Bioinorganic Chemistry by Alfred X. Trautwein, Eckhard Bill, Emile L. Bominaar (auth.)
By Alfred X. Trautwein, Eckhard Bill, Emile L. Bominaar (auth.)
Contents: A.X. Trautwein, E. invoice, E.L. Bominaar, H. Winkler, Lübeck, FRG: Iron-Containing Proteins and comparable Analogs - Complementary Mössbauer, EPR and Magnetic Susceptibility Studies.- B.K. Keppler, C. Friesen, H.G. Moritz, H. Vongerichten, E. Vogel, Heidelberg, FRG: Tumor-Inhibiting Bis(ß-Diketonato) steel Complexes: Budotitane.- O.M.N. Dhubhghaill, P.J. Sadler, London, united kingdom: The constitution and Reactivity of Arsenic Compounds: Biological job and Drug Design.
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The complex then possesses an easy plane of magnetization, giving spin expectations values mainly within the molecular xy plane for the majority of the crystal orientations relative to the applied field. 0 T. The anisotropy of the A tensor is, within the tolerance, compatible with the dipolar field predicted for the admixture of 15% 4A 2 character into the ground doublet, deduced from the g__ value. 2 K show that the hyperfine fields, and the associated line splittings in the spectra, reach their saturation value already for small applied fields (B> 10 mT).
0 , which are characteristic of a IMs = +_1/2) Kramers doublet of spin S = 3/2 in axial ligand field with weak rhombic distortion. From the first-order perturbation expression gx, elfy = 4 _+ 6 . 01. We note, that signals of paramagnetic Fe-S centers in the protein are saturated under the measuring conditions of Fig. 20. 38 Alfred X. Trautwein et al. 96 I Fig. 20. 6 K. 2 M6ssbauer Spectroscopy PMO contains one [2Fe-2S] cluster and one mononuclear non-heme iron (cofactor) per active center. The protein can be reversibly depleted from its cofactor iron and reconstituted with ferrous iron under reducing conditions in the presence of substrate .
This procedure is comparable to measurements of the static magnetic susceptibility and has approximately the same accuracy, however, with the advantage that contributions from different paramagnetic centers can be discerned. An application is illustrated in Fig. 18 for the ferric iron in the heme enzyme prostaglandin-H-synthase (PGHsynthase) [32, 33, 34]. Moderate values of D (~g[3B) can also be determined by EPR from the competition of zero-field interaction with Zeeman interaction (Sect. 3). The magnetic perturbation of the spin multiplet by the resonance field causes mixing of wave functions, depending on D and g[3B.