Intra- and inter-molecular electron transfer in cytochrome c and myoglobin observed by the muon spin relaxation method

K. Nagamine, F. L. Pratt, S. Ohira, I. Watanabe, K. Ishida, S. N. Nakamura, T. Matsuzaki

Research output: Contribution to journalConference articlepeer-review

23 Citations (Scopus)

Abstract

Rapid electron motion in the proteins, cytochrome c and myoglobin has been studied using muon spin relaxation. Measurements between 5 and 300 K show that the inter-site diffusion rate for the topologically 1D motion along the polypeptide chain is only weakly dependent on temperature. Evidence for an increase in higher dimensional motion is seen around 200 K in cytochrome c, apparently reflecting structural change. For myoglobin the variation with temperature is different, reflecting the different protein dynamics of this molecule.

Original languageEnglish
Pages (from-to)631-635
Number of pages5
JournalPhysica B: Condensed Matter
Volume289-290
DOIs
Publication statusPublished - 2000 Aug
Externally publishedYes
Event8th International Conference on Muon Spin Rotation, Relaxation and Resonance (muSR'99) - Les Diablerets, Switz
Duration: 1999 Aug 301999 Sept 3

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Electrical and Electronic Engineering

Fingerprint

Dive into the research topics of 'Intra- and inter-molecular electron transfer in cytochrome c and myoglobin observed by the muon spin relaxation method'. Together they form a unique fingerprint.

Cite this