Magnetic susceptibility in paramagnetic NMR

Bertini, Ivano; Luchinat, Claudio; Parigi, Giacomo

doi:10.1016/s0079-6565(02)00002-x

Cited by 442 publications

(392 citation statements)

References 4 publications

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“…This is in agreement with the smaller values of the axial and rhombic anisotropy of the magnetic susceptibility tensor found by 1 H-NMR for ferric H64Q/V68FmNgb-CN compared to the cyanide complexes of vertebrate Mb and Hbs [22]. The magnetic susceptibility tensor determined by NMR correlates with the g tensor determined by EPR [50]. In the following, we will consider the factors that could possibly explain why the g z values of NGB-CN and its mutants are much lower than those of MbCN and HbCN.…”

Section: Discussionsupporting

confidence: 84%

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EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin

Doorslaer

Trandafir

Harmer

et al. 2014

Biophysical Chemistry

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Section: Discussionsupporting

confidence: 84%

“…This expression is valid if only the ground-state contribution needs to be considered and all excited states can be ignored [41,49,50,59,60]. It has been known for a long time that this is not valid for cyanide complexes of haem proteins [49,59], for which the first excited state is contributing to a large extent at room temperature.…”

Section: Discussionmentioning

confidence: 99%

EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin

Doorslaer

Trandafir

Harmer

et al. 2014

Biophysical Chemistry

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“…Focusing on the dipolar component of the hyperfine tensor, A dip , there is a decrease along the series from Mn to Ni, hence giving a progressively smaller contribution to the shift anisotropy, as seen by comparing terms (e) of Table IV. The calculated tensor with no spin-orbit coupling inclusion corresponds to the dipolar interaction between the magnetic moments of the observed nucleus and magnetic moment of the TM ion [29,36]. the considered ions reported in Table II, a progressively weaker dipolar interaction is observed when going from Mn 2+ towards Ni 2+ .…”

Section: Resultsmentioning

confidence: 93%

“…calization of the unpaired-electron spin density from the TM sites towards the s orbitals of the OC is prominent [36]. Terms (b), (c) and (d) represent the spin-orbit coupling contributions to the total contact shielding, either via the g-shift or the spin-orbit-based A FC,2 term.…”

Section: Theorymentioning

confidence: 99%

DFT investigation of the effect of spin-orbit coupling on the NMR shifts in paramagnetic solids

et al. 2017

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Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for studying the structural and electronic properties of paramagnetic solids. However, the interpretation of paramagnetic NMR spectra is often challenging as a result of the interactions of unpaired electrons with the nuclear spins of interest. In this work, we extend the formalism of the paramagnetic NMR shielding in the presence of spin-orbit coupling towards solid systems with multiple paramagnetic centres. We demonstrate how the single-ion Electron Paramagnetic Resonance (EPR) g-tensor is defined and calculated in periodic paramagnetic solids. We then calculate the hyperfine tensor and the g-tensor with density functional theory (DFT) to show the validity of the presented model and we further demonstrate how these interactions can be combined to give the overall paramagnetic shielding tensor, σ s . The method is applied to a series of olivine-type LiTMPO4 materials (with TM=Mn, Fe, Co and Ni) and the corresponding 7 Li and 31 P NMR spectra are simulated. We analyse the effects of spin-orbit coupling and of the electron-nuclear magnetic interactions on the calculated NMR parameters. A detailed comparison is presented between contact and dipolar interactions across the LiTMPO4 series, in which the magnitudes and signs of the non-relativistic and relativistic components of the overall isotropic shift and shift anisotropy are computed and rationalized.

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“…These methods require the introduction of spin-labels (Tamm et al 2007;Schiemann and Prisner 2007;Keizers and Ubbink 2011;Yagi et al 2011;Loscha et al 2012;Russo et al 2013) attached to or within a protein. In NMR-spectroscopic studies, attachment of a single paramagnetic lanthanide center (Keizers and Ubbink 2011) with an anisotropic Dv-tensor (Bertini et al 2002) has been employed to obtain PCSs, which report on the distance and radial coordinates of a nuclear spin with respect to the paramagnetic center. For Gd 3?…”

Section: Introductionmentioning

confidence: 99%

Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy

et al. 2015

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We recently engineered encodable lanthanide binding tags (LBTs) into proteins and demonstrated their applicability in Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography and luminescence studies. Here, we engineered two-loop-LBTs into the model protein interleukin-1b (IL1b) and measured 1 H, 15 Npseudocontact shifts (PCSs) by NMR spectroscopy. We determined the Dv-tensors associated with each Tm 3? -loaded loop-LBT and show that the experimental PCSs yield structural information at the interface between the two metal ion centers at atomic resolution. Such information is very valuable for the determination of the sites of interfaces in protein-protein-complexes. Combining the experimental PCSs of the two-loop-LBT construct IL1b-S2R2 and the respective single-loop-LBT constructs IL1b-S2, IL1b-R2 we additionally determined the distance between the metal ion centers. Further, we explore the use of two-loop LBTs loaded with Gd 3? as a novel tool for distance determination by Electron Paramagnetic Resonance spectroscopy and show the NMR-derived distances to be remarkably consistent with distances derived from Pulsed Electron-Electron Dipolar Resonance.

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Magnetic susceptibility in paramagnetic NMR

Cited by 442 publications

References 4 publications

EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin

EPR analysis of cyanide complexes of wild-type human neuroglobin and mutants in comparison to horse heart myoglobin

DFT investigation of the effect of spin-orbit coupling on the NMR shifts in paramagnetic solids

Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy

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