Single and double nitroxide labeled bis(terpyridine)-copper(<scp>ii</scp>): influence of orientation selectivity and multispin effects on PELDOR and RIDME

Meyer, Andreas; Abdullin, Dinar; Schnakenburg, Gregor; Schiemann, Olav

doi:10.1039/c5cp07621h

Cited by 40 publications

(63 citation statements)

References 65 publications

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“…The latter case has severala dvantages and applications: 1) the use of metal centers forP DS allows to reduce the number of spin labels and, consequently,t he number of protein mutations, 2) it enables orthogonal spin labeling [8] as the metal center has different spectroscopic properties than the majority of spin labels, 3) the distance constraintso btained from such PDS measurementse nable the localization of metal ions within the protein fold by trilateration [9,10] and the docking of different parts of protein complexes using metal ions as anchor points. [11] To date, PDS measurements have been applied to av ariety of different intrinsic metal centers, such as Cu 2 + , [12][13][14][15][16][17][18][19][20] Mn 2 + , [21][22][23][24][25] Co 2 + , [26,27] and low-spin Fe 3 + , [6,[28][29][30][31] as well as ironsulfur [17,[32][33][34] and manganese [35,36] clusters. In all these cases, the protocols for PSD measurements are well-established and the extractiono fd istance constraints from the corresponding PDS data can be readily achieved under the high-field approximation.…”

Section: Introductionmentioning

confidence: 99%

Pulsed EPR Dipolar Spectroscopy under the Breakdown of the High‐Field Approximation: The High‐Spin Iron(III) Case

Abdullin

Matsuoka

Yulikov

et al. 2019

Chemistry A European J

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Pulsed EPR dipolar spectroscopy (PDS) offers several methodsf or measuring dipolarc oupling and thus the distance between electron-spin centers. To date, PDS measurements to metal centers were limited to ions that adhere to the high-field approximation. Here, the PDS methodology is extended to cases where the high-field approximation breaks down on the example of the high-spinF e 3 + /nitroxide spin-pair.F irst, the theory developed by Maryasov et al. (Appl. Magn. Reson. 2006, 30,6 83-702) was adapted to derive equations for the dipolar coupling constant,w hich revealed that the dipolar spectrum does not only depend on the length and orientation of the interspin distance vector with respect to the applied magnetic field but also on its orientation to the effective g-tensor of the Fe 3 + ion. Then, it is showno nam odel system and ah eme protein that aP DS method called relaxation-inducedd ipolarm odulation enhancement (RIDME)i sw ell-suited to measuring such spectra and that the experimentally obtained dipolar spectra are in full agreement with the derived equations. Finally,aRIDME data analysisp rocedure was developed, which facilitates the determination of distance and angular distributions from the RIDMEd ata. Thus, this study enables the application of PDS to for example, the highly relevant class of high-spinF e 3 + heme proteins.Supporting information and the ORCID identification number(s) for the <-author(s) of this article can be found under: https://doi.

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Section: Introductionmentioning

confidence: 99%

Pulsed EPR Dipolar Spectroscopy under the Breakdown of the High‐Field Approximation: The High‐Spin Iron(III) Case

Abdullin

Matsuoka

Yulikov

et al. 2019

Chemistry A European J

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“…In order to avoid using narrow bandwidth excitation pulses as used in DEER sequences, an alternative method uses the natural longitudinal relaxation of the metal ion to probe the dipolar interaction between it and a nitroxide [48,49]. This method, relaxation-induced dipolar modulation enhancement (RIDME), is suited to situations where the relaxation profiles of each spin centre are quite different (discussed further below) and has been used to analyse not only copper complexes, but also complexes with metals having far larger g-anisotropy than copper, such as iron and gadolinium [49][50][51].…”

Section: Using Epr To Determine a Copper(ii)-nitroxide Distancementioning

confidence: 99%

Nitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function

Jones

Berliner

2016

Cell Biochem Biophys

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Copper is one of the most abundant biological metals, and its chemical properties mean that organisms need sophisticated and multilayer mechanisms in place to maintain homoeostasis and avoid deleterious effects. Studying copper proteins requires multiple techniques, but electron paramagnetic resonance (EPR) plays a key role in understanding Cu(II) sites in proteins. When spin-labels such as aminoxyl radicals (commonly referred to as nitroxides) are introduced, then EPR becomes a powerful technique to monitor not only the coordination environment, but also to obtain structural information that is often not readily available from other techniques. This information can contribute to explaining how cuproproteins fold and misfold. The theory and practice of EPR can be daunting to the non-expert; therefore, in this mini review, we explore how nitroxide spin-labelling can be used to help the inorganic biochemist gain greater understanding of cuproprotein structure and function in vitro and how EPR imaging may help improve understanding of copper homoeostasis in vivo.

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“…Usually, it is desirable to have a larger modulation depth, because it contributes to the SNR. The SNR of the PDS time trace is often defined as

true S N R = \frac{λ}{σ_{n}}

…”

Section: Pds Pulse Sequences and Signalsmentioning

confidence: 99%

Pulsed Dipolar EPR Spectroscopy and Metal Ions: Methodology and Biological Applications

Abdullin

Schiemann

2020

ChemPlusChem

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Pulsed dipolar electron paramagnetic resonance spectroscopy (PDS) is a valuable method for determining biomolecular structures and their conformational changes during function. Often, this method is applied to paramagnetic metal ions that are either intrinsic co‐factors of biomolecules or introduced into biomolecules as spin labels. Here, the key achievements and the remaining challenges of PDS on metal ions are summarized and critically discussed. The first part of the Review describes the methodology of PDS experiments and the related data analysis for each of the biologically relevant paramagnetic metal centers. The second part highlights applications with the aim to give an idea about what kind of questions from structural biology can be answered by PDS‐based distance measurements involving metal centers.

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Single and double nitroxide labeled bis(terpyridine)-copper(ii): influence of orientation selectivity and multispin effects on PELDOR and RIDME

Cited by 40 publications

References 65 publications

Pulsed EPR Dipolar Spectroscopy under the Breakdown of the High‐Field Approximation: The High‐Spin Iron(III) Case

Pulsed EPR Dipolar Spectroscopy under the Breakdown of the High‐Field Approximation: The High‐Spin Iron(III) Case

Nitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function

Pulsed Dipolar EPR Spectroscopy and Metal Ions: Methodology and Biological Applications

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