Reductive and non-reductive mechanisms of iron assimilation by the yeast Saccharomyces cerevisiae

J Gen Microbiol. 1989 Feb;135(2):257-63. doi: 10.1099/00221287-135-2-257.


Iron reduction and uptake was studied in wild-type and haem-deficient strains of Saccharomyces cerevisiae. Haem-deficient strains lacked inducible ferri-reductase activity and were unable to take up iron from different ferric chelates such as Fe(III)-citrate or rhodoturulic acid. In contrast, ferrioxamine B was taken up actively by the mutants as well as by the wild-type strains. At a low extracellular concentration, uptake was insensitive to ferrozine and competitively inhibited by Ga(III)-desferrioxamine B. Extracellular reductive dissociation of the siderophore occurred at higher extracellular concentrations. Two mechanisms appear to contribute to the uptake of ferrioxamine B by S. cerevisiae: one with high affinity, by which the siderophore is internalized as such and another with lower affinity by which iron is dissociated from the ligand prior to uptake.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminolevulinic Acid / pharmacology
  • Culture Media
  • Deferoxamine / metabolism
  • Deferoxamine / pharmacology
  • FMN Reductase*
  • Ferric Compounds / metabolism*
  • Heme / physiology
  • Iron / pharmacology
  • Iron Chelating Agents / metabolism
  • NADH, NADPH Oxidoreductases / metabolism
  • Oxidation-Reduction
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / metabolism*


  • Culture Media
  • Ferric Compounds
  • Iron Chelating Agents
  • Heme
  • ferrioxamine B
  • ferric citrate
  • Aminolevulinic Acid
  • Iron
  • FMN Reductase
  • NADH, NADPH Oxidoreductases
  • ferric citrate iron reductase
  • Deferoxamine