메뉴 건너뛰기




Volumn 125, Issue 1, 2007, Pages 159-165

Self-association of adrenodoxin studied by using analytical ultracentrifugation

Author keywords

Association constants; Sedimentation equilibrium; Sedimentation velocity; Self association; Thermodynamic non ideality

Indexed keywords

ADRENODOXIN; DIMER; MONOMER;

EID: 33750682627     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.07.011     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 0028794689 scopus 로고
    • Cytochrome P450: structure, function, and generation of reactive oxygen species
    • Bernhardt R. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol. Pharmacol. 127 (1995) 137-221
    • (1995) Rev. Physiol. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 2
    • 0030868605 scopus 로고    scopus 로고
    • Iron sulfur clusters: nature's modular, multipurpose structures
    • Beinert H., Holm R.H., and Münck E. Iron sulfur clusters: nature's modular, multipurpose structures. Science 277 (1997) 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 3
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx (4-108)
    • Müller A., Müller J.J., Muller Y.A., Uhlmann H., Bernhardt R., and Heinemann U. New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx (4-108). Structure 6 (1998) 269-280
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.J.2    Muller, Y.A.3    Uhlmann, H.4    Bernhardt, R.5    Heinemann, U.6
  • 4
    • 0033979988 scopus 로고    scopus 로고
    • The tertiary structure of full-length bovine adrenodoxin suggests functional dimers
    • Pikuleva I.A., Tesh K., Waterman M.R., and Kim Y. The tertiary structure of full-length bovine adrenodoxin suggests functional dimers. Arch. Biochem. Biophys. 373 (2000) 44-55
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 44-55
    • Pikuleva, I.A.1    Tesh, K.2    Waterman, M.R.3    Kim, Y.4
  • 5
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex structure suggests electron Transfer path in steroid biosynthesesis
    • Müller J.J., Lapko A., Bourenko G., Ruckpaul K., and Heinemann U. Adrenodoxin reductase-adrenodoxin complex structure suggests electron Transfer path in steroid biosynthesesis. J. Biol. Chem. 276 (2001) 2786-2789
    • (2001) J. Biol. Chem. , vol.276 , pp. 2786-2789
    • Müller, J.J.1    Lapko, A.2    Bourenko, G.3    Ruckpaul, K.4    Heinemann, U.5
  • 6
    • 0021351056 scopus 로고
    • Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase
    • Geren L.M., Brien O.P., Stonehuerner J., and Millett F. Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase. J. Biol. Chem. 259 (1984) 2155-2160
    • (1984) J. Biol. Chem. , vol.259 , pp. 2155-2160
    • Geren, L.M.1    Brien, O.P.2    Stonehuerner, J.3    Millett, F.4
  • 7
    • 0034819133 scopus 로고    scopus 로고
    • Covalently crosslinked complexes of bovine adrenodoxin with adrenodoxin reductase and cytochrome P450scc. Mass spectrometry and Edman degradation of complexes of the steroidogenic hydrolase system
    • Müller E.-C., Lapko A., Otto A., Müller J.J., Ruckpaul K., and Heinemann U. Covalently crosslinked complexes of bovine adrenodoxin with adrenodoxin reductase and cytochrome P450scc. Mass spectrometry and Edman degradation of complexes of the steroidogenic hydrolase system. Eur. J. Biochem. 268 (2001) 1837-1843
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1837-1843
    • Müller, E.-C.1    Lapko, A.2    Otto, A.3    Müller, J.J.4    Ruckpaul, K.5    Heinemann, U.6
  • 8
    • 0025998805 scopus 로고
    • Site-specific mutations in human ferrodoxin that affect binding to ferredoxin reductase and cytochrome P450scc
    • Coghlan V.M., and Vickery L.E. Site-specific mutations in human ferrodoxin that affect binding to ferredoxin reductase and cytochrome P450scc. J. Biol. Chem. 266 (1991) 18606-18612
    • (1991) J. Biol. Chem. , vol.266 , pp. 18606-18612
    • Coghlan, V.M.1    Vickery, L.E.2
  • 9
    • 0026488375 scopus 로고
    • Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
    • Wada A., and Waterman M.R. Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J. Biol. Chem. 267 (1992) 22877-22882
    • (1992) J. Biol. Chem. , vol.267 , pp. 22877-22882
    • Wada, A.1    Waterman, M.R.2
  • 10
    • 0035846906 scopus 로고    scopus 로고
    • The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners
    • Hannemann F., Rottmann M., Schiffer B., Zapp J., and Bernhardt R. The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners. J. Biol. Chem. 276 (2001) 1369-1375
    • (2001) J. Biol. Chem. , vol.276 , pp. 1369-1375
    • Hannemann, F.1    Rottmann, M.2    Schiffer, B.3    Zapp, J.4    Bernhardt, R.5
