On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes

The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cl...

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Autores principales: Mulliez, Etienne, Duarte, Victor, Arragain, Simon, Fontecave, Marc, Atta, Mohamed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5352715/
https://www.ncbi.nlm.nih.gov/pubmed/28361051
http://dx.doi.org/10.3389/fchem.2017.00017
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author Mulliez, Etienne
Duarte, Victor
Arragain, Simon
Fontecave, Marc
Atta, Mohamed
author_facet Mulliez, Etienne
Duarte, Victor
Arragain, Simon
Fontecave, Marc
Atta, Mohamed
author_sort Mulliez, Etienne
collection PubMed
description The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site. This review article summarizes recent important achievements obtained on these five enzymes with the main focus to delineate the role of this additional [4Fe-4S] cluster in catalysis.
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spelling pubmed-53527152017-03-30 On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes Mulliez, Etienne Duarte, Victor Arragain, Simon Fontecave, Marc Atta, Mohamed Front Chem Chemistry The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site. This review article summarizes recent important achievements obtained on these five enzymes with the main focus to delineate the role of this additional [4Fe-4S] cluster in catalysis. Frontiers Media S.A. 2017-03-16 /pmc/articles/PMC5352715/ /pubmed/28361051 http://dx.doi.org/10.3389/fchem.2017.00017 Text en Copyright © 2017 Mulliez, Duarte, Arragain, Fontecave and Atta. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Chemistry
Mulliez, Etienne
Duarte, Victor
Arragain, Simon
Fontecave, Marc
Atta, Mohamed
On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title_full On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title_fullStr On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title_full_unstemmed On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title_short On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes
title_sort on the role of additional [4fe-4s] clusters with a free coordination site in radical-sam enzymes
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5352715/
https://www.ncbi.nlm.nih.gov/pubmed/28361051
http://dx.doi.org/10.3389/fchem.2017.00017
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