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Literature summary for 1.14.11.17 extracted from

  • Sinnecker, S.; Svensen, N.; Barr, E.W.; Ye, S.; Bollinger, J.M.; Neese, F.; Krebs, C.
    Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant (2007), J. Am. Chem. Soc., 129, 6168-6179.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
density functional theory calculations based on a series of models for the key intermediate with the Fe(IV) ion coordinated by the expected two imidazoles from His99 and His255, two carboxylates, succinate and Asp101, and oxo ligands. Calculated parameters of distorted octahedral models for the intermediate, in which one of the carboxylates serves as a monodentate ligand and the other as a bidentate ligand, and a trigonal bipyramidal model, in which both carboxylates serve as monodentate ligands, agree well with the experimental parameters Escherichia coli

Protein Variants

Protein Variants Comment Organism
H99A replacement of the residue that contributes the imidazole ligand cis to the oxo group. Density functional theory calculations show that the imidazole is replaced by a water ligand Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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