ArticleJournal of the American Chemical Society2015
A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 63 citations in OpenAlex.
- A Divergent Mitochondrial Cytochrome c in Malaria Parasites With an Anomalously Low Redox Potential.Journal of molecular biology · 2026Article
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- Oleoyl coenzyme A triggers peroxygenase activity in cytochrome c.Journal of inorganic biochemistry · 2026Article
- Methionine coordination to the heme iron and its displacement by nitric oxide in the CcoP subunit of Pseudomonas aeruginosa cytochrome cbbJournal of inorganic biochemistry · 2026Article
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.Biosensors · 2023Article
- Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins.Inorganic chemistry · 2022Article
- Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022Article
- Carbon Monoxide Signaling: Examining Its Engagement with Various Molecular Targets in the Context of Binding Affinity, Concentration, and Biologic Response.Pharmacological reviews · 2022Review
- A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain.Journal of biomolecular structure & dynamics · 2022Article
- 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
- Structure and redox properties of the diheme electron carrier cytochrome cJournal of inorganic biochemistry · 2020Article
- Insights on the Conformational Ensemble of Cyt C Reveal a Compact State during Peroxidase Activity.Biophysical journal · 2020Article
- Discovery of a functional, contracted heme-binding motif within a multiheme cytochrome.The Journal of biological chemistry · 2019Article
- A Heme Propionate Staples the Structure of CytochromeInorganic chemistry · 2019Article
- Nanosecond photochemically promoted click chemistry for enhanced neuropeptide visualization and rapid protein labeling.Nature communications · 2019Article
- Lysine carbonylation is a previously unrecognized contributor to peroxidase activation of cytochromeChemical science · 2019Article
- The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.Biochemistry · 2018Article
- Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.Biophysical reviews · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
It has been suggested that the alkaline form of cytochrome c (cyt c) regulates function of this protein as an electron carrier in oxidative phosphorylation and as a peroxidase that reacts with cardiolipin (CL) during apoptosis. In this form, Met80, the native ligand to the heme iron, is replaced by a Lys. While it has become clear that the structure of cyt c changes, the extent and sequence of conformational rearrangements associated with this ligand replacement remain a subject of debate. Herein we report a high-resolution crystal structure of a Lys73-ligated cyt c conformation that reveals intricate change in the heme environment upon this switch in the heme iron ligation. The structure is surprisingly compact, and the heme coordination loop refolds into a β-hairpin with a turn formed by the highly conserved residues Pro76 and Gly77. Repositioning of residue 78 modifies the intraprotein hydrogen-bonding network and, together with adjustments of residues 52 and 74, increases the volume of the heme pocket to allow for insertion of one of the CL acyl moieties next to Asn52. Derivatization of Cys78 with maleimide creates a solution mimic of the Lys-ligated cyt c that has enhanced peroxidase activity, adding support for a role of the Lys-ligated cyt c in the apoptotic mechanism. Experiments with the heme peptide microperoxidase-8 and engineered model proteins provide a thermodynamic rationale for the switch to Lys ligation upon perturbations in the protein scaffold.
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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.