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Literature summary for 1.8.7.2 extracted from

  • Walters, E.M.; Garcia-Serres, R.; Naik, S.G.; Bourquin, F.; Glauser, D.A.; Schurmann, P.; Huynh, B.H.; Johnson, M.K.
    Role of histidine-86 in the catalytic mechanism of ferredoxin:thioredoxin reductase (2009), Biochemistry, 48, 1016-1024.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Organism UniProt Comment Textmining
Synechocystis sp.
-
PCC 6803
-