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Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─)
Iron water-soluble porphyrins have been long used as biomimetic compounds for modelling the active sites found in heme-enzymes. In this regard, the anionic porphyrin [Fe(III)(TPPS)](3─) and its coordination complexes have been repeatedly chosen as suitable water-soluble platforms for bioinorganic ch...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207616/ https://www.ncbi.nlm.nih.gov/pubmed/35734568 http://dx.doi.org/10.1016/j.heliyon.2022.e09555 |
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author | Mazzeo, Agostina Gaviglio, Carina Pellegrino, Juan Doctorovich, Fabio |
author_facet | Mazzeo, Agostina Gaviglio, Carina Pellegrino, Juan Doctorovich, Fabio |
author_sort | Mazzeo, Agostina |
collection | PubMed |
description | Iron water-soluble porphyrins have been long used as biomimetic compounds for modelling the active sites found in heme-enzymes. In this regard, the anionic porphyrin [Fe(III)(TPPS)](3─) and its coordination complexes have been repeatedly chosen as suitable water-soluble platforms for bioinorganic chemistry studies. In this work we report for the first time the crystal structure of the water-soluble nitrosyl complex [Fe(II)(TPPS) (NO(•))](4─) along with that of oxodimeric ferric species [μ-O-([Fe(III)(TPPS)])(2)](8─). |
format | Online Article Text |
id | pubmed-9207616 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-92076162022-06-21 Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) Mazzeo, Agostina Gaviglio, Carina Pellegrino, Juan Doctorovich, Fabio Heliyon Research Article Iron water-soluble porphyrins have been long used as biomimetic compounds for modelling the active sites found in heme-enzymes. In this regard, the anionic porphyrin [Fe(III)(TPPS)](3─) and its coordination complexes have been repeatedly chosen as suitable water-soluble platforms for bioinorganic chemistry studies. In this work we report for the first time the crystal structure of the water-soluble nitrosyl complex [Fe(II)(TPPS) (NO(•))](4─) along with that of oxodimeric ferric species [μ-O-([Fe(III)(TPPS)])(2)](8─). Elsevier 2022-06-09 /pmc/articles/PMC9207616/ /pubmed/35734568 http://dx.doi.org/10.1016/j.heliyon.2022.e09555 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Mazzeo, Agostina Gaviglio, Carina Pellegrino, Juan Doctorovich, Fabio Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title | Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title_full | Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title_fullStr | Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title_full_unstemmed | Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title_short | Structural characterization of the water-soluble porphyrin complexes [Fe(II)(TPPS) (NO(•))](4─) and [μ-O-([Fe(III)(TPPS)])(2)](8─) |
title_sort | structural characterization of the water-soluble porphyrin complexes [fe(ii)(tpps) (no(•))](4─) and [μ-o-([fe(iii)(tpps)])(2)](8─) |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207616/ https://www.ncbi.nlm.nih.gov/pubmed/35734568 http://dx.doi.org/10.1016/j.heliyon.2022.e09555 |
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