Chelatases: distort to select?
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.
Department of Molecular Biophysics, Lund University, Box 124, SE-22100 Lund, Sweden.
Salam
S
Al-Karadaghi
Ricardo
R
Franco
Mats
M
Hansson
John A
JA
Shelnutt
Grazia
G
Isaya
Gloria C
GC
Ferreira
D000818:Animals; D002384:Catalysis; D005294:Ferrochelatase / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D033862:Iron-Binding Proteins / Q000378:metabolism; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D011166:Porphyrins / Q000378:metabolism; D011485:Protein Binding; D000096923:Frataxin
D005294:Ferrochelatase; D033862:Iron-Binding Proteins; D008670:Metals; D011166:Porphyrins; D000096923:Frataxin