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Biophysical Reviews

, Volume 10, Issue 4, pp 1151–1185 | Cite as

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

  • Reinhard Schweitzer-Stenner
Review

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.

Keywords

Cytochrome c Cardiolipin Peroxidase activity Protein-membrane interactions 

Notes

Acknowledgements

The work from our research group reported in this paper was the product of hard work by my former graduate student, Dr. Leah Pandiscia, my current graduate student Bridget Milorey, and by two undergraduate researchers, Dmitry Malyshka and Lee Serpas.

Compliance with ethical standards

Conflict of interest

Reinhard Schweitzer-Stenner declares that he has no conflict of interests with regards to this article.

Ethical approval

No experiments with humans or animals were performed for this study.

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© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of ChemistryDrexel UniversityPhiladelphiaUSA

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