The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions
Here we report the effect of molecular crowding on long-range protein electron transfer (ET) and disentangle the specific responses of the redox site and the protein milieu. To this end, we studied two different one-electron redox proteins that share the cupredoxin fold but differ in the metal cente...
Guardado en:
| Publicado: |
2019
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00134686_v294_n_p117_Zitare http://hdl.handle.net/20.500.12110/paper_00134686_v294_n_p117_Zitare |
| Aporte de: |
Ejemplares similares
-
The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions
por: Zitare, U.A., et al. -
Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis
Publicado: (2018) -
Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis
por: Espinoza-Cara, A., et al. -
Computer simulation and SERR detection of cytochrome c dynamics at SAM-coated electrodes
por: Martí, Marcelo Adrián, et al.
Publicado: (2009) -
Computer simulation and SERR detection of cytochrome c dynamics at SAM-coated electrodes
por: Paggi, D.A., et al.