Amyloid fibril formation by a helical cytochrome

Thelma A. Pertinhez, Mario Bouchard, Esther J. Tomlinson, Rachel Wain, Stuart J. Ferguson, Christopher M. Dobson, Lorna J. Smith

Research output: Contribution to journalArticle


The substitution of alanines for the two cysteines which form thioether linkages to the haem group in cytochrome c552 from Hydogenobacter thermophilus destabilises the native protein fold. The holo form of this variant slowly converts into a partially folded apo state that over prolonged periods of time aggregates into fibrillar structures. Characterisation of these structures by electron microscopy and thioflavin-T binding assays shows that they are amyloid fibrils. The data demonstrate that when the native state of this cytochrome is destabilised by loss of haem, even this highly α-helical protein can form β-sheet structures of the type most commonly associated with protein deposition diseases.

Original languageEnglish
Pages (from-to)184-186
Number of pages3
JournalFEBS Letters
Issue number3
Publication statusPublished - Apr 27 2001



  • Amyloid fibril
  • Circular dichroism
  • Cytochrome c
  • Electron microscopy

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Pertinhez, T. A., Bouchard, M., Tomlinson, E. J., Wain, R., Ferguson, S. J., Dobson, C. M., & Smith, L. J. (2001). Amyloid fibril formation by a helical cytochrome. FEBS Letters, 495(3), 184-186.