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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 ; 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
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 Limited
external identifiers
  • wos:000256491900007
  • scopus:44449131445
ISSN
0264-6021
DOI
10.1042/BJ20070921
language
English
LU publication?
yes
id
485a845e-5cc9-4c6d-a1c0-154a8dbf327c (old id 1201507)
date added to LUP
2008-09-15 10:25:13
date last changed
2017-05-21 04:06:52
@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},
  keyword      = {oxygen binding,myoglobin,iron,cryoradiolytic,haem,peroxide complex},
  language     = {eng},
  pages        = {257--264},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection},
  url          = {http://dx.doi.org/10.1042/BJ20070921},
  volume       = {412},
  year         = {2008},
}