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Journal article
Relating the multi-functionality of cytochrome c to membrane binding and structural conversion
Biophysical reviews, v 10(4), pp 1151-1185
Aug 2018
PMID: 29574621
Abstract
Cytochrome c is known as an electron-carrying protein in the respiratory chain of mitochondria. Over the last 20 years, however, alternative functions of this very versatile protein have become the focus of research interests. Upon binding to anionic lipids such as cardiolipin, the protein acquires peroxidase activity. Multiple lines of evidence suggest that this requires a conformational change of the protein which involves partial unfolding of its tertiary structure. This review summarizes the current state of knowledge of how cytochrome c interacts with cardiolipin-containing surfaces and how this affects its structure and function. In this context, we delineate partially conflicting results regarding the affinity of cytochrome c binding to cardiolipin-containing liposomes of different size and its influence on the structure of the protein and the morphology of the membrane.
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Details
- Title
- Relating the multi-functionality of cytochrome c to membrane binding and structural conversion
- Creators
- Reinhard Schweitzer-Stenner - Drexel University
- Publication Details
- Biophysical reviews, v 10(4), pp 1151-1185
- Publisher
- Springer Nature
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Scopus ID
- 2-s2.0-85051170601
- Other Identifier
- 991019173852504721