Cargando…
Splitting of the O–O bond at the heme-copper catalytic site of respiratory oxidases
Heme-copper oxidases catalyze the four-electron reduction of O(2) to H(2)O at a catalytic site that is composed of a heme group, a copper ion (Cu(B)), and a tyrosine residue. Results from earlier experimental studies have shown that the O–O bond is cleaved simultaneously with electron transfer from...
Autores principales: | Poiana, Federica, von Ballmoos, Christoph, Gonska, Nathalie, Blomberg, Margareta R. A., Ädelroth, Pia, Brzezinski, Peter |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5473675/ https://www.ncbi.nlm.nih.gov/pubmed/28630929 http://dx.doi.org/10.1126/sciadv.1700279 |
Ejemplares similares
-
Regulation of cytochrome c oxidase activity by modulation of the catalytic site
por: Schäfer, Jacob, et al.
Publicado: (2018) -
Lipid-mediated Protein-protein Interactions Modulate Respiration-driven ATP
Synthesis
por: Nilsson, Tobias, et al.
Publicado: (2016) -
The proton pumping bo oxidase from Vitreoscilla
por: Graf, Simone, et al.
Publicado: (2019) -
Rapid Electron Transfer within the III-IV Supercomplex in Corynebacterium glutamicum
por: Graf, Simone, et al.
Publicado: (2016) -
NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP
por: Zhou, Shu, et al.
Publicado: (2021)