Chelatases: distort to select?
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/414693
- author
- Al-Karadaghi, Salam LU ; Franco, R ; Hansson, Mats LU ; Shelnutt, JA ; Isaya, G and Ferreira, GC
- organization
- publishing date
- 2006
- 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
- 2022-03-21 02:44:56
@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}},
}