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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)15087-15093
JournalAngewandte Chemie
Volume133
Issue number27
Early online date17 Feb 2021
DOIs
Publication statusPublished - 25 Jun 2021

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