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| Content Provider | Royal Society of Chemistry (RSC) |
|---|---|
| Author | Abbruzzetti, Stefania Mozzarelli, Andrea Bruno, Stefano Faggiano, Serena Viappiani, Cristiano Grandi, Elena |
| Copyright Year | 2006 |
| Abstract | Haem proteins have long been the most studied proteins in biophysics, and have become paradigms for the characterization of fundamental biomolecular processes as ligand binding and regulatory conformational transitions. The presence of the haem prosthetic group, the absorbance spectrum of which has a ligation sensitive region conveniently located in the UV-visible range, has offered a powerful and sensitive tool for the investigation of molecular functions. The central Fe atom is capable of reversibly binding diatomic ligands, including O2, CO, and NO. The Fe-ligand bond is photolabile, and a reactive unligated state can be transiently generated with a pulsed laser. The photodissociated ligands quickly rebind to the haem and the process can be monitored by transient absorbance methods. The ligand rebinding kinetics reflects protein dynamics and ligand migration within the protein inner cavities. The characterization of these processes was done in the past mainly by low temperature experiments. The use of silica gels to trap proteins allows the characterization of internal ligand dynamics at room temperature. In order to show the potential of the laser flash photolysis techniques, combined with modern numerical analysis methods, we report experiments conducted on two non-symbiotic haemoglobins from Arabidopsis thaliana. The comparison between time courses recorded on haemoglobins in solution and encapsulated in silica gels allows for the highlighting of different interplays between protein dynamics and ligand migration. |
| Starting Page | 1109 |
| Ending Page | 1120 |
| Page Count | 12 |
| File Format | HTM / HTML PDF |
| ISSN | 1474905X |
| Volume Number | 5 |
| Issue Number | 12 |
| Journal | Photochemical & Photobiological Sciences |
| DOI | 10.1039/b610236k |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Access Restriction | Subscribed |
| Subject Keyword | Oxygen Ligand Cofactor (biochemistry) Biophysics Protein dynamics Protein Silicon dioxide Arabidopsis thaliana Numerical analysis Heme Laser Covalent bond Flash photolysis |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physical and Theoretical Chemistry |
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