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
- Hersleth, HP
; Ryde, Ulf
LU
; Rydberg, Patrik
LU
; Gorbitz, CH
and Andersson, KK
- organization
- publishing date
- 2006
- 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
- 2023-01-04 23:40:16
@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}},
keywords = {{mechanical calculations; radical; ferryl; X-ray diffraction; structure of intermediates; quantum}},
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}},
}