ArticleJournal of the American Chemical Society2012
His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Enhancing Enzyme Activity Via Noncovalent Association with DNA-Functionalized Nanoparticles.JACS Au · 2026Article
- Deep UV Resonance Raman Spectroscopy: Applications to Membrane Proteins and Peptides.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Surface-Engineered Nanoparticles Enhance the Peroxidase Activity of Heme-Containing Proteins.ACS nano · 2025Article
- A Novel Heterozygous Pathogenic Variation inFrontiers in genetics · 2021Article
- 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
- Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.Biophysical reviews · 2018Review
- Ligation and Reactivity of Methionine-Oxidized Cytochrome c.Inorganic chemistry · 2018Article
- Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation.Scientific reports · 2016Article
- A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.Journal of the American Chemical Society · 2015Article
- Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Structural transformations of cytochrome c upon interaction with cardiolipin.Chemistry and physics of lipids · 2014Review
- Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c.The journal of physical chemistry. B · 2013Article
- Multifaceted effects of ATP on cardiolipin-bound cytochrome c.Biochemistry · 2013Article
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3 authors.
Funding
Abstract
Cytochrome c unfolds locally and reversibly upon heating at pH 3. UV resonance Raman (UVRR) spectra reveal that instead of producing unordered structure, unfolding converts turns and some helical elements to β-sheet. It also disrupts the Met80-heme bond, and has been previously shown to induce peroxidase activity. Aromatic residues that are H-bonded to a heme propionate (Trp59 and Tyr48) alter their orientation, indicating heme displacement. T-jump/UVRR measurements give time constants of 0.2, 3.9, and 67 μs for successive phases of β-sheet formation and concomitant reorientation of Trp59. UVRR spectra reveal protonation of histidines, and specifically of His26, whose H-bond to Pro44 anchors the 40s Ω loop; this loop is known to be the least stable 'foldon' in the protein. His26 protonation is proposed to disrupt its H-bond with Pro44, triggering the extension of a short β-sheet segment at the 'neck' of the 40s Ω loop into the loop itself and back into the 60s and 70s helices. The secondary structure change displaces the heme via H-bonds from residues in the growing β-sheet, thereby exposing it to exogenous ligands, and inducing peroxidase activity. This unfolding mechanism may play a role in cardiolipin peroxidation by cyt c during apoptosis.
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