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Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases

Hersleth, HP ; Ryde, Ulf LU ; Rydberg, Patrik LU ; Gorbitz, CH and Andersson, KK (2006) In Journal of Inorganic Biochemistry 100(4). p.460-476
Abstract
Peroxidases, oxygenases and catalases have similar high-valent metal-ion intermediates in their respective reaction cycles. In this review, haem-based examples will be discussed. The intermediates of the haem-containing enzymes have been extensively studied for many years by different spectroscopic methods like UV-Vis, EPR (electron paramagnetic resonance), resonance Raman, Mossbauer and MCD (magnetic circular dichroism). The first crystal structure of one of these high-valent intermediates was on cytochrome c peroxidase in 1987. Since then, structures have appeared for catalases in 1996, 2002, 2003, putatively for cytochrome P450 in 2000, for myoglobin in 2002, for horseradish peroxidase in 2002 and for cytochrome c peroxidase again in... (More)
Peroxidases, oxygenases and catalases have similar high-valent metal-ion intermediates in their respective reaction cycles. In this review, haem-based examples will be discussed. The intermediates of the haem-containing enzymes have been extensively studied for many years by different spectroscopic methods like UV-Vis, EPR (electron paramagnetic resonance), resonance Raman, Mossbauer and MCD (magnetic circular dichroism). The first crystal structure of one of these high-valent intermediates was on cytochrome c peroxidase in 1987. Since then, structures have appeared for catalases in 1996, 2002, 2003, putatively for cytochrome P450 in 2000, for myoglobin in 2002, for horseradish peroxidase in 2002 and for cytochrome c peroxidase again in 1994 and 2003. This review will focus on the most recent structural investigations for the different intermediates of these proteins. The structures of these intermediates will also be viewed in light of quantum mechanical (QM) calculations on haem models. In particular quantum refinement, which is a combination of QM calculations and crystallography, will be discussed. Only small structural changes accompany the generation of these intermediates. The crystal structures show that the compound I state, with a so called pi-cation radical on the haem group, has a relatively short iron-oxygen bond (1.67-1.76 A) in agreement with a double-bond character, while the compound 11 state or the compound I state with a radical on an amino acid residue have a relatively long iron-oxygen bond (1.86-1.92 angstrom) in agreement with a single-bond character where the oxygen-atom is protonated. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
mechanical calculations, radical, ferryl, X-ray diffraction, structure of intermediates, quantum
in
Journal of Inorganic Biochemistry
volume
100
issue
4
pages
460 - 476
publisher
Elsevier
external identifiers
  • wos:000237829000005
  • pmid:16510192
  • scopus:33645849237
ISSN
1873-3344
DOI
10.1016/j.jinorgbio.2006.01.018
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
id
e9e9dc8c-9661-4422-8b55-4569067c9f1e (old id 408306)
date added to LUP
2016-04-01 16:25:33
date last changed
2020-02-12 07:28:33
@article{e9e9dc8c-9661-4422-8b55-4569067c9f1e,
  abstract     = {Peroxidases, oxygenases and catalases have similar high-valent metal-ion intermediates in their respective reaction cycles. In this review, haem-based examples will be discussed. The intermediates of the haem-containing enzymes have been extensively studied for many years by different spectroscopic methods like UV-Vis, EPR (electron paramagnetic resonance), resonance Raman, Mossbauer and MCD (magnetic circular dichroism). The first crystal structure of one of these high-valent intermediates was on cytochrome c peroxidase in 1987. Since then, structures have appeared for catalases in 1996, 2002, 2003, putatively for cytochrome P450 in 2000, for myoglobin in 2002, for horseradish peroxidase in 2002 and for cytochrome c peroxidase again in 1994 and 2003. This review will focus on the most recent structural investigations for the different intermediates of these proteins. The structures of these intermediates will also be viewed in light of quantum mechanical (QM) calculations on haem models. In particular quantum refinement, which is a combination of QM calculations and crystallography, will be discussed. Only small structural changes accompany the generation of these intermediates. The crystal structures show that the compound I state, with a so called pi-cation radical on the haem group, has a relatively short iron-oxygen bond (1.67-1.76 A) in agreement with a double-bond character, while the compound 11 state or the compound I state with a radical on an amino acid residue have a relatively long iron-oxygen bond (1.86-1.92 angstrom) in agreement with a single-bond character where the oxygen-atom is protonated.},
  author       = {Hersleth, HP and Ryde, Ulf and Rydberg, Patrik and Gorbitz, CH and Andersson, KK},
  issn         = {1873-3344},
  language     = {eng},
  number       = {4},
  pages        = {460--476},
  publisher    = {Elsevier},
  series       = {Journal of Inorganic Biochemistry},
  title        = {Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases},
  url          = {http://dx.doi.org/10.1016/j.jinorgbio.2006.01.018},
  doi          = {10.1016/j.jinorgbio.2006.01.018},
  volume       = {100},
  year         = {2006},
}