Articles | Volume 2, issue 1
Research article
26 Apr 2021
Research article |  | 26 Apr 2021

The long-standing relationship between paramagnetic NMR and iron–sulfur proteins: the mitoNEET example. An old method for new stories or the other way around?

Francesca Camponeschi, Angelo Gallo, Mario Piccioli, and Lucia Banci

Related subject area

Field: Liquid-state NMR | Topic: Applications – biological macromolecules
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Cited articles

Andersson, P., Weigelt, J., and Otting, G.: Spin-state selection filters for the measurement of heteronuclear one-bond coupling constants, J. Biomol. NMR, 12, 435–441,, 1998. 
Arnesano, F., Banci, L., Bertini, I., Felli, I. C., Luchinat, C., and Thompsett, A. R.: A Strategy for the NMR Characterization of Type II Copper(II) Proteins: the Case of the Copper Trafficking Protein CopC from Pseudomonas Syringae, J. Am. Chem. Soc., 125, 7200–7208,, 2003. 
Arnesano, F., Banci, L., and Piccioli, M.: NMR structures of paramagnetic metalloproteins, Q. Rev. Biophys., 38, 167–219,, 2005. 
Bak, D. W., Zuris, J. A., Paddock, M. L., Jennings, P. A., and Elliott, S. J.: Redox Characterization of the FeS Protein MitoNEET and Impact of Thiazolidinedione Drug Binding, Biochemistry, 48, 10193–10195,, 2009. 
Short summary
The iron–sulfur cluster binding properties of human mitoNEET have been investigated by 1D and 2D 1H paramagnetic NMR spectroscopy. The NMR spectra of both oxidized and reduced mitoNEET are significantly different from those reported previously for other [Fe2S2] proteins. Our findings revealed the unique electronic properties of mitoNEET and suggests that the specific electronic structure of the cluster possibly drives the functional properties of different [Fe2S2] proteins.