Resonance Raman spectroscopic examination of ferrochelatase-induced porphyrin distortion
(2011) In Journal of Porphyrins and Phthalocyanines 15(5-6). p.357-363- Abstract
- Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Resonance Raman spectroscopy has been instrumental in defining the distortion (mode and extent) of the porphyrin substrate, which is a critical step in the catalytic mechanism of ferrochelatase. Saddling is the predominant porphyrin out-of-plane deformation induced upon binding to ferrochelatase. Our analysis demonstrated that the intensity of the gamma(15) line, which is assigned to an out-of-plane porphyrin vibration, in resonance Raman spectra obtained for wild-type-and variant ferrochelatase-bound porphyrin, correlates with the saddling deformation undergone by the porphyrin substrate.... (More)
- Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Resonance Raman spectroscopy has been instrumental in defining the distortion (mode and extent) of the porphyrin substrate, which is a critical step in the catalytic mechanism of ferrochelatase. Saddling is the predominant porphyrin out-of-plane deformation induced upon binding to ferrochelatase. Our analysis demonstrated that the intensity of the gamma(15) line, which is assigned to an out-of-plane porphyrin vibration, in resonance Raman spectra obtained for wild-type-and variant ferrochelatase-bound porphyrin, correlates with the saddling deformation undergone by the porphyrin substrate. Further analysis of the three dimensional X-ray structures of bacterial, human and yeast ferrochelatases and the type and extent of distortion of the protein-bound porphyrin substrate and inhibitors using normal structure decomposition, support the view that ferrochelatase catalysis involves binding of a distorted porphyrin substrate and releasing of a flatter, metalated porphyrin. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2094027
- author
- Franco, Ricardo ; Al-Karadaghi, Salam LU and Ferreira, Gloria C.
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- ferrochelatase, resonance Raman, protoporphyrin IX, heme, normal, structure decomposition, tetrapyrrole, enzyme, X-ray structures
- in
- Journal of Porphyrins and Phthalocyanines
- volume
- 15
- issue
- 5-6
- pages
- 357 - 363
- publisher
- World Scientific Publishing
- external identifiers
-
- wos:000292646900006
- scopus:79960349056
- ISSN
- 1099-1409
- DOI
- 10.1142/S1088424611003380
- language
- English
- LU publication?
- yes
- id
- b07ec25c-4d41-43bf-9ebc-bcaf72c8cc2e (old id 2094027)
- date added to LUP
- 2016-04-01 10:49:39
- date last changed
- 2022-06-30 06:18:11
@article{b07ec25c-4d41-43bf-9ebc-bcaf72c8cc2e,
abstract = {{Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Resonance Raman spectroscopy has been instrumental in defining the distortion (mode and extent) of the porphyrin substrate, which is a critical step in the catalytic mechanism of ferrochelatase. Saddling is the predominant porphyrin out-of-plane deformation induced upon binding to ferrochelatase. Our analysis demonstrated that the intensity of the gamma(15) line, which is assigned to an out-of-plane porphyrin vibration, in resonance Raman spectra obtained for wild-type-and variant ferrochelatase-bound porphyrin, correlates with the saddling deformation undergone by the porphyrin substrate. Further analysis of the three dimensional X-ray structures of bacterial, human and yeast ferrochelatases and the type and extent of distortion of the protein-bound porphyrin substrate and inhibitors using normal structure decomposition, support the view that ferrochelatase catalysis involves binding of a distorted porphyrin substrate and releasing of a flatter, metalated porphyrin.}},
author = {{Franco, Ricardo and Al-Karadaghi, Salam and Ferreira, Gloria C.}},
issn = {{1099-1409}},
keywords = {{ferrochelatase; resonance Raman; protoporphyrin IX; heme; normal; structure decomposition; tetrapyrrole; enzyme; X-ray structures}},
language = {{eng}},
number = {{5-6}},
pages = {{357--363}},
publisher = {{World Scientific Publishing}},
series = {{Journal of Porphyrins and Phthalocyanines}},
title = {{Resonance Raman spectroscopic examination of ferrochelatase-induced porphyrin distortion}},
url = {{http://dx.doi.org/10.1142/S1088424611003380}},
doi = {{10.1142/S1088424611003380}},
volume = {{15}},
year = {{2011}},
}