2016
DOI: 10.1039/c5cp07621h
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Single and double nitroxide labeled bis(terpyridine)-copper(ii): influence of orientation selectivity and multispin effects on PELDOR and RIDME

Abstract: A rigid, nitroxide substituted terpyridine ligand has been used to synthesize hetero- and homoleptic bis-terpyridine complexes of copper(II). The homoleptic complex represents a three-spin system, while the metal ion in the heteroleptic complex is in average bound to one nitroxide bearing ligand. Both complexes are used as model systems for EPR distance measurements using pulsed electron-electron double resonance (PELDOR or DEER) and relaxation induced dipolar modulation enhancement (RIDME) sequences. The resu… Show more

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Cited by 40 publications
(63 citation statements)
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References 65 publications
(94 reference statements)
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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%
“…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%
“…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%
“…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 trueSNR=λσn …”
Section: Pds Pulse Sequences and Signalsmentioning
confidence: 99%