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The NMR contribution to protein–protein networking in Fe–S protein maturation
Iron–sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6006191/ https://www.ncbi.nlm.nih.gov/pubmed/29569085 http://dx.doi.org/10.1007/s00775-018-1552-x |
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author | Banci, Lucia Camponeschi, Francesca Ciofi-Baffoni, Simone Piccioli, Mario |
author_facet | Banci, Lucia Camponeschi, Francesca Ciofi-Baffoni, Simone Piccioli, Mario |
author_sort | Banci, Lucia |
collection | PubMed |
description | Iron–sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe–S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe–2S], [3Fe–4S] and [4Fe–4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe–S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe–S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of “Fe–S interactomics”. This contribution was particularly effective when protein–protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies. |
format | Online Article Text |
id | pubmed-6006191 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-60061912018-07-04 The NMR contribution to protein–protein networking in Fe–S protein maturation Banci, Lucia Camponeschi, Francesca Ciofi-Baffoni, Simone Piccioli, Mario J Biol Inorg Chem Minireview Iron–sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe–S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe–2S], [3Fe–4S] and [4Fe–4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe–S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe–S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of “Fe–S interactomics”. This contribution was particularly effective when protein–protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies. Springer Berlin Heidelberg 2018-03-22 2018 /pmc/articles/PMC6006191/ /pubmed/29569085 http://dx.doi.org/10.1007/s00775-018-1552-x Text en © The Author(s) 2018, corrected publication May/2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, duplication, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made. |
spellingShingle | Minireview Banci, Lucia Camponeschi, Francesca Ciofi-Baffoni, Simone Piccioli, Mario The NMR contribution to protein–protein networking in Fe–S protein maturation |
title | The NMR contribution to protein–protein networking in Fe–S protein maturation |
title_full | The NMR contribution to protein–protein networking in Fe–S protein maturation |
title_fullStr | The NMR contribution to protein–protein networking in Fe–S protein maturation |
title_full_unstemmed | The NMR contribution to protein–protein networking in Fe–S protein maturation |
title_short | The NMR contribution to protein–protein networking in Fe–S protein maturation |
title_sort | nmr contribution to protein–protein networking in fe–s protein maturation |
topic | Minireview |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6006191/ https://www.ncbi.nlm.nih.gov/pubmed/29569085 http://dx.doi.org/10.1007/s00775-018-1552-x |
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