Detergent-solubilized Escherichia coli cytochrome bo3 ubiquinol oxidase: A monomeric, not a dimeric complex

Andrej Musatov, Jaime Ortega-Lopez, Borries Demeler, Jeffrey P. Osborne, Robert B. Gennis, Neal C. Robinson

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The protein molecular weight, M(r), and hydrodynamic radius, R(s), of Triton X-100-solubilized Escherichia coli cytochrome bo3 were evaluated by computer fitting of sedimentation velocity data with finite element solutions to the Lamm equation. Detergent-solubilized cytochrome bo3 sediments as a homogeneous species with an s(20,w) of 6.75 s and a D(20,w) of 3.71x10-7 cm2/s, corresponding to a R(s) of 5.8 nm and a M(r) of 144 000±3500. The protein molecular weight agrees very well with the value of 143 929 calculated from the four known subunit sequences and the value of 143 025 measured by MALDI mass spectrometry for the histidine-tagged enzyme. We conclude that detergent-solubilized E. coli ubiquinol oxidase is a monomeric complex of the four known subunits. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)153-156
Number of pages4
JournalFEBS Letters
Volume457
Issue number1
DOIs
StatePublished - Aug 20 1999

Keywords

  • Computer analysis
  • Cytochrome bo ubiquinol oxidase
  • Escherichia coli
  • Sedimentation equilibrium
  • Sedimentation velocity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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