ArticleProceedings of the National Academy of Sciences of the United States of America2010
Cytochrome c polymerization by successive domain swapping at the C-terminal helix.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.
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Who cites it
64 citing papers in PubMed, 1 synthesis or guideline pooled it, 169 citations in OpenAlex.
- The past, present, and future of artificial zinc finger proteins: design strategies and chemical and biological applications.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Pooled it
- Dimerization-induced conformational transitions of yeast iso-1 cytochromeMagnetic resonance letters · 2026Article
- Understanding domain swapping in the c-Src SH3 domain through hinge-loop mutagenesis.Acta crystallographica. Section D, Structural biology · 2025Article
- Apoprotein Intermolecular Interactions and Heme Insertion for 3D Domain Swapping in Myoglobin.ACS omega · 2025Article
- A High-Resolution Crystallographic Study of Cytochrome c6: Structural Basis for Electron Transfer in Cyanobacterial Photosynthesis.International journal of molecular sciences · 2025Article
- Domain swapping: a mathematical model for quantitative assessment of structural effects.FEBS open bio · 2024Article
- Conjugation with the Carrier Helped to Reveal acidification-Induced Structural Shift in the Peptide from Phospholipase Domain of Parvovirus B19.The protein journal · 2024Article
- Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study.Protein and peptide letters · 2024Article
- Peptide Models of the Cytoplasmic Tail of Influenza A/H1N1 Virus Hemagglutinin Expand Understanding its pH-Dependent Modes of Interaction with Matrix Protein M1.The protein journal · 2023Article
- Direct tests of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Resonance Raman Studies on Heme Ligand Stretching Modes in Methionine80-Depleted CytochromeThe journal of physical chemistry. B · 2023Article
- Direct Tests of Cytochrome Function in the Electron Transport Chain of Malaria Parasites.bioRxiv : the preprint server for biology · 2023Article
- 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
- Equilibrium Between Dimeric and Monomeric Forms of Human Epidermal Growth Factor is Shifted Towards Dimers in a Solution.The protein journal · 2022Article
- Open-Bundle Structure as the Unfolding Intermediate of CytochromeBiomolecules · 2022Article
- NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin.Life (Basel, Switzerland) · 2021Article
- Hydroxyl radical mediated damage of proteins in low oxygen solution investigated using X-ray footprinting mass spectrometry.Journal of synchrotron radiation · 2021Article
- Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins.ACS nano · 2021Article
- Divergent CytochromemBio · 2021Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs at the early stage of apoptosis. For nearly half a century, it has been known that cyt c forms polymers, but the polymerization mechanism remains unknown. We found that cyt c forms polymers by successive domain swapping, where the C-terminal helix is displaced from its original position in the monomer and Met-heme coordination is perturbed significantly. In the crystal structures of dimeric and trimeric cyt c, the C-terminal helices are replaced by the corresponding domain of other cyt c molecules and Met80 is dissociated from the heme. The solution structures of dimeric, trimeric, and tetrameric cyt c were linear based on small-angle X-ray scattering measurements, where the trimeric linear structure shifted toward the cyclic structure by addition of PEG and (NH(4))(2)HPO(4). The absorption and CD spectra of high-order oligomers (approximately 40 mer) were similar to those of dimeric and trimeric cyt c but different from those of monomeric cyt c. For dimeric, trimeric, and tetrameric cyt c, the DeltaH of the oligomer dissociation to monomers was estimated to be about -20 kcal/mol per protomer unit, where Met-heme coordination appears to contribute largely to DeltaH. The present results suggest that cyt c polymerization occurs by successive domain swapping, which may be a common mechanism of protein polymerization.
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