Long-Range Electron Transfer from Iron(II)-Cytochrome c to (Zinc-Cytochrome c Peroxidase)(+) within the 1: 1 Complex

Nong Liang, Chae Hee Kang, Pui Shing Ho, E. Margoliash, Brian M Hoffman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


Long-range electron transfer within crystallographically defined protein complexes can be studied by substituting zinc protoporphyrin IX for heme in one partner. Electron transfer within such a complex is initiated by flash photoproduction of the zinc protoporphyrin triplet state (3ZnP), which either can decay back to the ground state or can reduce a ferriheme partner, The redox intermediate B returns to the ground state by thermal electron transfer from Fe11P to the cation radical ZnP.+, Until now, reaction 2 has not been observed directly. This report demonstrates the process in the archetypical 1:1 protein electron transfer complex between yeast cytochrome c peroxidase (CcP) and cytochrome c (Cc) and shows that it exhibits a much more pronounced dependence on the cytochrome c employed than does the photostimulated, forward reaction. It is noteworthy that in this case the thermal reaction (2) is equivalent to the physiological oxidation of Fe11Cc by the H2O2-oxidized enzyme.

Original languageEnglish (US)
Pages (from-to)4665-4666
Number of pages2
JournalJournal of the American Chemical Society
Issue number15
StatePublished - Jan 1 1986

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Long-Range Electron Transfer from Iron(II)-Cytochrome c to (Zinc-Cytochrome c Peroxidase)(+) within the 1: 1 Complex'. Together they form a unique fingerprint.

Cite this