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Resonance Raman spectroscopy of Fe–S proteins and their redox properties
Resonance Raman spectra of Fe–S proteins are sensitive to the cluster type, structure and symmetry. Furthermore, bands that originate from bridging and terminal Fe–S vibrations in the 2Fe–2S, 3Fe–4S and 4Fe–4S clusters can be sensitively distinguished in the spectra, as well as the type of non-cyste...
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/PMC6006211/ https://www.ncbi.nlm.nih.gov/pubmed/29368020 http://dx.doi.org/10.1007/s00775-018-1533-0 |
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author | Todorovic, Smilja Teixeira, Miguel |
author_facet | Todorovic, Smilja Teixeira, Miguel |
author_sort | Todorovic, Smilja |
collection | PubMed |
description | Resonance Raman spectra of Fe–S proteins are sensitive to the cluster type, structure and symmetry. Furthermore, bands that originate from bridging and terminal Fe–S vibrations in the 2Fe–2S, 3Fe–4S and 4Fe–4S clusters can be sensitively distinguished in the spectra, as well as the type of non-cysteinyl coordinating ligands, if present. For these reasons, resonance Raman spectroscopy has been playing an exceptionally active role in the studies of Fe–S proteins of diverse structures and functions. We provide here a concise overview of the structural information that can be obtained from resonance Raman spectroscopy on Fe–S clusters, and in parallel, refer to their thermodynamic properties (e.g., reduction potential), which together define the physiological roles of Fe–S proteins. We demonstrate how the knowledge gained over the past several decades on simple clusters nowadays enables studies of complex structures that include Fe–S clusters coupled to other centers and transient processes that involve cluster inter-conversion, biogenesis, disassembly and catalysis. |
format | Online Article Text |
id | pubmed-6006211 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-60062112018-07-04 Resonance Raman spectroscopy of Fe–S proteins and their redox properties Todorovic, Smilja Teixeira, Miguel J Biol Inorg Chem Minireview Resonance Raman spectra of Fe–S proteins are sensitive to the cluster type, structure and symmetry. Furthermore, bands that originate from bridging and terminal Fe–S vibrations in the 2Fe–2S, 3Fe–4S and 4Fe–4S clusters can be sensitively distinguished in the spectra, as well as the type of non-cysteinyl coordinating ligands, if present. For these reasons, resonance Raman spectroscopy has been playing an exceptionally active role in the studies of Fe–S proteins of diverse structures and functions. We provide here a concise overview of the structural information that can be obtained from resonance Raman spectroscopy on Fe–S clusters, and in parallel, refer to their thermodynamic properties (e.g., reduction potential), which together define the physiological roles of Fe–S proteins. We demonstrate how the knowledge gained over the past several decades on simple clusters nowadays enables studies of complex structures that include Fe–S clusters coupled to other centers and transient processes that involve cluster inter-conversion, biogenesis, disassembly and catalysis. Springer Berlin Heidelberg 2018-01-24 2018 /pmc/articles/PMC6006211/ /pubmed/29368020 http://dx.doi.org/10.1007/s00775-018-1533-0 Text en © The Author(s) 2018, corrected publication June/2018 Open Access This 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 Todorovic, Smilja Teixeira, Miguel Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title | Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title_full | Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title_fullStr | Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title_full_unstemmed | Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title_short | Resonance Raman spectroscopy of Fe–S proteins and their redox properties |
title_sort | resonance raman spectroscopy of fe–s proteins and their redox properties |
topic | Minireview |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6006211/ https://www.ncbi.nlm.nih.gov/pubmed/29368020 http://dx.doi.org/10.1007/s00775-018-1533-0 |
work_keys_str_mv | AT todorovicsmilja resonanceramanspectroscopyoffesproteinsandtheirredoxproperties AT teixeiramiguel resonanceramanspectroscopyoffesproteinsandtheirredoxproperties |