| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152539 | Journal of Inorganic Biochemistry | 2017 | 8 Pages |
Abstract
The bis-Fe(IV) intermediate of the diheme enzyme MauG is a lynchpin species in the biogenesis of the tryptophan tryptophylquinone cofactor. A heterolytic OO bond cleavage reaction assisted by a distal glutamate residue is found to be critical for the formation of this high-valence intermediate.156
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Jiafeng Geng, Lu Huo, Aimin Liu,