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Article

Binding of S. cerevisiae iso-1 cytochrome c and its surface lysine-to-alanine variants to cardiolipin: charge effects and the role of the lipid to protein ratio.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 May 2020

Paradisi Alessandro, Bellei Marzia, Paltrinieri Licia, Bortolotti Carlo Augusto, Di Rocco Giulia, Ranieri Antonio, Borsari Marco, Sola Marco, Battistuzzi Gianantonio

Abstract excerpt

The interaction of cytochrome c with cardiolipin (CL) is a critical step in the initial stages of apoptosis and is mediated by a positively charged region on the protein surface comprising several lysine residues (site A). Here, the interaction of wt S. cerevisiae cytochrome c (ycc) and its K72A/K73A, K72A/K79A, K73A/K79A and K72A/K73A/K79A variants with CL was studied through UV-Vis and MCD spectroscopies at pH...

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Identifiers

PMID: 32189145
DOI: 10.1007/s00775-020-01776-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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