Cargando…
Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochrome bc(1) perturbs heme b(H) redox potential and spin state
Hemes are common elements of biological redox cofactor chains involved in rapid electron transfer. While the redox properties of hemes and the stability of the spin state are recognized as key determinants of their function, understanding the molecular basis of control of these properties is challen...
Autores principales: | Kuleta, Patryk, Lasham, Jonathan, Sarewicz, Marcin, Ekiert, Iwona, Sharma, Vivek, Ekiert, Robert, Osyczka, Artur |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8379992/ https://www.ncbi.nlm.nih.gov/pubmed/34389670 http://dx.doi.org/10.1073/pnas.2026169118 |
Ejemplares similares
-
Mitochondrial Disease-related Mutation G167P in Cytochrome b of Rhodobacter capsulatus Cytochrome bc(1) (S151P in Human) Affects the Equilibrium Distribution of [2Fe-2S] Cluster and Generation of Superoxide
por: Borek, Arkadiusz, et al.
Publicado: (2015) -
Identification of hydrogen bonding network for proton transfer at the quinol oxidation site of Rhodobacter capsulatus cytochrome bc(1)
por: Borek, Arkadiusz, et al.
Publicado: (2023) -
Mitochondrial disease-related mutations at the cytochrome b-iron–sulfur protein (ISP) interface: Molecular effects on the large-scale motion of ISP and superoxide generation studied in Rhodobacter capsulatus cytochrome bc(1)()
por: Ekiert, Robert, et al.
Publicado: (2016) -
Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc(1) function in vivo
por: Ekiert, Robert, et al.
Publicado: (2014) -
Identifying involvement of Lys251/Asp252 pair in electron transfer and associated proton transfer at the quinone reduction site of Rhodobacter capsulatus cytochrome bc(1)
por: Kuleta, Patryk, et al.
Publicado: (2016)