Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal-Dependent Formate Dehydrogenase.

Biological carbon dioxide (CO ) reduction is an important step by which organisms form valuable energy-richer molecules required for further metabolic processes. The Mo-dependent formate dehydrogenase (FDH) from Rhodobacter capsulatus catalyzes reversible formate oxidation to CO at a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor. To elucidate potential substrate binding sites relevant for the mechanism, we studied herein the interaction with the inhibitory molecules azide and cyanate, which are isoelectronic to CO and charged as formate.

The role of electron correlations in the binding properties of Ca, Sr, and Ba.

In order to apply wavefunction-based correlation methods to solids it is necessary to have reliable Hartree-Fock (HF) results for the infinite system of interest. We performed Hartree-Fock calculations for the group 2 heavy alkali-earth metals Ca, Sr, and Ba. For that, basis sets of valence-double-ζ quality have been optimized for the periodic systems.