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

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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
Pages (from-to)153-156
Number of pages4
JournalFEBS Letters
Issue number1
StatePublished - Aug 20 1999


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


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