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

C. Tziatzios, D. Schubert, P. Schuck, C. R.D. Lancaster, Robert B Gennis, B. Barquera

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)48-53
Number of pages6
JournalProgress in Colloid and Polymer Science
Volume127
DOIs
StatePublished - Dec 22 2004

Keywords

  • Membrane protein
  • Sedimentation equilibrium analysis
  • Sedimentation velocity analysis
  • State of association

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Polymers and Plastics
  • Organic Chemistry
  • Colloid and Surface Chemistry
  • Materials Chemistry

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