Načítá se...
Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG
The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a bis-Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) w...
Uloženo v:
| Hlavní autoři: | , , , |
|---|---|
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2013
|
| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3683780/ https://ncbi.nlm.nih.gov/pubmed/23720312 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1301544110 |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!
|