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Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties
Structural and functional properties of ferrous Mycobacterium tuberculosis (Mt-Nb) and human (Hs-Nb) nitrobindins (Nbs) were investigated. At pH 7.0 and 25.0 °C, the unliganded Fe(II) species is penta-coordinated and unlike most other hemoproteins no pH-dependence of its coordination was detected ov...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915275/ https://www.ncbi.nlm.nih.gov/pubmed/33562340 http://dx.doi.org/10.3390/ijms22041674 |
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author | De Simone, Giovanna di Masi, Alessandra Pesce, Alessandra Bolognesi, Martino Ciaccio, Chiara Tognaccini, Lorenzo Smulevich, Giulietta Abbruzzetti, Stefania Viappiani, Cristiano Bruno, Stefano Monaca, Sara Della Pietraforte, Donatella Fattibene, Paola Coletta, Massimo Ascenzi, Paolo |
author_facet | De Simone, Giovanna di Masi, Alessandra Pesce, Alessandra Bolognesi, Martino Ciaccio, Chiara Tognaccini, Lorenzo Smulevich, Giulietta Abbruzzetti, Stefania Viappiani, Cristiano Bruno, Stefano Monaca, Sara Della Pietraforte, Donatella Fattibene, Paola Coletta, Massimo Ascenzi, Paolo |
author_sort | De Simone, Giovanna |
collection | PubMed |
description | Structural and functional properties of ferrous Mycobacterium tuberculosis (Mt-Nb) and human (Hs-Nb) nitrobindins (Nbs) were investigated. At pH 7.0 and 25.0 °C, the unliganded Fe(II) species is penta-coordinated and unlike most other hemoproteins no pH-dependence of its coordination was detected over the pH range between 2.2 and 7.0. Further, despite a very open distal side of the heme pocket (as also indicated by the vanishingly small geminate recombination of CO for both Nbs), which exposes the heme pocket to the bulk solvent, their reactivity toward ligands, such as CO and NO, is significantly slower than in most hemoproteins, envisaging either a proximal barrier for ligand binding and/or crowding of H(2)O molecules in the distal side of the heme pocket which impairs ligand binding to the heme Fe-atom. On the other hand, liganded species display already at pH 7.0 and 25 °C a severe weakening (in the case of CO) and a cleavage (in the case of NO) of the proximal Fe-His bond, suggesting that the ligand-linked movement of the Fe(II) atom onto the heme plane brings about a marked lengthening of the proximal Fe-imidazole bond, eventually leading to its rupture. This structural evidence is accompanied by a marked enhancement of both ligands dissociation rate constants. As a whole, these data clearly indicate that structural–functional relationships in Nbs strongly differ from what observed in mammalian and truncated hemoproteins, suggesting that Nbs play a functional role clearly distinct from other eukaryotic and prokaryotic hemoproteins. |
format | Online Article Text |
id | pubmed-7915275 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79152752021-03-01 Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties De Simone, Giovanna di Masi, Alessandra Pesce, Alessandra Bolognesi, Martino Ciaccio, Chiara Tognaccini, Lorenzo Smulevich, Giulietta Abbruzzetti, Stefania Viappiani, Cristiano Bruno, Stefano Monaca, Sara Della Pietraforte, Donatella Fattibene, Paola Coletta, Massimo Ascenzi, Paolo Int J Mol Sci Article Structural and functional properties of ferrous Mycobacterium tuberculosis (Mt-Nb) and human (Hs-Nb) nitrobindins (Nbs) were investigated. At pH 7.0 and 25.0 °C, the unliganded Fe(II) species is penta-coordinated and unlike most other hemoproteins no pH-dependence of its coordination was detected over the pH range between 2.2 and 7.0. Further, despite a very open distal side of the heme pocket (as also indicated by the vanishingly small geminate recombination of CO for both Nbs), which exposes the heme pocket to the bulk solvent, their reactivity toward ligands, such as CO and NO, is significantly slower than in most hemoproteins, envisaging either a proximal barrier for ligand binding and/or crowding of H(2)O molecules in the distal side of the heme pocket which impairs ligand binding to the heme Fe-atom. On the other hand, liganded species display already at pH 7.0 and 25 °C a severe weakening (in the case of CO) and a cleavage (in the case of NO) of the proximal Fe-His bond, suggesting that the ligand-linked movement of the Fe(II) atom onto the heme plane brings about a marked lengthening of the proximal Fe-imidazole bond, eventually leading to its rupture. This structural evidence is accompanied by a marked enhancement of both ligands dissociation rate constants. As a whole, these data clearly indicate that structural–functional relationships in Nbs strongly differ from what observed in mammalian and truncated hemoproteins, suggesting that Nbs play a functional role clearly distinct from other eukaryotic and prokaryotic hemoproteins. MDPI 2021-02-07 /pmc/articles/PMC7915275/ /pubmed/33562340 http://dx.doi.org/10.3390/ijms22041674 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article De Simone, Giovanna di Masi, Alessandra Pesce, Alessandra Bolognesi, Martino Ciaccio, Chiara Tognaccini, Lorenzo Smulevich, Giulietta Abbruzzetti, Stefania Viappiani, Cristiano Bruno, Stefano Monaca, Sara Della Pietraforte, Donatella Fattibene, Paola Coletta, Massimo Ascenzi, Paolo Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title | Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title_full | Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title_fullStr | Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title_full_unstemmed | Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title_short | Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties |
title_sort | mycobacterial and human ferrous nitrobindins: spectroscopic and reactivity properties |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915275/ https://www.ncbi.nlm.nih.gov/pubmed/33562340 http://dx.doi.org/10.3390/ijms22041674 |
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