The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates |
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Authors: | Hersleth Hans-Petter Hsiao Ya-Wen Ryde Ulf Görbitz Carl Henrik Andersson K Kristoffer |
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Affiliation: | University of Oslo, Department of Molecular Biosciences, P. O. Box 1041 Blindern, N-0316 Oslo. |
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Abstract: | 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. |
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Keywords: | Myoglobin Peroxidases Oxygenases Peroxide complex Radiation damage Iron complexes Protein structure X‐Ray crystallography Quantum refinement |
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