  • 13
    • 0018563695 scopus 로고
    • The formation of binary and ternary complexes of cytochrome P450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex. The implication in ACTH function
    • Kido T., and Kimura T. The formation of binary and ternary complexes of cytochrome P450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex. The implication in ACTH function. J. Biol. Chem. 254 (1979) 11806-11815
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 14
    • 0024539032 scopus 로고
    • Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P450scc reduction reaction
    • Hara T., and Kumura T. Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P450scc reduction reaction. J. Biochem. 105 (1989) 601-605
    • (1989) J. Biochem. , vol.105 , pp. 601-605
    • Hara, T.1    Kumura, T.2
  • 15
    • 0034675267 scopus 로고    scopus 로고
    • Evidence for the cluster model of mitochondrial steroid hydroxylase system derived from dissociation constants of the complex between adrenodoxin reductase and adrenodoxin
    • Hara T., Koba C., Takeshima M., and Sagara Y. Evidence for the cluster model of mitochondrial steroid hydroxylase system derived from dissociation constants of the complex between adrenodoxin reductase and adrenodoxin. Biochem. Biophys. Res. Commun. 276 (2000) 210-215
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 210-215
    • Hara, T.1    Koba, C.2    Takeshima, M.3    Sagara, Y.4
  • 16
    • 0021099477 scopus 로고
    • Cytochrome P450scc adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers
    • Lambeth J., and Pember O.S. Cytochrome P450scc adrenodoxin complex. Reduction properties of the substrate-associated cytochrome and relation of the reduction states of heme and iron-sulfur centers. J. Biol. Chem. 258 (1983) 5596-5602
    • (1983) J. Biol. Chem. , vol.258 , pp. 5596-5602
    • Lambeth, J.1    Pember, O.S.2
  • 17
    • 0037172776 scopus 로고    scopus 로고
    • A new electron mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin
    • Beilke D., Weiss R., Löhr F., Pristovsek P., Hannemann F., Bernhardt R., and Rüterjans H. A new electron mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin. Biochemistry 41 (2002) 7969-7978
    • (2002) Biochemistry , vol.41 , pp. 7969-7978
    • Beilke, D.1    Weiss, R.2    Löhr, F.3    Pristovsek, P.4    Hannemann, F.5    Bernhardt, R.6    Rüterjans, H.7
  • 18
    • 0034666656 scopus 로고    scopus 로고
    • Analysis of protein self-association under conditions of the thermodynamic nonideality
    • Behlke J., and Ristau O. Analysis of protein self-association under conditions of the thermodynamic nonideality. Biophys. Chemist. 87 (2000) 1-13
    • (2000) Biophys. Chemist. , vol.87 , pp. 1-13
    • Behlke, J.1    Ristau, O.2
  • 19
    • 0026496878 scopus 로고
    • Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2Fe-2S/ cluster ligands
    • Uhlmann H., Beckert V., Schwarz D., and Bernhardt R. Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2Fe-2S/ cluster ligands. Biochem. Biophys. Res. Commun. 188 (1992) 1131-1138
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1131-1138
    • Uhlmann, H.1    Beckert, V.2    Schwarz, D.3    Bernhardt, R.4
  • 20
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H., Kraft R., and Bernhardt R. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J. Biol. Chem. 269 (1994) 22557-22564
    • (1994) J. Biol. Chem. , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 21
    • 0015939436 scopus 로고
    • Studies on adrenal steroid hydroxylases. Oxidation-reduction properties of adrenal iron-sulfur proteins
    • Huang J.J., and Kimura T. Studies on adrenal steroid hydroxylases. Oxidation-reduction properties of adrenal iron-sulfur proteins. Biochemistry 12 (1973) 404-409
    • (1973) Biochemistry , vol.12 , pp. 404-409
    • Huang, J.J.1    Kimura, T.2
  • 22
    • 0015829813 scopus 로고
    • Theory of aggregation in solution: I. General equations and application to the stacking of bases, nucleosides, etc.
    • Hill T.J., and Chen Y.D. Theory of aggregation in solution: I. General equations and application to the stacking of bases, nucleosides, etc. Biopolymers 12 (1973) 1285-1312
    • (1973) Biopolymers , vol.12 , pp. 1285-1312
    • Hill, T.J.1    Chen, Y.D.2
  • 23
    • 0030064692 scopus 로고    scopus 로고
    • Direct analysis of solute self-association by sedimentation equilibrium
    • Wills P.R., Jacobsen M.P., and Winzor D.J. Direct analysis of solute self-association by sedimentation equilibrium. Biopolymers 38 (1996) 119-130
    • (1996) Biopolymers , vol.38 , pp. 119-130
