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  Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography.

Beitlich, T., Kühnel, K., Schulze-Briese, C., Shoeman, R. L., & Schlichting, I. (2007). Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography. Journal of Synchrotron Radiation, 14(1), 11-23. doi:10.1107/S0909049506049806.

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Beitlich, T., Author
Kühnel, K.1, Author           
Schulze-Briese, C., Author
Shoeman, R. L., Author
Schlichting, I., Author
Affiliations:
1Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society, ou_1933285              

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Free keywords: radiolytic reduction; photoreduction; myoglobin; cytochrome P450; chloroperoxidase; microspectrophotometer; energy dependence; hydrated electrons; radical scavengers; radiation damage.
 Abstract: The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed.

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Language(s): eng - English
 Dates: 2007-01-082007-01
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0909049506049806
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Title: Journal of Synchrotron Radiation
Source Genre: Journal
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Pages: - Volume / Issue: 14 (1) Sequence Number: - Start / End Page: 11 - 23 Identifier: -