Cargando…
Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c
Heme, an essential molecule for virtually all living organisms, acts primarily as a cofactor in a large number of proteins. However, how heme is mobilized from the site of synthesis to the locations where hemoproteins are assembled remains largely unknown in cells, especially bacterial ones. In this...
Autores principales: | Han, Sirui, Guo, Kailun, Wang, Wei, Tao, Yizhi J., Gao, Haichun |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10470608/ https://www.ncbi.nlm.nih.gov/pubmed/37462360 http://dx.doi.org/10.1128/mbio.01320-23 |
Ejemplares similares
-
NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants
por: Guo, Kailun, et al.
Publicado: (2022) -
Nitrite modulates aminoglycoside tolerance by inhibiting cytochrome heme-copper oxidase in bacteria
por: Zhang, Yongting, et al.
Publicado: (2020) -
Structural basis of membrane machines that traffick and attach heme to cytochromes
por: Huynh, Jonathan Q., et al.
Publicado: (2023) -
Heme–Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case
por: Schweitzer-Stenner, Reinhard
Publicado: (2022) -
Structural
Adaptability Facilitates Histidine Heme
Ligation in a Cytochrome P450
por: McIntosh, John A., et al.
Publicado: (2015)