Protein Variants | Comment | Organism |
---|---|---|
H86Y | spectroscopic and redox characterization of the [Fe4-S4] center in H86Y ferredoxin:thoredoxin reductase in the accessible redox states of both the native and N-ethylmaleimide-modified forms. H86 is required for formation of the partially valence-localized [Fe4-S4]2+ cluster that is the hallmark of two-electron-reduced intermediate. Results indicate a functional role for H86 in protonation/deprotonation of the cluster-interacting thiol and anchoring the cluster interacting thiol in close proximity to the cluster in the two-electron-reduced intermediate | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | - |
PCC 6803 | - |