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Cytochrome c biogenesis System I

Cytochromes c are widespread respiratory proteins characterized by the covalent attachment of heme. The formation of c-type cytochromes requires, in all but a few exceptional cases, the formation of two thioether bonds between the two cysteine sulfurs in a –CXXCH– motif in the protein and the vinyl...

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Autores principales: Stevens, Julie M, Mavridou, Despoina A I, Hamer, Rebecca, Kritsiligkou, Paraskevi, Goddard, Alan D, Ferguson, Stuart J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601427/
https://www.ncbi.nlm.nih.gov/pubmed/21958041
http://dx.doi.org/10.1111/j.1742-4658.2011.08376.x
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author Stevens, Julie M
Mavridou, Despoina A I
Hamer, Rebecca
Kritsiligkou, Paraskevi
Goddard, Alan D
Ferguson, Stuart J
author_facet Stevens, Julie M
Mavridou, Despoina A I
Hamer, Rebecca
Kritsiligkou, Paraskevi
Goddard, Alan D
Ferguson, Stuart J
author_sort Stevens, Julie M
collection PubMed
description Cytochromes c are widespread respiratory proteins characterized by the covalent attachment of heme. The formation of c-type cytochromes requires, in all but a few exceptional cases, the formation of two thioether bonds between the two cysteine sulfurs in a –CXXCH– motif in the protein and the vinyl groups of heme. The vinyl groups of the heme are not particularly activated and therefore the addition reaction does not physiologically occur spontaneously in cells. There are several diverse post-translational modification systems for forming these bonds. Here, we describe the complex multiprotein cytochrome c maturation (Ccm) system (in Escherichia coli comprising the proteins CcmABCDEFGH), also called System I, that performs the heme attachment. System I is found in plant mitochondria, archaea and many Gram-negative bacteria; the systems found in other organisms and organelles are described elsewhere in this minireview series.
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spelling pubmed-36014272013-03-20 Cytochrome c biogenesis System I Stevens, Julie M Mavridou, Despoina A I Hamer, Rebecca Kritsiligkou, Paraskevi Goddard, Alan D Ferguson, Stuart J FEBS J Minireview Cytochromes c are widespread respiratory proteins characterized by the covalent attachment of heme. The formation of c-type cytochromes requires, in all but a few exceptional cases, the formation of two thioether bonds between the two cysteine sulfurs in a –CXXCH– motif in the protein and the vinyl groups of heme. The vinyl groups of the heme are not particularly activated and therefore the addition reaction does not physiologically occur spontaneously in cells. There are several diverse post-translational modification systems for forming these bonds. Here, we describe the complex multiprotein cytochrome c maturation (Ccm) system (in Escherichia coli comprising the proteins CcmABCDEFGH), also called System I, that performs the heme attachment. System I is found in plant mitochondria, archaea and many Gram-negative bacteria; the systems found in other organisms and organelles are described elsewhere in this minireview series. Blackwell Publishing Ltd 2011-11 /pmc/articles/PMC3601427/ /pubmed/21958041 http://dx.doi.org/10.1111/j.1742-4658.2011.08376.x Text en © 2011 The Authors Journal compilation © 2011 FEBS http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Minireview
Stevens, Julie M
Mavridou, Despoina A I
Hamer, Rebecca
Kritsiligkou, Paraskevi
Goddard, Alan D
Ferguson, Stuart J
Cytochrome c biogenesis System I
title Cytochrome c biogenesis System I
title_full Cytochrome c biogenesis System I
title_fullStr Cytochrome c biogenesis System I
title_full_unstemmed Cytochrome c biogenesis System I
title_short Cytochrome c biogenesis System I
title_sort cytochrome c biogenesis system i
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601427/
https://www.ncbi.nlm.nih.gov/pubmed/21958041
http://dx.doi.org/10.1111/j.1742-4658.2011.08376.x
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