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Conference Paper

The state of association of the Na+-translocating reduced nicotinamide adenine dinucleotide: quinone oxidoreductase in detergent solution - an ultracentrifugation study

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Lancaster,  C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Tziatzios, C., Schubert, D., Schuck, P., Lancaster, C. R. D., Gennis, R. B., & Barquera, B. (2004). The state of association of the Na+-translocating reduced nicotinamide adenine dinucleotide: quinone oxidoreductase in detergent solution - an ultracentrifugation study. Progress in Colloid and Polymer Science, 127, 48-53. doi:10.1007/b98012.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DAD6-B
Abstract
Na+:reduced nicotinamide adenine dinucleotide:quinone reductase (Na+ -NQR) is a redox-driven sodium pump found in some bacterial respiratory chains. The oligomeric state of Na+-NQR from Vibrio cholerae was studied by sedimentation velocity and sedimentation equilibrium experiments in the analytical ultracentrifuge. Sedimentation velocity analysis of the purified enzyme in solutions of the nonionic detergent n-dodecyl-β-D-maltoside (Dm) revealed the presence of a nearly homogeneous protein population. From its sedimentation and diffusion coefficient, and considering reasonable amounts of Dm bound by the enzyme, it is shown that the component corresponds to monomeric Na+-NQR. This result is corroborated by sedimentation equilibrium experiments, performed under conditions of density matching for the bound detergent. No influence of NaCl on the sedimentation behaviour of Na+-NQR was detected. The amount of the protein-bound detergent was found to be about 0.57 g Dm per gram of protein.