4.3 Article

NMR of Paramagnetic Proteins: 13C Derived Paramagnetic Relaxation Enhancements Are an Additional Source of Structural Information in Solution

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MAGNETOCHEMISTRY
卷 9, 期 3, 页码 -

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MDPI
DOI: 10.3390/magnetochemistry9030066

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HIPIP; iron-sulfur proteins; metalloproteins; structural biology; paramagnetic NMR; paramagnetic relaxation enhancement; NMR solution structure

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In paramagnetic metalloproteins, C-13 ' and C-13(alpha) nuclei can be measured to obtain electron spin-nuclear spin distance restraints. These C-13 based restraints provide additional structural information that is not redundant with the more commonly used H-1 nuclei. This study demonstrates the complementarity of C-13 PRE restraints with H-1 PRE restraints, showing that C-13 R-1 values can be measured at short distances from the paramagnetic center and can be combined with other NMR restraints to improve the quality and quantity of the NMR information.
In paramagnetic metalloproteins, longitudinal relaxation rates of C-13 ' and C-13(alpha) nuclei can be measured using C-13 detected experiments and converted into electron spin-nuclear spin distance restraints, also known as Paramagnetic Relaxation Enhancement (PRE) restraints. C-13 are less sensitive to paramagnetism than H-1 nuclei, therefore, C-13 based PREs constitute an additional, non-redundant, structural information. We will discuss the complementarity of C-13 PRE restraints with H-1 PRE restraints in the case of the High Potential Iron Sulfur Protein (HiPIP) PioC, for which the NMR structure of PioC has been already solved by a combination of classical and paramagnetism-based restraints. We will show here that C-13 R-1 values can be measured also at very short distances from the paramagnetic center and that the obtained set of C-13 based restraints can be added to H-1 PREs and to other classical and paramagnetism based NMR restraints to improve quality and quantity of the NMR information.

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