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
作者： Emma K. Wilson , Nigel S. Scrutton , Helmut Colfen , Stephen E. Harding , Michael P. Jacobsen
DOI: 10.1111/J.1432-1033.1997.0393A.X
关键词: Flavoprotein 、 Sedimentation equilibrium 、 Trimethylamine dehydrogenase 、 Electron-transferring flavoprotein 、 Chemistry 、 Stereochemistry 、 Macromolecule 、 Dissociation constant 、 Redox 、 Biophysics 、 Electron transfer
摘要: 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 15 000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, means the psi function [Wills, P.R., Jacobsen, M.P. Winzor, D. J. (1996) Biopolymers 38, 119-130] yielded an intrinsic dissociation constant 3-7 μM flavoprotein with equivalent independent sites on homodimeric enzyme. This investigation indicates potential sedimentation equilibrium quantitative characterization interactions dissimilar macromolecules.
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