The three-his triad in Dke1: comparisons to the classical facial triad.

ABSTRACT: The oxygen activating mononuclear non-heme ferrous enzymes catalyze a diverse range of chemistry yet typically maintain a common structural motif: two histidines and a carboxylate coordinating the iron center in a facial triad. A new Fe(II) coordinating triad has been observed in two enzymes, diketone-cleaving dioxygenase, Dke1, and cysteine dioxygenase (CDO), and is composed of three histidine residues. The effect of this three-His motif in Dke1 on the geometric and electronic structure of the Fe(II) center is explored via a combination of absorption, CD, MCD, and VTVH MCD spectroscopies and DFT calculations. This geometric and electronic structure of the three-His triad is compared to that of the classical (2-His-1-carboxylate) facial triad in the alpha-ketoglutarate (alphaKG)-dependent

SUBMITTER: Diebold AR 

PROVIDER: S-EPMC2924660 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature