Cargando…
A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H(2)O(2)) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme pero...
Autores principales: | Rizzolo, Kimberly, Cohen, Steven E., Weitz, Andrew C., López Muñoz, Madeline M., Hendrich, Michael P., Drennan, Catherine L., Elliott, Sean J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6405878/ https://www.ncbi.nlm.nih.gov/pubmed/30846684 http://dx.doi.org/10.1038/s41467-019-09020-4 |
Ejemplares similares
-
Supramolecular polymer formation by a de novo hemoprotein with a synthetic diheme compound
por: Isogai, Yasuhiro, et al.
Publicado: (2018) -
Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin
por: Wang, X., et al.
Publicado: (2018) -
Structural Analysis of Diheme Cytochrome c by Hydrogen–Deuterium Exchange Mass Spectrometry and Homology
Modeling
por: Zhang, Ying, et al.
Publicado: (2014) -
Occurrence and sequence of Sphaeroides Heme Protein and Diheme Cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae
por: Meyer, Terry E, et al.
Publicado: (2010) -
Structure–function characterization of the mono- and diheme forms of MhuD, a noncanonical heme oxygenase from Mycobacterium tuberculosis
por: Snyder, Samuel N., et al.
Publicado: (2021)