Relating the Multi-functionality of Cytochrome C to Membrane Binding and Structural Conversion

Overview

Journal Biophys Rev

Publisher Springer

Specialty Biophysics

Date 2018 Mar 26

PMID 29574621

Citations 17

Authors

Reinhard Schweitzer-Stenner

Affiliations

Soon will be listed here.

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.

Citing Articles

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The Increase in the Peroxidase Activity of the Cytochrome with Substitutions in the Universal Binding Site Is Associated with Changes in the Ability to Interact with External Ligands.

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