A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Möss...
Guardado en:
Autores principales: | Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/43e89e2788134c44bc04e90574efd768 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
por: Andrew J. Hayes, et al.
Publicado: (2021) -
Interactions between Melanin Enzymes and Their Atypical Recruitment to the Secretory Pathway by Palmitoylation
por: Srijana Upadhyay, et al.
Publicado: (2016) -
Primary Cutaneous Atypical Spindle Cell Lipomatous Tumor
por: Madeline S. Tchack, et al.
Publicado: (2021) -
The Burkholderia pseudomallei intracellular ‘TRANSITome’
por: Yun Heacock-Kang, et al.
Publicado: (2021) -
Deciphering minimal antigenic epitopes associated with Burkholderia pseudomallei and Burkholderia mallei lipopolysaccharide O-antigens
por: Marielle Tamigney Kenfack, et al.
Publicado: (2017)