    • Wills, P.R.1    Jacobsen, M.P.2    Winzor, D.J.3
  • 24
    • 0035942981 scopus 로고    scopus 로고
    • Studies of solute self-association by sedimentation equilibrium: allowance for effects of thermodynamic non-ideality beyond the consequences of nearest-neighbor interactions
    • Wills P.R., and Winzor D.J. Studies of solute self-association by sedimentation equilibrium: allowance for effects of thermodynamic non-ideality beyond the consequences of nearest-neighbor interactions. Biophys. Chemist. 91 (2001) 253-262
    • (2001) Biophys. Chemist. , vol.91 , pp. 253-262
    • Wills, P.R.1    Winzor, D.J.2
  • 25
    • 23544458810 scopus 로고
    • The statistical thermodynamics of multicomponent systems
    • McMillan W.G., and Mayer J.E. The statistical thermodynamics of multicomponent systems. J. Chem. Phys. 13 (1945) 276-305
    • (1945) J. Chem. Phys. , vol.13 , pp. 276-305
    • McMillan, W.G.1    Mayer, J.E.2
  • 26
    • 0003054946 scopus 로고    scopus 로고
    • Allowance for the thermodynamic nonideality in the analysis of sedimentation equilibrium distributions reflecting complex formation between dissimilar reactants
    • Winzor D.J., Jacobsen M.P., and Wills P.R. Allowance for the thermodynamic nonideality in the analysis of sedimentation equilibrium distributions reflecting complex formation between dissimilar reactants. Prog. Colloid & Polym. Sci. 113 (1999) 69-75
    • (1999) Prog. Colloid & Polym. Sci. , vol.113 , pp. 69-75
    • Winzor, D.J.1    Jacobsen, M.P.2    Wills, P.R.3
  • 27
    • 0001601983 scopus 로고
    • P-V-T behaviour of hard body fluids. Theory and experiment
    • Boublik T., and Nezbeda I. P-V-T behaviour of hard body fluids. Theory and experiment. Collect. Czechoslov. Chem. Commun. 51 (1986) 2301-2432
    • (1986) Collect. Czechoslov. Chem. Commun. , vol.51 , pp. 2301-2432
    • Boublik, T.1    Nezbeda, I.2
  • 28
    • 0033921410 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of mixed associations using numerical constrains to impose mass or signal conservation
    • Philo J.S. Sedimentation equilibrium analysis of mixed associations using numerical constrains to impose mass or signal conservation. Methods Enzymol. 321 (2000) 100-120
    • (2000) Methods Enzymol. , vol.321 , pp. 100-120
    • Philo, J.S.1
  • 29
    • 0003000499 scopus 로고
    • Conservation of signal: a new algorithm for the elimination of the reference concentration as an independently variable parameter in the analysis of sedimentation equilibrium
    • Schuster T.M., and Laue T.M. (Eds), Birkhauser, Boston, MA
    • Minton A.P. Conservation of signal: a new algorithm for the elimination of the reference concentration as an independently variable parameter in the analysis of sedimentation equilibrium. In: Schuster T.M., and Laue T.M. (Eds). Modern Analytical Ultracentrifugation (1994), Birkhauser, Boston, MA 81-93
    • (1994) Modern Analytical Ultracentrifugation , pp. 81-93
    • Minton, A.P.1
  • 30
    • 33750724888 scopus 로고    scopus 로고
    • Lammnum: a program to study self-associating macromolecules in sedimentation velocity experiments
    • Scott D.J., Harding S.E., and Rowe A.J. (Eds), Royal Society of Chemistry, Cambridge
    • Behlke J., and Ristau O. Lammnum: a program to study self-associating macromolecules in sedimentation velocity experiments. In: Scott D.J., Harding S.E., and Rowe A.J. (Eds). Analytical Ultracentrifugation, Techniques and Methods (2005), Royal Society of Chemistry, Cambridge 122-132
    • (2005) Analytical Ultracentrifugation, Techniques and Methods , pp. 122-132
    • Behlke, J.1    Ristau, O.2
  • 31
    • 0016702458 scopus 로고
    • Sedimentation of generalized systems of interacting particles: I. Solution of systems of complete Lamm equations
    • Claverie J.-M., Dreux H., and Cohen R. Sedimentation of generalized systems of interacting particles: I. Solution of systems of complete Lamm equations. Biopolymers 14 (1975) 1685-1700
    • (1975) Biopolymers , vol.14 , pp. 1685-1700
    • Claverie, J.-M.1    Dreux, H.2    Cohen, R.3
  • 32
    • 0003094006 scopus 로고
    • Simulation of transport experiments for interacting systems
    • Frieden C., and Nichol L.W. (Eds), Wiley, New York
    • Cox D.J., and Dale R.S. Simulation of transport experiments for interacting systems. In: Frieden C., and Nichol L.W. (Eds). Protein-Protein Interaction (1981), Wiley, New York 173-201
    • (1981) Protein-Protein Interaction , pp. 173-201
    • Cox, D.J.1    Dale, R.S.2
  • 33
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions of the Lamm equation
