ArticleJournal of the American Chemical Society2016
Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Order-to-Disorder and Disorder-to-Order Transitions of Proteins upon Binding to Phospholipid Membranes: Common Ground and Dissimilarities.Biomolecules · 2025Review
- Cardiolipin's multifaceted role in immune response: a focus on interacting proteins.Frontiers in immunology · 2025Review
- Direct tests of cytochromeProceedings of the National Academy of Sciences of the United States of America · 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
- Naturally Occurring I81N Mutation in Human CytochromeACS omega · 2022Article
- Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.Nature communications · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- The importance of Asn52 in the structure-function relationship of human cytochromeRSC advances · 2020Article
- The Human CytochromeBiochemistry · 2020Article
- Binding of S. cerevisiae iso-1 cytochrome c and its surface lysine-to-alanine variants to cardiolipin: charge effects and the role of the lipid to protein ratio.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- Naturally Occurring A51V Variant of Human CytochromeThe journal of physical chemistry. B · 2019Article
- Determination of proton concentration at cardiolipin-containing membrane interfaces and its relation with the peroxidase activity of cytochromeChemical science · 2019Article
- MOMP, cell suicide as a BCL-2 family business.Cell death and differentiation · 2018Review
- Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy.Science (New York, N.Y.) · 2017Article
- An approach for the identification of exemplar sites for scaling up targeted field observations of benthic biogeochemistry in heterogeneous environments.Biogeochemistry · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Cytochrome c can acquire peroxidase activity when it binds to cardiolipin in mitochondrial membranes. The resulting oxygenation of cardiolipin by cytochrome c provides an early signal for the onset of apoptosis. The structure of this enzyme-substrate complex is a matter of considerable debate. We present three structures at 1.7-2.0 Å resolution of a domain-swapped dimer of yeast iso-1-cytochrome c with the detergents, CYMAL-5, CYMAL-6, and ω-undecylenyl-β-d-maltopyranoside, bound in a channel that places the hydrocarbon moieties of these detergents next to the heme. The heme is poised for peroxidase activity with water bound in place of Met80, which serves as the axial heme ligand when cytochrome c functions as an electron carrier. The hydroxyl group of Tyr67 sits 3.6-4.0 Å from the nearest carbon of the detergents, positioned to act as a relay in radical abstraction during peroxidase activity. Docking studies with linoleic acid, the most common fatty acid component of cardiolipin, show that C11 of linoleic acid can sit adjacent to Tyr67 and the heme, consistent with the oxygenation pattern observed in lipidomics studies. The well-defined hydrocarbon binding pocket provides atomic resolution evidence for the extended lipid anchorage model for cytochrome c/cardiolipin binding. Dimer dissociation/association kinetics for yeast versus equine cytochrome c indicate that formation of mammalian cytochrome c dimers in vivo would require catalysis. However, the dimer structure shows that only a modest deformation of monomeric cytochrome c would suffice to form the hydrocarbon binding site occupied by these detergents.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.