Current understanding of the function of magnesium chelatase

Biochem Soc Trans. 2002 Aug;30(4):643-5. doi: 10.1042/bst0300643.


Despite the global significance of chlorophylls and other modified tetrapyrroles, many aspects of their biosynthetic pathways are poorly understood. A key enzyme at the branch point between the haem and chlorophyll pathways, magnesium chelatase, couples the free energy of ATP hydrolysis to the insertion of magnesium into porphyrin, a process that is likely to be mediated through protein conformational changes. Conclusions from recent structural and functional studies of individual subunits are combined to provide a mechanistic outline of the full magnesium chelatase complex. Gathering further information presents a considerable challenge, and recent steps towards this goal will be introduced.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Binding Sites
  • Cyanobacteria / enzymology
  • Kinetics
  • Lyases / chemistry
  • Lyases / metabolism*
  • Porphyrins / metabolism
  • Protein Subunits / metabolism


  • Porphyrins
  • Protein Subunits
  • Adenosine Triphosphate
  • Lyases
  • magnesium chelatase