Iron spectroscopic terms

FeMoco, both as a constituent of the FeMo protein and an isolated entity, has been the subject of detailed spectroscopic examination. 57Fe Mossbauer and EPR studies of the cofactor have been interpreted in terms of an S = centre that contains one molybdenum and ca. six irons in a spin-coupled structure. The EPR signal serves as a valuable fingerprint of FeMoco furthermore, release of FeMoco from the FeMo protein produces an EPR spectrum with broader features, but the same profile, thereby indicating that the core of this cluster is little changed by the extraction procedure. Treatment of FeMoco with ca. one equivalent of... 

Of the various techniques routinely available, IR and 13C NMR spectroscopy usually provide the most valuable information in terms of the determination of the most appropriate valence description (A-D, Chart 1) of the carbon fragment. Mossbauer spectroscopy has also been used with good effect with iron-containing poly-carbon complexes.89 This solution-based work is complemented by a significant number of solid-state structural studies, which are described in greater detail below. Electronic spectroscopic methods, including luminescence methods, have been used to probe the electronic structures of a small number of poly-yndiyl complexes and polymers.288 315 340 342 377 380 Selected IR, 13C NMR, and UV-vis data have been given in Tables I-VIII, above. 

Combined EPR and 57Fe Mossbauer spectroscopic studies of the MoFe protein in various overall oxidation states39 40,42,44 48,49) have provided strong evidence for the presence of six metal clusters two M centers that are the protein-bound form of the FeMo-cofactor (a novel Mo-Fe-S cluster) and four unusual tetranuclear iron clusters referred to as the P clusters. These will be discussed separately below. In addition, Mossbauer spectra of MoFe proteins from Azotobacter vinelandii, Clostridium pas-teurianum, and Klebsiella pneumoniae all show an additional component termed S39 40 42, which accounts for 6% of the total Fe present (2 Fe per molecule) and which has Mossbauer parameters (AEq = 1.35 mm/s d = 0.60 mm/s) different from those expected for likely impurities such as high-spin Fe2+ or Fe3+ ( adventitious iron). At present, it is difficult to decide whether species S is an unusual and persistent impurity or an integral part of the MoFe protein. 

The [Fe(terpy)2] cation is low-spin, as demonstrated by Mossbauer, electronic, H NMR, and resonance Raman spectroscopy and magnetic measurements (20,184,187, 228, 266). Similarly, spectroscopic studies of the iron(III) cation have indicated a low-spin ( B) ground term (382). There have been numerous electrochemical studies of the bis complexes (177, 200, 256, 298, 332, 344, 373, 378, 379, 397, 398). Ligand-centered reductions to formal oxidation states of iron(I), iron(O), and iron( — 1) and oxidations to iron(III) are observed. The complex [Fe(terpy)L][C104]2 [L = tris(2 -pyridyl)l,3,5-triazine (Fig. 15)] has been prepared (399, 442). 

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