Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc1 complex and the aa3-type oxidase. Evidence for the existence of an alternative cytochrome c oxidase in this bacterium

J.-W. de Gier, R J Van Spanning, L F Oltmann, A.H. Stouthamer

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

A Paracoccus denitrificans fbcC-ctaDII double mutant strain impaired in the synthesis of both the bc1 complex and the aa3-type oxidase has been constructed. This mutant strain, which is still able to grow on methylamine as sole carbon and energy source, exhibits unimpaired oxygen consumption with succinate, methylamine and endogenous substrates as electron donors. From kinetic studies of the oxidation and reduction rates of cytochromes c, it can be concluded that P. denitrificans contains a second cytochrome c oxidase, different from the aa3-type.

Original languageEnglish
Pages (from-to)23-6
Number of pages4
JournalFEBS Letters
Volume306
Issue number1
DOIs
Publication statusPublished - 13 Jul 1992

Keywords

  • Electron Transport Complex III
  • Electron Transport Complex IV
  • Genes, Bacterial
  • Kinetics
  • Methylamines
  • Mutation
  • Oxidation-Reduction
  • Oxygen Consumption
  • Paracoccus denitrificans
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity
  • Journal Article
  • Research Support, Non-U.S. Gov't

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