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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 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0005-2728 0006-3002 1879-2650 |
DOI: | 10.1016/j.bbabio.2014.03.003 |