ArticleThe Journal of biological chemistry2015
Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 61 citations in OpenAlex.
- Tyrosine 48 Phosphorylation of CytochromeBiomolecules · 2026Article
- In silico study of cytochrome-C binding to a cardiolipin-containing membrane.European biophysics journal : EBJ · 2026Article
- Probing the Interactions of Cytochrome c with Anionic Phospholipid Nanodiscs Using Millisecond Hydrogen-Deuterium Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Cardiac Tyrosine 97 Phosphorylation of CytochromeInternational journal of molecular sciences · 2025Article
- Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities.Biomolecules · 2025Review
- Advances in utilizing reverse micelles to investigate membrane proteins.Biochemical Society transactions · 2024Review
- Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation.Biophysical chemistry · 2024Article
- An NMR Approach for Investigating Membrane Protein-Lipid Interactions Using Native Reverse Micelles.Bio-protocol · 2024Article
- Phosphorylations and Acetylations of CytochromeCells · 2024Review
- 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
- 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
- Cytochrome c phosphorylation: Control of mitochondrial electron transport chain flux and apoptosis.The international journal of biochemistry & cell biology · 2020Article
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- Dyslipidemia in Kidney Disorders: Perspectives on Mitochondria Homeostasis and Therapeutic Opportunities.Frontiers in physiology · 2020Review
- Regulation of Respiration and Apoptosis by Cytochrome c Threonine 58 Phosphorylation.Scientific reports · 2019Article
- Anthocyanins and Their Metabolites as Therapeutic Agents for Neurodegenerative Disease.Antioxidants (Basel, Switzerland) · 2019Review
- Site-Resolved and Quantitative Characterization of Very Weak Protein-Ligand Interactions.ACS chemical biology · 2019Article
- Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.Structure (London, England : 1993) · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The interaction between cytochrome c and the anionic lipid cardiolipin has been proposed as a primary event in the apoptotic signaling cascade. Numerous studies that have examined the interaction of cytochrome c with cardiolipin embedded in a variety of model phospholipid membranes have suggested that partial unfolding of the protein is a precursor to the apoptotic response. However, these studies lacked site resolution and used model systems with negligible or a positive membrane curvature, which is distinct from the large negative curvature of the invaginations of the inner mitochondrial membrane where cytochrome c resides. We have used reverse micelle encapsulation to mimic the potential effects of confinement on the interaction of cytochrome c with cardiolipin. Encapsulation of oxidized horse cytochrome c in 1-decanoyl-rac-glycerol/lauryldimethylamine-N-oxide/hexanol reverse micelles prepared in pentane yields NMR spectra essentially identical to the protein in free aqueous solution. The structure of encapsulated ferricytochrome c was determined to high precision (<r.m.s. deviation>bb ∼ 0.23 Å) using NMR-based methods and is closely similar to the cryogenic crystal structure (<r.m.s. deviation>bb ∼ 1.2 Å). Incorporation of cardiolipin into the reverse micelle surfactant shell causes localized chemical shift perturbations of the encapsulated protein, providing the first view of the cardiolipin/cytochrome c interaction interface at atomic resolution. Three distinct sites of interaction are detected: the so-called A- and L-sites, plus a previously undocumented interaction centered on residues Phe-36, Gly-37, Thr-58, Trp-59, and Lys-60. Importantly, in distinct contrast to earlier studies of this interaction, the protein is not significantly disturbed by the binding of cardiolipin in the context of the reverse micelle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.