Cargando…
A conserved arginine residue is critical for stabilizing the N2 FeS cluster in mitochondrial complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase), the first enzyme of the electron-transport chain, captures the free energy released by NADH oxidation and ubiquinone reduction to translocate protons across an energy-transducing membrane and drive ATP synthesis during oxidative phosphorylation...
Autores principales: | Hameedi, Mikhail A., Grba, Daniel N., Richardson, Katherine H., Jones, Andrew J.Y., Song, Wei, Roessler, Maxie M., Wright, John J., Hirst, Judy |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8042128/ https://www.ncbi.nlm.nih.gov/pubmed/33640456 http://dx.doi.org/10.1016/j.jbc.2021.100474 |
Ejemplares similares
-
A broad survey reveals substitution tolerance of residues ligating FeS clusters in [NiFe] hydrogenase
por: Yonemoto, Isaac T, et al.
Publicado: (2014) -
Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I()
por: Hirst, Judy, et al.
Publicado: (2016) -
Using a chimeric respiratory chain and EPR spectroscopy to determine the origin of semiquinone species previously assigned to mitochondrial complex I
por: Wright, John J., et al.
Publicado: (2020) -
Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer
por: Petrenko, Alexander, et al.
Publicado: (2017) -
Parasites FeS Up: Iron-Sulfur Cluster Biogenesis in Eukaryotic Pathogens
por: Dellibovi-Ragheb, Teegan A., et al.
Publicado: (2013)