Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG

@article{Jensen2012GeometricAE,
  title={Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG},
  author={Lyndal M. R. Jensen and Yergalem T. Meharenna and Victor L Davidson and Thomas L Poulos and Britt Hedman and Carrie M Wilmot and Ritimukta Sarangi},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2012},
  volume={17},
  pages={1241-1255}
}
Biosynthesis of the tryptophan tryptophylquinone (TTQ) cofactor activates the enzyme methylamine dehydrogenase. The diheme enzyme MauG catalyzes O-atom insertion and cross-linking of two Trp residues to complete TTQ synthesis. Solution optical and Mössbauer spectroscopic studies have indicated that the reactive form of MauG during turnover is an unusual bisFe(IV) intermediate, which has been formulated as a His-ligated ferryl heme [Fe(IV)=O] (heme A), and an Fe(IV) heme with an atypical His/Tyr… CONTINUE READING

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