Mössbauer Spectroscopy and Transition Metal Chemistry

Gütlich, Philipp; Link, Rainer; Trautwein, Alfred X.

doi:10.1007/978-3-662-12545-8

Cited by 432 publications

(382 citation statements)

References 0 publications

Supporting

Mentioning

334

Contrasting

Unclassified

Order By: Relevance

“…The experimental values of the magnetic hyperfine coupling tensors A in 1-270 (Table S1) reflect this approximation, since the A values for the two subspectra have opposite signs, resulting from the spins of the individual ions being parallel and antiparallel to the applied field. The ferric site, with the larger spin, has negative A-tensor components as expected, according to the negative intrinsic A values for isolated FeS 4 sites due to the strong negative Fermi-contact contribution [17]. In conclusion, the [2Fe-2S] ?…”

Section: Reduced 1-270 Construct Of Anamorsinsupporting

confidence: 71%

“…The hypothesis is supported by the fact that the isomer shift of the ferric site does not decrease with temperature in the range 160-220 K (Table 3), as would be expected for any ''isolated'' iron with a localized valence state. The temperature invariance is indeed completely against the usual trend of isomer shifts to decrease with temperature owing to the increasing second-order Doppler shift [17]. The observed opposite behavior can only occur if the ferric site gains ferrous character from increasing electron delocalization, caused by either coherent resonance interaction or the onset of incoherent ''electron hopping.''…”

Section: Reduced Fl Constructmentioning

confidence: 80%

“…by diagonalization of the usual spin Hamiltonian for the spin S = 1/2 of the [2Fe-2S] clusters; the hyperfine interactions for both 57 Fe sites were calculated by using the usual nuclear Hamiltonian with hyperfine coupling constant given with respect to S [17,18].…”

Section: Mössbauer Spectroscopymentioning

confidence: 99%

“…Consistently, no histidine residues are present close to the M2 motif and only one histidine residue is present in the entire CIAPIN1 domain, the third from last residue at the C-terminus. Oxygen coordination can be also excluded as quadrupole splittings and isomer shifts larger than those measured in the Mössbauer spectrum of the oxidized FL are expected to be observed [17,32]. Although each [2Fe-2S] cluster bound to either the M1 motif or the M2 motif of anamorsin is ligated by four cysteine residues, the Mössbauer parameters of these [2Fe-2S] clusters in their reduced state share some features with the Rieske centers, having a two-histidine/two-cysteine coordination (Table 2).…”

Section: Reduced Fl Constructmentioning

confidence: 99%

See 3 more Smart Citations

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

et al. 2013

View full text Add to dashboard Cite

The eukaryotic anamorsin protein family, which has recently been proposed to be part of an electron transfer chain functioning in the early steps of cytosolic iron-sulfur (Fe/S) protein biogenesis, is characterized by a largely unstructured domain (CIAPIN1) containing two conserved cysteine-rich motifs (CX 8 CX 2 CXC and CX 2 CX 7 CX 2 C) whose Fe/S binding properties and electronic structures are not well defined. Here, we found that (1) each motif in human anamorsin is able to bind independently a [2Fe-2S] cluster through its four cysteine residues, the binding of one cluster mutually excluding the binding of the second, (2) the reduced [2Fe-2S] ? clusters exhibit a unique electronic structure with considerable anisotropy in their coordination environment, different from that observed in reduced, plant-type and vertebratetype [2Fe-2S] ferredoxin centers, (3) the reduced cluster bound to the CX 2 CX 7 CX 2 C motif reveals an unprecedented valence localization-to-delocalization transition as a function of temperature, and (4) only the [2Fe-2S] cluster bound to the CX 8 CX 2 CXC motif is involved in the electron transfer with its physiological protein partner Ndor1. The unique electronic properties of both [2Fe-2S] centers can be interpreted by considering that both cysteine-rich motifs are located in a highly unstructured and flexible protein region, whose local conformational heterogeneity can induce anisotropy in metal coordination. This study contributes to the understanding of the functional role of the CIAPIN1 domain in the anamorsin family, suggesting that only the [2Fe-2S] cluster bound to the CX 8 CX 2 CXC motif is indispensable in the electron transfer chain assembling cytosolic Fe/S proteins.

show abstract

Section: Reduced 1-270 Construct Of Anamorsinsupporting

confidence: 71%

Section: Reduced Fl Constructmentioning

confidence: 80%

Section: Mössbauer Spectroscopymentioning

confidence: 99%

Section: Reduced Fl Constructmentioning

confidence: 99%

See 2 more Smart Citations

Human anamorsin binds [2Fe–2S] clusters with unique electronic properties

et al. 2013

View full text Add to dashboard Cite

show abstract

“…[2][3][4][5][6][7] The method is based on the Mössbauer effect 1 which is the recoil emission/absorption of γ radiation from a solid sample. [2][3][4] The most well-known application of Mössbauer spectroscopy is for the determination of 57 Fe in metal complexes. However, there exist more than 40 other elements in the periodic table which possess γ-active isotopes and for which the Mössbauer spectra can be obtained.…”

Section: Introductionmentioning

confidence: 99%

DFT Approach to the Calculation of Mössbauer Isomer Shifts

Kurian

Filatov

2008

J. Chem. Theory Comput.

View full text Add to dashboard Cite

With the help of a recently suggested computational scheme [J. Chem. Phys. 2007, 127, 084101], Mössbauer isomer shifts are calculated within the context of density functional theory, for a series of iron containing compounds. The influence of the choice of a density functional and of the truncation of a basis set on the results of calculations is analyzed. It has been observed that the hybrid density functionals, especially BH&HLYP, provide better correlation with experimental results than pure density functionals. The analysis of basis set truncation reveals that the addition (or removal) of the tightmost primitive functions to a large uncontracted basis set has only a minor influence on the calculated isomer shift values. It is observed that, with the use of a small contracted basis set, a reasonable accuracy for the calculated isomer shifts can be achieved.

show abstract