A high‐resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties

Enrico Ravera; Lucia Gigli; Elizaveta A. Suturina; Vito Calderone; Marco Fragai; Giacomo Parigi; Claudio Luchinat

doi:10.1002/ange.202101149

A high‐resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties

Enrico Ravera, Lucia Gigli, Elizaveta A. Suturina, Vito Calderone, Marco Fragai, Giacomo Parigi, Claudio Luchinat

Department of Chemistry

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Abstract

Metalloproteins constitute a significant fraction of the proteome of all organisms and their characterization is critical for both basic sciences and biomedical applications. A large portion of metalloproteins bind paramagnetic metal ions, and paramagnetic NMR spectroscopy has been widely used in their structural characterization. However, the signals of nuclei in the immediate vicinity of the metal center are often broadened beyond detection. In this work, we show that it is possible to determine the coordination environment of the paramagnetic metal in the protein at a resolution inaccessible to other techniques. Taking the structure of a diamagnetic analogue as a starting point, a geometry optimization is carried out by fitting the pseudocontact shifts obtained from first principles quantum chemical calculations to the experimental ones.

Original language	English
Pages (from-to)	15087-15093
Journal	Angewandte Chemie
Volume	133
Issue number	27
Early online date	17 Feb 2021
DOIs	https://doi.org/10.1002/ange.202101149
Publication status	Published - 25 Jun 2021

Bibliographical note

Funding Information:
This work is dedicated to Ivano Bertini (1940–2012), founder of CERM and pioneer of Biological Inorganic Chemistry. The characterization of metal coordination in biological systems through NMR was a very important part of his research, of which this work is a natural evolution. This work has been supported by the Fondazione Cassa di Risparmio di Firenze, and the Italian Ministero dell′Istruzione, dell′Università e della Ricerca through the “Progetto Dipartimenti di Eccellenza 2018–2022” to the Department of Chemistry “Ugo Schiff” of the University of Florence, and the University of Florence through the “Progetti Competitivi per Ricercatori” to ER. LG acknowledges the support of an EMBO Short‐Term Fellowship (STF8629). We acknowledge the CINECA award to ER under the ISCRA initiative, for the availability of high‐performance computing resources and support. The authors acknowledge the support and the use of resources of Instruct‐ERIC, a landmark ESFRI project, and specifically the CERM/CIRMMP Italy center.

Publisher Copyright:
© 2021 Wiley-VCH GmbH

Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.

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10.1002/ange.202101149

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This is the peer reviewed version of the following article: Ravera, E, Gigli, L, Suturina, EA, Calderone, V, Fragai, M, Parigi, G & Luchinat, C 2021, 'A high‐resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties', Angewandte Chemie. 9, which has been published in final form at https://doi.org/10.1002/ange.20210114. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
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abstract = "Metalloproteins constitute a significant fraction of the proteome of all organisms and their characterization is critical for both basic sciences and biomedical applications. A large portion of metalloproteins bind paramagnetic metal ions, and paramagnetic NMR spectroscopy has been widely used in their structural characterization. However, the signals of nuclei in the immediate vicinity of the metal center are often broadened beyond detection. In this work, we show that it is possible to determine the coordination environment of the paramagnetic metal in the protein at a resolution inaccessible to other techniques. Taking the structure of a diamagnetic analogue as a starting point, a geometry optimization is carried out by fitting the pseudocontact shifts obtained from first principles quantum chemical calculations to the experimental ones.",

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A high‐resolution view of the coordination environment in a paramagnetic metalloprotein from its magnetic properties

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