    • Schuck P. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions of the Lamm equation. Biophys. J. 75 (1998) 1503-1512
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 34
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), Royal Society, Cambridge
    • Laue T.M., Shah B.D., Ridgeway T.M., and Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), Royal Society, Cambridge 90-125
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 35
    • 0008566463 scopus 로고
    • General solution to the inverse problem of the differential equation of the ultracentrifuge
    • Todd G.P., and Haschemeyer R.H. General solution to the inverse problem of the differential equation of the ultracentrifuge. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 6739-6743
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 6739-6743
    • Todd, G.P.1    Haschemeyer, R.H.2
  • 36
    • 0008531095 scopus 로고
    • Reversible association processes of globular proteins: V. The study of associating systems by the methods of macromolecular physics
    • Steiner R.F. Reversible association processes of globular proteins: V. The study of associating systems by the methods of macromolecular physics. Arch. Biochem. Biophys. 49 (1954) 400-416
    • (1954) Arch. Biochem. Biophys. , vol.49 , pp. 400-416
    • Steiner, R.F.1
  • 37
    • 0014439427 scopus 로고
    • Computer simulation of sedimentation in the ultracentrifuge: IV. Sedimentation of self-associating solutes
    • Cox D.J. Computer simulation of sedimentation in the ultracentrifuge: IV. Sedimentation of self-associating solutes. Arch. Biochem. Biophys. 129 (1969) 106-123
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 106-123
    • Cox, D.J.1
  • 38
    • 0001639451 scopus 로고
    • Thermodynamic non-ideality and sedimentation equilibrium
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), Royal Society, Cambridge
    • Wills P.R., and Winzor D.J. Thermodynamic non-ideality and sedimentation equilibrium. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), Royal Society, Cambridge 311-330
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 311-330
    • Wills, P.R.1    Winzor, D.J.2
  • 39
    • 33750739905 scopus 로고    scopus 로고
    • A new possibility to recognize the concentration dependence of sedimentation coefficients
    • Behlke J., and Ristau O. A new possibility to recognize the concentration dependence of sedimentation coefficients. Prog. Colloid & Polym. Sci. 131 (2006) 29-32
    • (2006) Prog. Colloid & Polym. Sci. , vol.131 , pp. 29-32
    • Behlke, J.1    Ristau, O.2
  • 40
    • 0002792629 scopus 로고
    • The scaled particle theory for particles of arbitrary shape
    • Gibbons R.M. The scaled particle theory for particles of arbitrary shape. Mol. Phys. 17 (1969) 81-86
    • (1969) Mol. Phys. , vol.17 , pp. 81-86
    • Gibbons, R.M.1
  • 42
    • 0002926689 scopus 로고
    • The concentration dependence of sedimentation
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), Royal Society, Cambridge
    • Rowe A.J. The concentration dependence of sedimentation. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), Royal Society, Cambridge 394-406
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 394-406
    • Rowe, A.J.1
  • 43
    • 0017381152 scopus 로고
    • Analysis of non ideal behavior in concentrated hemoglobin solutions
    • Ross P.D., and Minton A.P. Analysis of non ideal behavior in concentrated hemoglobin solutions. J. Mol. Biol. 112 (1977) 437-452
    • (1977) J. Mol. Biol. , vol.112 , pp. 437-452
    • Ross, P.D.1    Minton, A.P.2
  • 44
    • 0037160547 scopus 로고    scopus 로고
    • A new approximate whole boundary solution of the Lamm equation for the analysis of sedimentation experiments
    • Behlke J., and Ristau O. A new approximate whole boundary solution of the Lamm equation for the analysis of sedimentation experiments. Biophys. Chemist. 95 (2002) 59-68
    • (2002) Biophys. Chemist. , vol.95 , pp. 59-68
    • Behlke, J.1    Ristau, O.2
  • 45
    • 0035965284 scopus 로고    scopus 로고
    • The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011β). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin
    • Schiffler B., Kiefer M., Wilken A., Hannemann F., Adolph H.W., and Bernhardt R. The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011β). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin. J. Biol. Chem. 276 (2001) 36225-36232
    • (2001) J. Biol. Chem. , vol.276 , pp. 36225-36232
    • Schiffler, B.1    Kiefer, M.2    Wilken, A.3    Hannemann, F.4    Adolph, H.W.5    Bernhardt, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.