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The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection

Hersleth, Hans-Petter ; Hsiao, Ya-Wen LU ; Ryde, Ulf LU orcid ; Gorbitz, Carl Henrik and Andersson, K. Kristoffer (2008) In Biochemical Journal 412. p.257-264
Abstract
Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallograpic data collection. We have generated and solved the 1.30 angstrom (1 angstrom= 0.1 nin) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe-O distance of 1.8 angstrom and O-O bond of 1.3 angstrom in accordance with a Fe-II-O-O- (or Fe-III-O-O2-) structure. The generation of... (More)
Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallograpic data collection. We have generated and solved the 1.30 angstrom (1 angstrom= 0.1 nin) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe-O distance of 1.8 angstrom and O-O bond of 1.3 angstrom in accordance with a Fe-II-O-O- (or Fe-III-O-O2-) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metal loproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O-O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
oxygen binding, myoglobin, iron, cryoradiolytic, haem, peroxide complex
in
Biochemical Journal
volume
412
pages
257 - 264
publisher
Portland Press
external identifiers
  • wos:000256491900007
  • scopus:44449131445
  • pmid:18215120
ISSN
0264-6021
DOI
10.1042/BJ20070921
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
485a845e-5cc9-4c6d-a1c0-154a8dbf327c (old id 1201507)
date added to LUP
2016-04-01 14:29:13
date last changed
2025-10-14 12:48:02
@article{485a845e-5cc9-4c6d-a1c0-154a8dbf327c,
  abstract     = {{Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallograpic data collection. We have generated and solved the 1.30 angstrom (1 angstrom= 0.1 nin) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe-O distance of 1.8 angstrom and O-O bond of 1.3 angstrom in accordance with a Fe-II-O-O- (or Fe-III-O-O2-) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metal loproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O-O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction.}},
  author       = {{Hersleth, Hans-Petter and Hsiao, Ya-Wen and Ryde, Ulf and Gorbitz, Carl Henrik and Andersson, K. Kristoffer}},
  issn         = {{0264-6021}},
  keywords     = {{oxygen binding; myoglobin; iron; cryoradiolytic; haem; peroxide complex}},
  language     = {{eng}},
  pages        = {{257--264}},
  publisher    = {{Portland Press}},
  series       = {{Biochemical Journal}},
  title        = {{The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection}},
  url          = {{https://lup.lub.lu.se/search/files/136746075/108_myo0.pdf}},
  doi          = {{10.1042/BJ20070921}},
  volume       = {{412}},
  year         = {{2008}},
}