Expression studies on the ba3 quinol oxidase from Paracoccus denitrificans. A bb3 variant is enzymatically inactive

Eur J Biochem. 1997 Jun 15;246(3):618-24. doi: 10.1111/j.1432-1033.1997.00618.x.

Abstract

Expression of the quinol oxidase from Paracoccus denitrificans has been examined using a polyclonal antibody directed against subunit II and a promoter probe vector carrying the promoter region of the qox operon. Under aerobic conditions nitrate and nitrite act as specific inducers of the expression. To obtain an enzymatically competent quinol oxidase complex, an intact ctaB gene is required, which constitutes part of the cta operon coding for the aa3 cytochrome c oxidase of P. denitrificans. Deletion of ctaB leads to a change in heme composition of the quinol oxidase with heme b replacing the high-spin heme a of the binuclear center, causing loss of electron transport activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies / metabolism
  • Base Sequence
  • Blotting, Western
  • Circular Dichroism
  • Cytochrome b Group / genetics
  • Cytochrome b Group / metabolism*
  • Electron Transport Complex IV / genetics
  • Electron Transport Complex IV / metabolism*
  • Gene Expression Regulation, Bacterial
  • Gene Expression Regulation, Enzymologic
  • Heme / metabolism
  • Magnetics
  • Molecular Sequence Data
  • Nitrates / metabolism
  • Nitrites / metabolism
  • Operon
  • Paracoccus denitrificans / enzymology*
  • Paracoccus denitrificans / genetics
  • Peptide Fragments / immunology
  • Protein Conformation
  • Spectrophotometry, Atomic

Substances

  • Antibodies
  • Cytochrome b Group
  • Nitrates
  • Nitrites
  • Peptide Fragments
  • Heme
  • cytochrome ba3
  • Electron Transport Complex IV