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Chelatases: distort to select?

Al-Karadaghi, Salam LU ; Franco, R ; Hansson, Mats LU ; Shelnutt, JA ; Isaya, G and Ferreira, GC (2006) In Trends in Biochemical Sciences 31(3). p.135-142
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... (More)
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. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Trends in Biochemical Sciences
volume
31
issue
3
pages
135 - 142
publisher
Elsevier
external identifiers
  • wos:000236473700001
  • scopus:33644816286
ISSN
0167-7640
DOI
10.1016/j.tibs.2006.01.001
language
English
LU publication?
yes
id
6f4b5edd-11e2-4445-b3d7-476a23f0fef9 (old id 414693)
date added to LUP
2016-04-01 12:20:21
date last changed
2020-12-15 03:10:17
@misc{6f4b5edd-11e2-4445-b3d7-476a23f0fef9,
  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.},
  author       = {Al-Karadaghi, Salam and Franco, R and Hansson, Mats and Shelnutt, JA and Isaya, G and Ferreira, GC},
  issn         = {0167-7640},
  language     = {eng},
  number       = {3},
  pages        = {135--142},
  publisher    = {Elsevier},
  series       = {Trends in Biochemical Sciences},
  title        = {Chelatases: distort to select?},
  url          = {http://dx.doi.org/10.1016/j.tibs.2006.01.001},
  doi          = {10.1016/j.tibs.2006.01.001},
  volume       = {31},
  year         = {2006},
}