protein ligand interaction; Protein stability; Redox potential

Indexed keywords

FLAVODOXIN;

EID: 0032179716     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)88876-8     Document Type: Conference Paper
Times cited : (17)

References (26)
  • 1
    • 0002724653 scopus 로고
    • Ferredoxins, flavodoxins and related proteins: Structure, function and evolution
    • Fay P., Van Baalen C. (Eds.), Elsevier Science Publishers, Amsterdam
    • [1] Rogers L.J., Ferredoxins, flavodoxins and related proteins: structure, function and evolution, in: Fay P., Van Baalen C. (Eds.), The cyanobacterium, Elsevier Science Publishers, Amsterdam, 1987, pp. 35-67.
    • (1987) The Cyanobacterium , pp. 35-67
    • Rogers, L.J.1
  • 2
    • 0000323018 scopus 로고
    • General properties of flavodoxins
    • Müller F. (Ed.), CRC Press, Boca Raton, Florida
    • [2] Mayhew, S.G., Tollin G., General properties of flavodoxins, in: Müller F. (Ed.), Chemistry and Biochemistry of flavoenzymes, vol III, CRC Press, Boca Raton, Florida, 1992, pp. 389-426.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 389-426
    • Mayhew, S.G.1    Tollin, G.2
  • 3
    • 0002714616 scopus 로고
    • Structure and redox properties of clostridial flavodoxin
    • Müller F. (Ed.), CRC Press, Boca Raton, Florida
    • [3] Ludwig M.L., Luschinsky C.L., Structure and redox properties of Clostridial flavodoxin, in: Müller F. (Ed.), Chemistry and Biochemistry of flavoenzymes, vol III, CRC Press, Boca Raton, Florida, 1992, pp. 427-466.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 427-466
    • Ludwig, M.L.1    Luschinsky, C.L.2
  • 6
    • 0029989460 scopus 로고    scopus 로고
    • Closure of a tyrosine/tryptophane aromatic gate leads to a compact fold in apoflavodoxin
    • [6] Genzor, C.G., Perales-Alcón, A., Sancho, J., Romero A., Closure of a tyrosine/tryptophane aromatic gate leads to a compact fold in apoflavodoxin, Nature Struct. Biol. 3 (1996) 329-332.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 329-332
    • Genzor, C.G.1    Perales-Alcón, A.2    Sancho, J.3    Romero, A.4
  • 7
    • 0026005943 scopus 로고
    • Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119
    • [7] Fillat M.F., Borrias W.E., Weisbeerk P.J., Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119, Biochem. J. 280 (1991) 187-191.
    • (1991) Biochem. J. , vol.280 , pp. 187-191
    • Fillat, M.F.1    Borrias, W.E.2    Weisbeerk, P.J.3
  • 8
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • [8] Deng W.P., Nickoloff J.A., Site-directed mutagenesis of virtually any plasmid by eliminating a unique site, Anal. Biochem. 200 (1992) 81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 10
    • 0015210981 scopus 로고
    • Chemical and physical characterization of the shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavin analog binding to the apoprotein
    • [10] Edmondson D.E., Tollin G., Chemical and physical characterization of the Shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavin analog binding to the apoprotein, Biochemistry 10 (1971) 124-132.
    • (1971) Biochemistry , vol.10 , pp. 124-132
    • Edmondson, D.E.1    Tollin, G.2
  • 12
    • 0342327312 scopus 로고    scopus 로고
    • Differential stabilisation of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials
    • [12] Lostao A., Gómez-Moreno C., Mayhew S.G., Sancho J., Differential stabilisation of the three FMN redox forms by Tyrosine 94 and Tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials, Biochemistry 36 (1997) 14334-14344.
    • (1997) Biochemistry , vol.36 , pp. 14334-14344
    • Lostao, A.1    Gómez-Moreno, C.2    Mayhew, S.G.3    Sancho, J.4
  • 13
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton T.E. (Ed.), IRL Press, Oxford
    • [13] Pace C.N., Shirley B.A., Thomson J.A., Measuring the conformational stability of a protein, in: Creighton T.E. (Ed.), Protein structure A practical approach, IRL Press, Oxford, 1989, pp. 311-330.
    • (1989) Protein Structure A Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 14
    • 0023697408 scopus 로고
    • Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • [14] Santoro M.M., Bolen D.W., Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants, Biochemistry 27 (1988) 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 15
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • [15] Privalov P.L., Stability of proteins. Small globular proteins, Adv. Protein Chem. 33 (1979) 167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 16
    • 0023442217 scopus 로고
    • Protein stability curves
    • [16] Becktel W.J., Schellman J.A., Protein stability curves, Biopolymers 26 (1987) 1859-1977.
    • (1987) Biopolymers , vol.26 , pp. 1859-1977
    • Becktel, W.J.1    Schellman, J.A.2
  • 17
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton T.E. (Ed.), Freeman, New York
    • [17] Ptitsyn O.B., The molten globule state, in: Creighton T.E. (Ed.), Protein Folding, Freeman, New York, 1992, pp. 243-300.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 18
    • 0027160575 scopus 로고
    • Structural energetics of the molten globule state
    • [18] Haynie D.T., Freire E., Structural energetics of the molten globule state, Proteins Struct. Funct. Genet. 16 (1993) 115-140.
    • (1993) Proteins Struct. Funct. Genet. , vol.16 , pp. 115-140
    • Haynie, D.T.1    Freire, E.2
  • 19
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • [19] Roder H., Elove G.A., Englander S.W., Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR, Nature 335 (1988) 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elove, G.A.2    Englander, S.W.3
  • 20
    • 0023758305 scopus 로고
    • Evidence for an early folding intermediate on the folding pathway of ribonuclease A
    • [20] Udgaonkar J.B., Baldwin R.L., Evidence for an early folding intermediate on the folding pathway of ribonuclease A, Nature 335 (1988) 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 21
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • [21] Jennings P.A., Wright P.E., Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science 262 (1993) 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 22
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • [22] Raschke T.M., Marqusee S., The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions, Nature Struct. Biol. 4 (1997) 298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 23
    • 0026511653 scopus 로고
    • Dissection of an enzyme by protein engineering. The N-and C-terminal fragments of barnase form a native-like complex with restored enzymic activity
    • [23] Sancho J., Fersht A.R., Dissection of an enzyme by protein engineering. The N-and C-terminal fragments of barnase form a native-like complex with restored enzymic activity, J. Mol. Biol. 224 (1992) 741-747.
    • (1992) J. Mol. Biol , vol.224 , pp. 741-747
    • Sancho, J.1    Fersht, A.R.2
  • 24
    • 2642674396 scopus 로고    scopus 로고
    • Cooperative stabilization of a molten globule apoflavodoxin fragment
    • [24] Maldonado S., Jiménez M.A., Langdon G.M., Sancho J., Cooperative stabilization of a molten globule apoflavodoxin fragment, Biochemistry 37 (1998) 10589-10596.
    • (1998) Biochemistry , vol.37 , pp. 10589-10596
    • Maldonado, S.1    Jiménez, M.A.2    Langdon, G.M.3    Sancho, J.4
  • 25
    • 0027955916 scopus 로고
    • Site directed mutagenesis of Tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hidenborough): Regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions
    • [25] Swenson R.P., Krey G.D., Site directed mutagenesis of Tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hidenborough): Regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions, Biochemistry 33 (1994) 8505-8514.
    • (1994) Biochemistry , vol.33 , pp. 8505-8514
    • Swenson, R.P.1    Krey, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.