ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017
The key role played by charge in the interaction of cytochrome c with cardiolipin.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength.Journal of inorganic biochemistry · 2024Article
- Article
- Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.Molecules (Basel, Switzerland) · 2022Review
- Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022Article
- PB1F2 from Influenza A Virus Regulates the Interaction between Cytochrome C and Cardiolipin.Membranes · 2022Article
- NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin.Life (Basel, Switzerland) · 2021Article
- Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids.Journal of molecular biology · 2021Article
- The effect of cardiolipin side chain composition on cytochrome c protein conformation and peroxidase activity.Physiological reports · 2021Article
- 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 · 2020Article
- Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.Structure (London, England : 1993) · 2019Article
- CytochromeThe Journal of biological chemistry · 2019Article
- pH-Induced Switch between Different Modes of CytochromeACS omega · 2019Article
- Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.Biophysical reviews · 2018Review
- Förster Resonance Energy Transfer Study of Cytochrome c-Lipid Interactions.Journal of fluorescence · 2018Article
- New insight into the interaction of TRAF2 C-terminal domain with lipid raft microdomains.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Article
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10 authors.
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Abstract
Cytochrome c undergoes structural variations upon binding of cardiolipin, one of the phospholipids constituting the mitochondrial membrane. Although several mechanisms governing cytochrome c/cardiolipin (cyt c/CL) recognition have been proposed, the interpretation of the process remains, at least in part, unknown. To better define the steps characterizing the cyt c-CL interaction, the role of Lys72 and Lys73, two residues thought to be important in the protein/lipid binding interaction, were recently investigated by mutagenesis. The substitution of the two (positively charged) Lys residues with Asn revealed that such mutations cancel the CL-dependent peroxidase activity of cyt c; furthermore, CL does not interact with the Lys72Asn mutant. In the present paper, we extend our study to the Lys → Arg mutants to investigate the influence exerted by the charge possessed by the residues located at positions 72 and 73 on the cyt c/CL interaction. On the basis of the present work a number of overall conclusions can be drawn: (i) position 72 must be occupied by a positively charged residue to assure cyt c/CL recognition; (ii) the Arg residues located at positions 72 and 73 permit cyt c to react with CL; (iii) the replacement of Lys72 with Arg weakens the second (low-affinity) binding transition; (iv) the Lys73Arg mutation strongly increases the peroxidase activity of the CL-bound protein.
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