The role of the lysines in the alkaline heme-linked ionization of ferric cytochrome c

Graham W. Pettigrew*, Irit Aviram, Abel Schejter

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Fully amidinated cytochrome c has a 695 nm band which is lost with a pK of 9.2 in a transition to a low-spin state. Fully maleylated cytochrome c can also exist in a low-spin state without the 695 nm band although the pH of the transition is very dependent on the salt concentration. Neither of these derivatives have free lysine groups. It is concluded that the hemelinked alkaline ionization of native cytochrome c is not triggered by deprotonation of a lysine residue, and that lysine does not necessarily coordinate the iron in the low-spin alkaline species.

Original languageEnglish
Pages (from-to)807-813
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume68
Issue number3
DOIs
StatePublished - 9 Feb 1976

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