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Electron Transfer in Ferritin as Probed by Muon Spin Relaxation
| Content Provider | Semantic Scholar |
|---|---|
| Author | Telling, Mark T. F. Kilcoyne, Susan H. |
| Copyright Year | 2012 |
| Abstract | Electron-transfer processes play a vital role in many biological phenomena, from energy storage to photosynthesis. Positive muons allow such transfer processes in macromolecules, such as proteins, to be probed on a microscopic level. We have used this probe via muon spin relaxation (μSR) to investigate electron-transfer processes in ferritin; the normal iron storage protein. Data collected at finite fields is well described using the Risch-Kehr model at all measured temperatures with inter and intra-chain diffusion rates of 109 and 1011 rad s-1 being determined respectively. The results are compared to similar measurements on other proteins. |
| Starting Page | 86 |
| Ending Page | 90 |
| Page Count | 5 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/j.phpro.2012.04.046 |
| Alternate Webpage(s) | http://eprints.hud.ac.uk/id/eprint/12089/1/MuSR'11_Paper_138.pdf |
| Alternate Webpage(s) | https://core.ac.uk/download/pdf/82575517.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/j.phpro.2012.04.046 |
| Volume Number | 30 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
