Two Allogons of an O2 -activating Bis(disiloxido)ferrate(II) Accessible Selectively just by Variation of the Crystallization Temperature.

Deprotonation of O(iPr2 SiOH)2 (iPr LH2 ) with LiOtBu followed by reaction with FeCl2 in THF led to the complex [iPr L2 Fe][Li(THF)2 ]2 , 2, which represents a structural and spectroscopic model of the α-Fe sites of Fe/ZSM-5. Reaction with O2 in THF solution proceeds rather fast and is complete within 200 ms; an intermediate O2 adduct could not be identified by stopped-flow methods. Cooling blue solutions of 2 to -80 °C led to the growth of blue crystals of 2⋅THF, the analysis of which by XRD revealed a FeO4 core that is somewhat distorted from planarity towards a tetrahedral structure. By contrast, cooling such solutions to -30 °C led to pink crystals of an allogon featuring a perfectly square planar FeO4 entity. Hence, 2 represents a unique case where two different structural isomers (allogons) can be crystallized from the same solvent selectively, controlled by the temperature. DFT calculations were performed to understand this finding.

Stepwise assembly of the active site of [NiFe]-hydrogenase.

[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H2 into 2e- and 2H+ under ambient conditions. Catalysis takes place at the heterobimetallic NiFe(CN)2(CO) center, whose multistep biosynthesis involves careful handling of two transition metals as well as potentially harmful CO and CN- molecules. Here, we investigated the sequential assembly of the [NiFe] cofactor, previously based on primarily indirect evidence, using four different purified maturation intermediates of the catalytic subunit, HoxG, of the O2-tolerant membrane-bound hydrogenase from Cupriavidus necator. These included the cofactor-free apo-HoxG, a nickel-free version carrying only the Fe(CN)2(CO) fragment, a precursor that contained all cofactor components but remained redox inactive and the fully mature HoxG. Through biochemical analyses combined with comprehensive spectroscopic investigation using infrared, electronic paramagnetic resonance, Mössbauer, X-ray absorption and nuclear resonance vibrational spectroscopies, we obtained detailed insight into the sophisticated maturation process of [NiFe]-hydrogenase.

Cobalt and Iron Stabilized Ketyl, Ketiminyl and Aldiminyl Radical Anions.

Carbonyl and iminyl based radical anions are reactive intermediates in a variety of transformations in organic synthesis. Herein, the isolation of ketyl, and more importantly unprecedented ketiminyl and aldiminyl radical anions coordinated to cobalt and iron complexes is presented. Insights into the electronic structure of these unusual metal bound radical anions is provided by X-Ray diffraction analysis, NMR, IR, UV/Vis and Mössbauer spectroscopy, solid and solution state magnetometry, as well as a by a detailed computational analysis. The metal bound radical anions are very reactive and facilitate the activation of intra- and intermolecular C-H bonds.