Cargando…
Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system
Productive biomolecular recognition requires exquisite control of affinity and specificity. Accordingly, nature has devised many strategies to achieve proper binding interactions. Bacterial multicomponent monooxygenases provide a fascinating example, where a diiron hydroxylase must reversibly intera...
Autores principales: | Acheson, Justin F., Bailey, Lucas J., Elsen, Nathaniel L., Fox, Brian G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4200526/ https://www.ncbi.nlm.nih.gov/pubmed/25248368 http://dx.doi.org/10.1038/ncomms6009 |
Ejemplares similares
-
Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme
por: Adak, Sanjoy, et al.
Publicado: (2023) -
A phylogenomic profile of hemerythrins, the nonheme diiron binding respiratory proteins
por: Bailly, Xavier, et al.
Publicado: (2008) -
Structure and assembly of the diiron cofactor in the heme-oxygenase–like domain of the N-nitrosourea–producing enzyme SznF
por: McBride, Molly J., et al.
Publicado: (2021) -
Stabilization of intermediate spin states in mixed-valent diiron dichalcogenide complexes
por: Henthorn, Justin T., et al.
Publicado: (2022) -
Recent Advances in Biomolecular Recognition
por: Zhu, Qiang, et al.
Publicado: (2023)