An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase

Emma K. Wilson; Nigel S. Scrutton; Helmut Cölfen; Stephen E. Harding; Michael P. Jacobsen; Donald J. Winzor

An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase

Emma K. Wilson, Nigel S. Scrutton, Helmut Cölfen, Stephen E. Harding, Michael P. Jacobsen, Donald J. Winzor

Research output: Contribution to journal › Article › peer-review

Abstract

The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron-transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation-equilibrium distributions obtained at 15 000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P.R., Jacobsen, M.P. and Winzor, D. J. (1996) Biopolymers 38, 119-130] has yielded an intrinsic dissociation constant of 3-7 μM for the interaction of electron-transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules.

Original language	English
Pages (from-to)	393-399
Number of pages	6
Journal	European Journal of Biochemistry
Volume	243
Issue number	1-2
Publication status	Published - 1997

Keywords

Analytical ultracentrifugation
Electron-transfer flavoprotein
Protein interaction
Trimethylamine dehydrogenase

Fingerprint

Dive into the research topics of 'An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase'. Together they form a unique fingerprint.

Cite this

Wilson, E. K., Scrutton, N. S., Cölfen, H., Harding, S. E., Jacobsen, M. P., & Winzor, D. J. (1997). An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase. European Journal of Biochemistry, 243(1-2), 393-399.

@article{db98eea1f18c4b6aa552edc572c0aa4f,

title = "An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase",

abstract = "The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron-transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation-equilibrium distributions obtained at 15 000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P.R., Jacobsen, M.P. and Winzor, D. J. (1996) Biopolymers 38, 119-130] has yielded an intrinsic dissociation constant of 3-7 μM for the interaction of electron-transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules.",

keywords = "Analytical ultracentrifugation, Electron-transfer flavoprotein, Protein interaction, Trimethylamine dehydrogenase",

author = "Wilson, {Emma K.} and Scrutton, {Nigel S.} and Helmut C{\"o}lfen and Harding, {Stephen E.} and Jacobsen, {Michael P.} and Winzor, {Donald J.}",

year = "1997",

language = "English",

volume = "243",

pages = "393--399",

journal = "European Journal of Biochemistry",

issn = "1432-1033",

publisher = "John Wiley & Sons Ltd",

number = "1-2",

}

Wilson, EK, Scrutton, NS, Cölfen, H, Harding, SE, Jacobsen, MP & Winzor, DJ 1997, 'An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase', European Journal of Biochemistry, vol. 243, no. 1-2, pp. 393-399.

An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase. / Wilson, Emma K.; Scrutton, Nigel S.; Cölfen, Helmut et al.
In: European Journal of Biochemistry, Vol. 243, No. 1-2, 1997, p. 393-399.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - An ultracentrifugal approach to quantitative characterization of the molecular assembly of a physiological electron-transfer complex. The interaction of electron-transferring flavoprotein with trimethylamine dehydrogenase

AU - Wilson, Emma K.

AU - Scrutton, Nigel S.

AU - Cölfen, Helmut

AU - Harding, Stephen E.

AU - Jacobsen, Michael P.

AU - Winzor, Donald J.

PY - 1997

Y1 - 1997

N2 - The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron-transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation-equilibrium distributions obtained at 15 000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P.R., Jacobsen, M.P. and Winzor, D. J. (1996) Biopolymers 38, 119-130] has yielded an intrinsic dissociation constant of 3-7 μM for the interaction of electron-transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules.

AB - The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron-transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation-equilibrium distributions obtained at 15 000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P.R., Jacobsen, M.P. and Winzor, D. J. (1996) Biopolymers 38, 119-130] has yielded an intrinsic dissociation constant of 3-7 μM for the interaction of electron-transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules.

KW - Analytical ultracentrifugation

KW - Electron-transfer flavoprotein

KW - Protein interaction

KW - Trimethylamine dehydrogenase

M3 - Article

SN - 1432-1033

VL - 243

SP - 393

EP - 399

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 1-2

ER -