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NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin.
- Source :
-
Life (2075-1729) . Oct2021, Vol. 11 Issue 10, p1031-1031. 1p. - Publication Year :
- 2021
-
Abstract
- Conformational change of cytochrome c (cyt c) caused by interaction with cardiolipin (CL) is an important step during apoptosis, but the underlying mechanism is controversial. To comprehensively clarify the structural transformations of cyt c upon interaction with CL and avoid the unpredictable alias that might come from protein labeling or mutations, the conformation of purified yeast iso–1 cyt c with natural isotopic abundance in different contents of CL was measured by using NMR spectroscopy, in which the trimethylated group of the protein was used as a natural probe. The data demonstrate that cyt c has two partially unfolded conformations when interacted with CL: one with Fe–His33 coordination and the other with a penta–coordination heme. The Fe–His33 coordination conformation can be converted into a penta–coordination heme conformation in high content of CL. The structure of cyt c becomes partially unfolded with more exposed heme upon interaction with CL, suggesting that cyt c prefers a high peroxidase activity state in the mitochondria, which, in turn, makes CL easy to be oxidized, and causes the release of cyt c into the cytoplasm as a trigger in apoptosis. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20751729
- Volume :
- 11
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- Life (2075-1729)
- Publication Type :
- Academic Journal
- Accession number :
- 153348037
- Full Text :
- https://doi.org/10.3390/life11101031