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The Influence of X‐Rays on the Structural Studies of Peroxide‐Derived Myoglobin Intermediates
Author(s) -
Hersleth HansPetter,
Hsiao YaWen,
Ryde Ulf,
Görbitz Carl Henrik,
Andersson K. Kristoffer
Publication year - 2008
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200890189
Subject(s) - myoglobin , chemistry , peroxidase , heme , peroxide , reaction intermediate , photochemistry , metal , reactive intermediate , enzyme , catalysis , biochemistry , organic chemistry
In recent years, the awareness of potential radiation damage of metal centers in protein crystals during crystallographic data collection has received increasing attention. The radiation damage can lead to radiation‐induced changes and reduction of the metal sites. One of the research fields where these concerns have been comprehensively addressed is the study of the reaction intermediates of the heme peroxidase and oxygenase reaction cycles. For both the resting states and the high‐valent intermediates, the X‐rays used in the structure determination have given undesired side effects through radiation‐induced changes to the trapped intermediates. However, X‐rays have been used to generate and trap the peroxy/hydroperoxy state in crystals. In this review, the structural work and the influence of X‐rays on these intermediates in myoglobin are summarized and viewed in light of analogous studies on similar intermediates in peroxidases and oxygenases.