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Biological carbon dioxide (CO2) 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 CO2 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 CO2 and charged as formate. We employed infrared (IR) spectroscopy in combination with density functional theory (DFT) and inhibition kinetics. One distinct inhibitory molecule was found to bind to either a non-competitive or a competitive binding site in the secondary coordination sphere of the active site. Site-directed mutagenesis of key amino acid residues in the vicinity of the bis-MGD cofactor revealed changes in both non-competitive and competitive binding, whereby the inhibitor is in case of the latter interaction presumably bound between the cofactor and the adjacent Arg587.
The oxygen on Ag(111) system has been investigated with Auger electron-photoelectron coincidence spectroscopy (APECS).
The coincidence spectra between O 1s core level photoelectrons and O KLL Auger electrons have been studied together with Ag(3)d/AgM4,5NN coincidences.
We also describe the electron-electron coincidence spectrometer setup, CoESCA, consisting of two angle resolved time-of-flight spectrometers at a synchrotron light source.
Contributions from molecular oxygen and chemisorbed oxygen are assigned using the coincidence data, conclusions are drawn primarily from the O 1s/O KLL data.
The data acquisition and treatment procedure are also outlined.
The chemisorbed oxygen species observed are relevant for the catalytic ethylene oxidation.