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Englishusing X-ray absorption near edge structure (XANES) spectroscopy, we show that under prolonged exposure to Synchrotron X-rays, at T < 10 K, the Fe-heme in carbonmonoxy-myoglobin (MbCO) undergoes a slow two-state transition process. The final spectrum is nearly identical to that of the classical photoproduct (Mb*CO) obtained by UV-visible light illumination at 15 K. By increasing the temperature, the starting spectrum of MbCO is recovered at T > 100 K, demonstrating that the process is reversible and no damage occurred at the heme site in the time course of the experiment. Thus, the overall X-ray-induced process at low temperature is identical to the well-known (light-induced) photolysis of CO-hemeproteins.
| Titolo: | X-Ray-Induced Lysis of the Fe-O Bond in Carbonmonoxy-Myoglobin |
| Autori: | |
| Data di pubblicazione: | 2010 |
| Rivista: | |
| Abstract: | using X-ray absorption near edge structure (XANES) spectroscopy, we show that under prolonged exposure to Synchrotron X-rays, at T < 10 K, the Fe-heme in carbonmonoxy-myoglobin (MbCO) undergoes a slow two-state transition process. The final spectrum is nearly identical to that of the classical photoproduct (Mb*CO) obtained by UV-visible light illumination at 15 K. By increasing the temperature, the starting spectrum of MbCO is recovered at T > 100 K, demonstrating that the process is reversible and no damage occurred at the heme site in the time course of the experiment. Thus, the overall X-ray-induced process at low temperature is identical to the well-known (light-induced) photolysis of CO-hemeproteins. |
| Handle: | http://hdl.handle.net/11697/16412 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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