Time-Resolved X-Ray Crystallography of Heme Proteins
Heme proteins, with their natural photosensitivity, are excellent systems for the application of time-resolved crystallographic methods. Ligand dissociation can be readily initiated by a short laser pulse with global structural changes probed at the atomic level by X-rays in real time. Third-generation synchrotrons provide 100-ps X-ray pulses of sufficient intensity for monitoring very fast processes. Successful application of such time-resolved crystallographic experiments requires that the structural changes being monitored are compatible with the crystal lattice. These techniques have recently permitted observing for the first time allosteric transitions in real time for a cooperative dimeric hemoglobin.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006586
- Journal Information:
- Methods Enzymol., Journal Name: Methods Enzymol. Journal Issue: 2008 Vol. 437; ISSN 0076-6879; ISSN MENZAU
- Country of Publication:
- United States
- Language:
- ENGLISH
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