The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis

På svenska

Author

Summary, in English

Bacillus subtilis ferrochelatase is encoded by the hemH gene of the hemEHY gene cluster and catalyses the incorporation of Fe2+ into protoporphyrin IX. B. subtilis ferrochelatase produced in Escherichia coli was purified. It was found to be a monomeric, water-soluble enzyme of molecular mass 35 kDa which in addition to Fe2+ can incorporate Zn2+ and Cu2+ into protoporphyrin IX. Chemical modification experiments indicated that the single cysteine residue in the ferrochelatase is required for enzyme activity although it is not a conserved residue compared to other ferrochelatases. In growing B. subtilis, the ferrochelatase constitutes approximately 0.05% (by mass) of the total cell protein, which corresponds to some 600 ferrochelatase molecules/cell. The turnover number of isolated ferrochelatase, 18-29 min-1, was found to be consistent with the rate of haem synthesis in exponentially growing cells (0.2 mol haem formed/min/mol enzyme). It is concluded that the B. subtilis ferrochelatase has enzymic properties which are similar to those of other characterised ferrochelatases of known primary structure, i.e. ferrochelatases of the mitochondrial inner membrane of yeast and mammalian cells. However, in contrast to these enzymes the B. subtilis enzyme is a water-soluble protein and should be more amenable to structural analysis.

Publishing year

1994

Language

English

Pages

201-208

Publication/Series

European Journal of Biochemistry

Volume

220

Issue

1

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biochemistry and Molecular Biology

Keywords

  • Gene Deletion
  • Ferrochelatase/genetics/*isolation & purification/metabolism
  • Molecular
  • Escherichia coli/enzymology/genetics
  • Cloning
  • Catalysis
  • Amino Acid Sequence
  • Bacillus subtilis/*enzymology/genetics
  • Genes
  • Bacterial
  • Kinetics
  • Molecular Sequence Data
  • Molecular Weight
  • Solubility
  • Water

Status

Published

Research group

  • Plant Biology

ISBN/ISSN/Other

  • ISSN: 0014-2956