Relating the multi-functionality of cytochrome c to membrane binding and structural conversion

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...

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Veröffentlicht in:Biophysical reviews 2018-08, Vol.10 (4), p.1151-1185
1. Verfasser: Schweitzer-Stenner, Reinhard
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description 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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subjects Binding
Biochemistry
Biological and Medical Physics
Biological Techniques
Biomedical and Life Sciences
Biophysics
Cardiolipin
Cell Biology
Cytochrome
Cytochrome c
Cytochromes
Electron transport
Life Sciences
Lipid peroxidation
Lipids
Liposomes
Membrane Biology
Mitochondria
Mitochondrial DNA
Morphology
Nanotechnology
Peroxidase
Protein folding
Protein structure
Proteins
Review
Structure-function relationships
Tertiary structure
title Relating the multi-functionality of cytochrome c to membrane binding and structural conversion
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