The terminal oxidases of Paracoccus denitrificans

J.-W. de Gier, M Lübben, W N Reijnders, C A Tipker, D.J. Slotboom, R J van Spanning, A.H. Stouthamer, J. van der Oost

Research output: Contribution to JournalArticleAcademicpeer-review


Three distinct types of terminal oxidases participate in the aerobic respiratory pathways of Paracoccus denitrificans. Two alternative genes encoding subunit I of the aa3-type cytochrome c oxidase have been isolated before, namely ctaDI and ctaDII. Each of these genes can be expressed separately to complement a double mutant (delta ctaDI, delta ctaDII), indicating that they are isoforms of subunit I of the aa3-type oxidase. The genomic locus of a quinol oxidase has been isolated: cyoABC. This protohaem-containing oxidase, called cytochrome bb3, is the only quinol oxidase expressed under the conditions used. In a triple oxidase mutant (delta ctaDI, delta ctaDII, cyoB::KmR) an alternative cytochrome c oxidase has been characterized; this cbb3-type oxidase has been partially purified. Both cytochrome aa3 and cytochrome bb3 are redox-driven proton pumps. The proton-pumping capacity of cytochrome cbb3 has been analysed; arguments for and against the active transport of protons by this novel oxidase complex are discussed.

Original languageEnglish
Pages (from-to)183-96
Number of pages14
JournalMolecular Microbiology
Issue number2
Publication statusPublished - Jul 1994


  • Aerobiosis
  • Amino Acid Sequence
  • Bacterial Proteins
  • Base Sequence
  • Electron Transport
  • Electron Transport Complex IV
  • Genes, Bacterial
  • Genetic Complementation Test
  • Heme
  • Operon
  • Oxidoreductases
  • Oxygen
  • Paracoccus denitrificans
  • Protons
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Comparative Study
  • Journal Article
  • Research Support, Non-U.S. Gov't


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