ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 74 citations in OpenAlex.
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Tyrosine 67 Phosphorylation Controls Respiration and Limits the Apoptotic Functions of CytochromeCells · 2025Article
- Cardiac Tyrosine 97 Phosphorylation of CytochromeInternational journal of molecular sciences · 2025Article
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- Phosphorylation of cytochrome c at tyrosine 48 finely regulates its binding to the histone chaperone SET/TAF-Iβ in the nucleus.Protein science : a publication of the Protein Society · 2024Article
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Phosphorylations and Acetylations of CytochromeCells · 2024Review
- Artesunate acts through cytochrome c to inhibit growth of pediatric AML cells.Scientific reports · 2023Article
- Combined analytical approach empowers precise spectroscopic interpretation of subcellular components of pancreatic cancer cells.Analytical and bioanalytical chemistry · 2023Article
- Phosphorylation disrupts long-distance electron transport in cytochrome c.Nature communications · 2022Article
- Double face of cytochrome c in cancers by Raman imaging.Scientific reports · 2022Article
- Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants.FEBS open bio · 2021Article
- Metabolomic Identification of Anticancer Metabolites of Australian Propolis and Proteomic Elucidation of Its Synergistic Mechanisms with Doxorubicin in the MCF7 Cells.International journal of molecular sciences · 2021Article
- Lysine 53 Acetylation of CytochromeCells · 2021Article
- In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes.ACS omega · 2021Review
- Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.Life (Basel, Switzerland) · 2021Review
- Post-Translational Modifications of CytochromeInternational journal of molecular sciences · 2020Review
- 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
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome c (Cc) is a key protein in cell life (respiration) and cell death (apoptosis). On the one hand, it serves as a mitochondrial redox carrier, transferring electrons between the membrane-embedded complexes III and IV. On the other hand, it acts as a cytoplasmic apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The two functions of cytochrome c are finely tuned by the phosphorylation of tyrosines and, in particular, those located at positions 48 and 97. However, the specific cytochrome c-phosphorylating kinase is still unknown. To study the structural and functional changes induced by tyrosine phosphorylation in cytochrome c, we studied the two phosphomimetic mutants Y48E and Y97E, in which each tyrosine residue is replaced by glutamate. Such substitutions alter both the physicochemical features and the function of each mutant compared with the native protein. Y97E is significantly less stable than the WT species, whereas Y48E not only exhibits lower values for the alkaline transition pK (a) and the midpoint redox potential, but it also impairs Apaf-1-mediated caspase activation. Altogether, these findings suggest that the specific phosphorylation of Tyr48 makes cytochrome c act as an anti-apoptotic switch.
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