ArticleFEBS open bio2021
Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants.
Article in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Tyrosine 67 Phosphorylation Controls Respiration and Limits the Apoptotic Functions of CytochromeCells · 2025Article
- Regulation of mNature plants · 2025Article
- Lysine acetylation of aquaporin-3 promotes water permeability but is not essential for urine concentrating ability.American journal of physiology. Renal physiology · 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
- Rapid reconstitution of ubiquitinated nucleosome using a non-denatured histone octamer ubiquitylation approach.Cell & bioscience · 2024Article
- Prostate Cancer-Specific Lysine 53 Acetylation of CytochromeBiomolecules · 2024Article
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Phosphorylations and Acetylations of CytochromeCells · 2024Review
- Cytochrome c lysine acetylation regulates cellular respiration and cell death in ischemic skeletal muscle.Nature communications · 2023Article
- De novo sequencing and construction of a unique antibody for the recognition of alternative conformations of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Ten years of FEBS Open Bio.FEBS open bio · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications frequently modulate protein functions. Lysine acetylation in particular plays a key role in interactions between respiratory cytochrome c and its metabolic partners. To date, in vivo acetylation of lysines at positions 8 and 53 has specifically been identified in mammalian cytochrome c, but little is known about the structural basis of acetylation-induced functional changes. Here, we independently replaced these two residues in recombinant human cytochrome c with glutamine to mimic lysine acetylation and then characterized the structure and function of the resulting K8Q and K53Q mutants. We found that the physicochemical features were mostly unchanged in the two acetyl-mimetic mutants, but their thermal stability was significantly altered. NMR chemical shift perturbations of the backbone amide resonances revealed local structural changes, and the thermodynamics and kinetics of electron transfer in mutants immobilized on gold electrodes showed an increase in both protein dynamics and solvent involvement in the redox process. We also observed that the K8Q (but not the K53Q) mutation slightly increased the binding affinity of cytochrome c to its physiological electron donor, cytochrome c
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