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2. Di(indenyl)beryllium

   https://doi.org/10.1002/anie.202107980  

   Koby, Ross_F; Schley, Nathan_D; Hanusa, Timothy_P (August 2021, Angewandte Chemie International Edition)

   Abstract The bonding in beryllocene, [BeCp₂], took decades to establish, owing to its unexpected mixed hapticity structure (i.e., [Be(η⁵‐Cp)(η¹‐Cp)]). Beryllium complexes containing the indenyl ligand, which is a close relative of the cyclopentadienyl anion, but which is also known to exhibit its own bonding peculiarities (e.g., facile η⁵⇄ η³shifts), have remained unknown. Standard metathetical approaches to their synthesis (e.g., with K[Ind′] + BeX₂in an ether solvent) give rise to intractable oils from which nothing identifiable can be isolated. In contrast, mechanochemical preparation, involving the solvent‐free grinding of BeBr₂and potassium indenides, leads to the production of discrete (indenyl)beryllium complexes, including [Be(C₉H₇)₂] (1) and [Be{1,3‐(SiMe₃)₂C₉H₅}Br] (2). The former displays η⁵/η¹‐coordinated ligands in the solid state, but DFT calculations indicate that an η⁵/η⁵‐conformation is less than 5 kcal mol⁻¹higher in energy. 

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5. Design of a minimal di-nickel hydrogenase peptide

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   Timm, Jennifer; Pike, Douglas H.; Mancini, Joshua A.; Tyryshkin, Alexei M.; Poudel, Saroj; Siess, Jan A.; Molinaro, Paul M.; McCann, James J.; Waldie, Kate M.; Koder, Ronald L.; et al (March 2023, Science Advances)

   Thorp, Holden (Ed.)

   Ancestral metabolic processes involve the reversible oxidation of molecular hydrogen by hydrogenase. Extant hydrogenase enzymes are complex, comprising hundreds of amino acids and multiple cofactors. We designed a 13–amino acid nickel-binding peptide capable of robustly producing molecular hydrogen from protons under a wide variety of conditions. The peptide forms a di-nickel cluster structurally analogous to a Ni-Fe cluster in [NiFe] hydrogenase and the Ni-Ni cluster in acetyl-CoA synthase, two ancient, extant proteins central to metabolism. These experimental results demonstrate that modern enzymes, despite their enormous complexity, likely evolved from simple peptide precursors on early Earth. 

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