The oxidation of methylamine in Paracoccus denitrificans

J.-W. de Gier, J. van der Oost, N Harms, A.H. Stouthamer, R J Van Spanning

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The in vivo oxidation of methylamine has been studied in Paracoccus denitrificans. Four components are involved in the electron transfer from methylamine to oxygen; methylamine dehydrogenase (MADH), amicyanin, cytochrome c and cytochrome-c oxidase. In P. denitrificans, MADH and its electron acceptor amicyanin are indispensable for growth on methylamine. In the present study, site-directed mutants have been used to demonstrate participation of cytochrome c550 and the aa3-type cytochrome-c oxidase. Moreover, evidence is provided for the operation of alternative routes, branching from amicyanin, in which at least cytochrome c1 and the cbb3-type cytochrome-c oxidase are involved.

Original languageEnglish
Pages (from-to)148-54
Number of pages7
JournalEuropean Journal of Biochemistry
Volume229
Issue number1
DOIs
Publication statusPublished - 1 Apr 1995

Keywords

  • Methylamines
  • Mutagenesis, Site-Directed
  • Oxidation-Reduction
  • Paracoccus denitrificans
  • Journal Article
  • Research Support, Non-U.S. Gov't

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