ArticleScientific reports2016
Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 61 citations in OpenAlex.
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- A novel thrombocytopenia-4-causing CYCS gene variant decreases caspase activity: Three-generation study.British journal of haematology · 2024Article
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Altered conformational dynamics contribute to species-specific effects of cytochrome c mutations on caspase activation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.Biosensors · 2023Article
- Article
- Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022Article
- Effect on intrinsic peroxidase activity of substituting coevolved residues from Ω-loop C of human cytochrome c into yeast iso-1-cytochrome c.Journal of inorganic biochemistry · 2022Article
- Naturally Occurring I81N Mutation in Human CytochromeACS omega · 2022Article
- On the origin of chaotrope-modulated electrocatalytic activity of cytochromeChemical communications (Cambridge, England) · 2022Article
- How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.Molecules (Basel, Switzerland) · 2021Review
- Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids.Journal of molecular biology · 2021Article
- In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes.ACS omega · 2021Review
- A Novel Heterozygous Pathogenic Variation inFrontiers in genetics · 2021Article
- The importance of Asn52 in the structure-function relationship of human cytochromeRSC advances · 2020Article
- Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.International journal of molecular sciences · 2020Article
- Insights on the Conformational Ensemble of Cyt C Reveal a Compact State during Peroxidase Activity.Biophysical journal · 2020Article
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- Serine-47 phosphorylation of cytochromeFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Naturally Occurring A51V Variant of Human CytochromeThe journal of physical chemistry. B · 2019Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thrombocytopenia 4 is an inherited autosomal dominant thrombocytopenia, which occurs due to mutations in the human gene for cytochrome c that results in enhanced mitochondrial apoptotic activity. The Gly41Ser mutation was the first to be reported. Here we report stopped-flow kinetic studies of azide binding to human ferricytochrome c and its Gly41Ser variant, together with backbone amide H/D exchange and (15)N-relaxation dynamics using NMR spectroscopy, to show that alternative conformations are kinetically and thermodynamically more readily accessible for the Gly41Ser variant than for the wild-type protein. Our work reveals a direct conformational link between the 40-57 Ω-loop in which residue 41 resides and the dynamical properties of the axial ligand to the heme iron, Met80, such that the replacement of glycine by serine promotes the dissociation of the Met80 ligand, thereby increasing the population of a peroxidase active state, which is a key non-native conformational state in apoptosis.
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