Stability and functionality of cysteine-less F(O)F1 ATP synthase from Escherichia coli

Phillip H. Kuo, Christian J. Ketchum, Robert K. Nakamoto

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


All 21 native cysteines in the Escherichia coli F(O)F1 ATP synthase were replaced by alanines. In isolated E. coli membranes, ATP-dependent proton pumping, turnover of ATP hydrolysis and steady-state transition state thermodynamic parameters of the cysteine-less enzyme were similar to wild- type. The cysteine-less enzyme was solubilized in n-octyl β-D- glucopyranoside, purified by affinity chromatography, and reconstituted into pre-formed liposomes made from E. coli lipids. The properties of the reconstituted, purified enzyme were not significantly different from the membranous enzyme. These data demonstrate that cysteine-less F(O)F1 is biochemically stable and has functionality similar to wild-type.

Original languageEnglish (US)
Pages (from-to)217-220
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - Apr 17 1998


  • ATP synthase
  • Bioenergetics
  • Cysteine
  • Proton pumping
  • Purification
  • Reconstitution

ASJC Scopus subject areas

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


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