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Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Cytochromes c are ubiquitous heme proteins that are found in most living organisms and are essential for various energy production pathways as well as other cellular processes. Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the form...

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Published in:Biochimica et biophysica acta 2014-07, Vol.1837 (7), p.989-998
Main Authors: Verissimo, Andreia F., Daldal, Fevzi
Format: Article
Language:English
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Summary:Cytochromes c are ubiquitous heme proteins that are found in most living organisms and are essential for various energy production pathways as well as other cellular processes. Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the formation of stereo-specific thioether bonds between the vinyl groups of heme b (protoporphyrin IX-Fe) and the thiol groups of apocytochromes c heme-binding site (C1XXC2H) cysteine residues. In some organisms this process involves up to nine (CcmABCDEFGHI) membrane proteins working together to achieve heme ligation, designated the Cytochrome c maturation (Ccm)-System I. Here, we review recent findings related to the Ccm-System I found in bacteria, archaea and plant mitochondria, with an emphasis on protein interactions between the Ccm components and their substrates (apocytochrome c and heme). We discuss the possibility that the Ccm proteins may form a multi subunit supercomplex (dubbed “Ccm machine”), and based on the currently available data, we present an updated version of a mechanistic model for Ccm. This article is part of a Special Issue entitled: 18th European Bioenergetic Conference. •Cytochrome c biogenesis is the covalent ligation of heme b to an apocyt c.•Ccm is an intricate post-translational protein modification process.•Ccm-System I involves nine membrane-bound proteins working together.•The Ccm proteins are proposed to form a large multi subunit supercomplex.•A mechanistic view of stereo-specific thioether bond formation is presented.
ISSN:0005-2728
0006-3002
1879-2650
DOI:10.1016/j.bbabio.2014.03.003