ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013
Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 42 citations in OpenAlex.
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- 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
- Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids.Journal of molecular biology · 2021Article
- The importance of Asn52 in the structure-function relationship of human cytochromeRSC advances · 2020Article
- The Human CytochromeBiochemistry · 2020Article
- Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.International journal of molecular sciences · 2020Article
- Naturally Occurring A51V Variant of Human CytochromeThe journal of physical chemistry. B · 2019Article
- A Heme Propionate Staples the Structure of CytochromeInorganic chemistry · 2019Article
- Ligation and Reactivity of Methionine-Oxidized Cytochrome c.Inorganic chemistry · 2018Article
- Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.Biochemistry · 2018Article
- Effect of a K72A Mutation on the Structure, Stability, Dynamics, and Peroxidase Activity of Human Cytochrome c.Biochemistry · 2017Article
- Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.Biochemistry · 2017Article
- Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation.Scientific reports · 2016Article
- Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability.Journal of inorganic biochemistry · 2016Article
- Disruption of cytochrome c heme coordination is responsible for mitochondrial injury during ischemia.Biochimica et biophysica acta · 2015Article
- Article
- Discovering co-occurring patterns and their biological significance in protein families.BMC bioinformatics · 2014Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Cytochrome c is a highly conserved protein, with 20 residues identical in all eukaryotic cytochromes c. Gly-41 is one of these invariant residues, and is the position of the only reported naturally occurring mutation in cytochrome c (human G41S). The basis, if any, for the conservation of Gly-41 is unknown. The mutation of Gly-41 to Ser enhances the apoptotic activity of cytochrome c without altering its role in mitochondrial electron transport. Here we have studied additional residue 41 variants and determined their effects on cytochrome c functions and conformation. A G41T mutation decreased the ability of cytochrome c to induce caspase activation and decreased the redox potential, whereas a G41A mutation had no impact on caspase induction but the redox potential increased. All residue 41 variants decreased the pK (a) of a structural transition of oxidized cytochrome c to the alkaline conformation, and this correlated with a destabilization of the interaction of Met-80 with the heme iron(III) at physiological pH. In reduced cytochrome c the G41T and G41S mutations had distinct effects on a network of hydrogen bonds involving Met-80, and in G41T the conformational mobility of two Ω-loops was altered. These results suggest the impact of residue 41 on the conformation of cytochrome c influences its ability to act in both of its physiological roles, electron transport and caspase activation.
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