Iron as a possible mediator of the oxic-to-anoxic transition in Paracoccus denitrificans

Biochem Mol Biol Int. 1997 Oct;43(2):305-10. doi: 10.1080/15216549700204081.

Abstract

Expression of the lacZ gene from the Fnr-regulated FF-melR promoter on a plasmid in iron-deprived Paracoccus denitrificans cells required not only a decreased oxygen tension but also supplementation with iron. The levels of beta-galactosidase and 5-aminolevulinate synthase showed comparable responses to changes in iron availability. The presence of soluble and particulate enzymes catalyzing the reduction of Fe(III) by NADH suggests a hypothesis in which the redox state of the cytoplasmic NAD-couple determines the concentration of free Fe(II) and thereby modulates the activity of a common regulator of the Fnr type.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5-Aminolevulinate Synthetase / genetics
  • 5-Aminolevulinate Synthetase / metabolism
  • Bacterial Proteins / pharmacology*
  • Escherichia coli Proteins*
  • Ferric Compounds / metabolism
  • Ferrous Compounds / metabolism
  • Gene Expression / drug effects
  • Iron / metabolism*
  • Iron / pharmacology
  • Iron-Sulfur Proteins / pharmacology*
  • NAD / metabolism
  • Oxidation-Reduction
  • Oxygen / pharmacology*
  • Paracoccus denitrificans / genetics
  • Paracoccus denitrificans / metabolism*
  • Transcription Factors / pharmacology
  • beta-Galactosidase / genetics
  • beta-Galactosidase / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • FNR protein, E coli
  • Ferric Compounds
  • Ferrous Compounds
  • Iron-Sulfur Proteins
  • Transcription Factors
  • NAD
  • Iron
  • 5-Aminolevulinate Synthetase
  • beta-Galactosidase
  • Oxygen