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Resonance Raman spectroscopic examination of ferrochelatase-induced porphyrin distortion

Franco, Ricardo; Al-Karadaghi, Salam LU and Ferreira, Gloria C. (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)
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author
organization
publishing date
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
Society of Porphyrins & Phthalocyanines
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
2011-08-25 12:03:33
date last changed
2017-01-15 03:17:12
@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},
  keyword      = {ferrochelatase,resonance Raman,protoporphyrin IX,heme,normal,structure decomposition,tetrapyrrole,enzyme,X-ray structures},
  language     = {eng},
  number       = {5-6},
  pages        = {357--363},
  publisher    = {Society of Porphyrins & Phthalocyanines},
  series       = {Journal of Porphyrins and Phthalocyanines},
  title        = {Resonance Raman spectroscopic examination of ferrochelatase-induced porphyrin distortion},
  url          = {http://dx.doi.org/10.1142/S1088424611003380},
  volume       = {15},
  year         = {2011},
}