Chelatases: distort to select?

Salam Al-Karadaghi, Ricardo Franco, Mats G. Hansson, John Allen Shelnutt, Grazia Isaya, Glória C. Ferreira

Research output: Other contribution

79 Citations (Scopus)

Abstract

Chelatases catalyze the insertion of a specific metal ion into porphyrins, a key step in the synthesis of metalated tetrapyrroles that are essential for many cellular processes. Despite apparent common structural features among chelatases, no general reaction mechanism accounting for metal ion specificity has been established. We propose that chelatase-induced distortion of the porphyrin substrate not only enhances the reaction rate by decreasing the activation energy of the reaction but also modulates which divalent metal ion is incorporated into the porphyrin ring. We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. We postulate that the ferrochelatase-frataxin interaction controls the type of metal ion that is delivered to ferrochelatase.
Original languageEnglish
Number of pages8
Volume31
DOIs
Publication statusPublished - Mar 2006

Keywords

  • tetrapyrrole derivative
  • unclassified drug
  • chelatase enzyme
  • ferrochelatase
  • frataxin
  • heme
  • iron
  • lyase
  • metal ion
  • porphyrin

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