ArticleProtein science : a publication of the Protein Society2005
ATP specifically drives refolding of non-native conformations of cytochrome c.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 47 citations in OpenAlex.
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Suitability of Adenosine Derivatives in Improving the Activity and Stability of Cytochrome c under Stress: Insights into the Effect of Phosphate Groups.The journal of physical chemistry. B · 2024Article
- Correlative Raman-Electron-Light (CREL) Microscopy Analysis of Lipid Droplets in Melanoma Cancer Stem Cells.Biosensors · 2022Article
- Two sides of the same coin? Unraveling subtle differences between human embryonic and induced pluripotent stem cells by Raman spectroscopy.Stem cell research & therapy · 2017Article
- The key role played by charge in the interaction of cytochrome c with cardiolipin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Multifaceted effects of ATP on cardiolipin-bound cytochrome c.Biochemistry · 2013Article
- The non-native conformations of cytochrome c in sodium dodecyl sulfate and their modulation by ATP.European biophysics journal : EBJ · 2011Article
- Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Mitochondrial targeting of electron scavenging antioxidants: Regulation of selective oxidation vs random chain reactions.Advanced drug delivery reviews · 2009Review
- Cytochrome c impaled: investigation of the extended lipid anchorage of a soluble protein to mitochondrial membrane models.The Biochemical journal · 2007Article
- A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis.Journal of the American Chemical Society · 2007Article
- Peroxidase activity and structural transitions of cytochrome c bound to cardiolipin-containing membranes.Biochemistry · 2006Article
- Insights into the role of the histidines in the structure and stability of cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2006Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An increasing body of evidence ascribes to misfolded forms of cytochrome c (cyt c) a role in pathophysiological events such as apoptosis and disease. Here, we examine the conformational changes induced by lipid binding to horse heart cyt c at pH 7 and study the ability of ATP (and other nucleotides) to refold several forms of unfolded cyt c such as oleic acid-bound cyt c, nicked cyt c, and acid denatured cyt c. The CD and fluorescence spectra demonstrate that cyt c unfolded by oleic acid has an intact secondary structure, and a disrupted tertiary structure and heme environment. Furthermore, evidence from the Soret CD, electronic absorption, and resonance Raman spectra indicates the presence of an equilibrium of at least two low-spin species having distinct heme-iron(III) coordination. As a whole, the data indicate that binding of cyt c to oleic acid leads to a partially unfolded conformation of the protein, resembling that typical of the molten globule state. Interestingly, the native conformation is almost fully recovered in the presence of ATP or dATP, while other nucleotides, such as GTP, are ineffective. Molecular modeling of ATP binding to cyt c and mutagenesis experiments show the interactions of phosphate groups with Lys88 and Arg91, with adenosine ring interaction with Glu62 explaining the unfavorable binding of GTP. The finding that ATP and dATP are unique among the nucleotides in being able to turn non-native states of cyt c back to native conformation is discussed in the light of cyt c involvement in cell apoptosis.
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