Electron transfer in ferritin as probed by muon spin relaxtion

Article English OPEN
Telling, Mark ; Kilcoyne, Susan H. (2012)
  • Publisher: Elsevier
  • Journal: Physics Procedia, volume 30, pages 86-90 (issn: 1875-3892)
  • Related identifiers: doi: 10.1016/j.phpro.2012.04.046
  • Subject: Q1 | QC | Physics and Astronomy(all)

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.
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