The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a 'g = 12' EPR feature analogous to that of 'slow' cytochrome oxidase

Melissa W. Calhoun, Robert B Gennis, John C. Salerno

Research output: Contribution to journalArticle

Abstract

The cytochrome bo quinol oxidase of Escherichia coli is homologous in sequence and in structure to cytochrome aa 3 type cytochrome oxidase in subunit 1, which contains the catalytic core. The cytochrome bo enzyme forms a formate complex which exhibits 'g = 12' and 'g = 2.9' EPR signals at X band; similar signals have previously been observed only in association with the 'slow' and formate-ligated states of cytochrome oxidase. These signals arise from transitions within integral spin multiplets identified with the homologous heme-copper binuclear catalytic centers in both enzymes.

Original languageEnglish (US)
Pages (from-to)127-129
Number of pages3
JournalFEBS Letters
Volume309
Issue number2
DOIs
StatePublished - Sep 7 1992

Keywords

  • Cytochrome bo
  • E. coli
  • EPR
  • Formate complex
  • Quinol oxidase

ASJC Scopus subject areas

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

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