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Chelatases: distort to select?

Authors
Journal
Trends in Biochemical Sciences
0968-0004
Publisher
Elsevier
Publication Date
Volume
31
Issue
3
Identifiers
DOI: 10.1016/j.tibs.2006.01.001

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.

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