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Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins
Hemoproteins include several heme-binding proteins with distinct structure and function. The presence of the heme group confers specific reactivity and spectroscopic properties to hemoproteins. In this review, we provide an overview of five families of hemoproteins in terms of dynamics and reactivit...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10135655/ https://www.ncbi.nlm.nih.gov/pubmed/37189430 http://dx.doi.org/10.3390/biom13040683 |
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author | Turilli-Ghisolfi, Emily Samuela Lualdi, Marta Fasano, Mauro |
author_facet | Turilli-Ghisolfi, Emily Samuela Lualdi, Marta Fasano, Mauro |
author_sort | Turilli-Ghisolfi, Emily Samuela |
collection | PubMed |
description | Hemoproteins include several heme-binding proteins with distinct structure and function. The presence of the heme group confers specific reactivity and spectroscopic properties to hemoproteins. In this review, we provide an overview of five families of hemoproteins in terms of dynamics and reactivity. First, we describe how ligands modulate cooperativity and reactivity in globins, such as myoglobin and hemoglobin. Second, we move on to another family of hemoproteins devoted to electron transport, such as cytochromes. Later, we consider heme-based reactivity in hemopexin, the main heme-scavenging protein. Then, we focus on heme–albumin, a chronosteric hemoprotein with peculiar spectroscopic and enzymatic properties. Eventually, we analyze the reactivity and dynamics of the most recently discovered family of hemoproteins, i.e., nitrobindins. |
format | Online Article Text |
id | pubmed-10135655 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-101356552023-04-28 Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins Turilli-Ghisolfi, Emily Samuela Lualdi, Marta Fasano, Mauro Biomolecules Review Hemoproteins include several heme-binding proteins with distinct structure and function. The presence of the heme group confers specific reactivity and spectroscopic properties to hemoproteins. In this review, we provide an overview of five families of hemoproteins in terms of dynamics and reactivity. First, we describe how ligands modulate cooperativity and reactivity in globins, such as myoglobin and hemoglobin. Second, we move on to another family of hemoproteins devoted to electron transport, such as cytochromes. Later, we consider heme-based reactivity in hemopexin, the main heme-scavenging protein. Then, we focus on heme–albumin, a chronosteric hemoprotein with peculiar spectroscopic and enzymatic properties. Eventually, we analyze the reactivity and dynamics of the most recently discovered family of hemoproteins, i.e., nitrobindins. MDPI 2023-04-17 /pmc/articles/PMC10135655/ /pubmed/37189430 http://dx.doi.org/10.3390/biom13040683 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Turilli-Ghisolfi, Emily Samuela Lualdi, Marta Fasano, Mauro Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title | Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title_full | Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title_fullStr | Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title_full_unstemmed | Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title_short | Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins |
title_sort | ligand-based regulation of dynamics and reactivity of hemoproteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10135655/ https://www.ncbi.nlm.nih.gov/pubmed/37189430 http://dx.doi.org/10.3390/biom13040683 |
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