Dimitri Niks

TL;DR: Recent solution studies of the Salmonella typhimurium alpha2beta2 complex coupled with X-ray crystal-structure determinations of complexes with substrates, intermediates and substrate analogs have driven important breakthroughs concerning the identification of the linkages between the bi-enzyme complex structure, catalysis at the alpha- and beta-active sites, and the allosteric regulation of substrate channeling.

TL;DR: The mARC-1/MOSC-1 and hmARC-2 genes were found to be monomeric in their active forms, which is in contrast to all other eukaryotic molybdenum enzymes that act as homo- or heterodimers.

TL;DR: A synergistic approach was adopted to determine the chemically rich crystal structure of the indoline quinonoid intermediate in the pyridoxal-5'-phosphate-dependent enzyme tryptophan synthase under conditions of active catalysis, suggesting the importance of an equilibrium between tautomeric forms of the substrate.

TL;DR: Recombinant expression of hmARC-1 and hm ARC-2 proteins in Escherichia coli reveals that both proteins are monomeric in their active forms, which is in contrast to all other eukaryotic molybdenum enzymes that act as homo- or heterodimers.

TL;DR: All molybdenum- and tungsten-containing formate dehydrogenases and related enzymes likely operate via a simple hydride transfer mechanism and are effective in catalyzing the reversible interconversion of CO2 and formate under the appropriate experimental conditions.