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Literature summary for 1.8.7.2 extracted from

  • Xu, X.; Schurmann, P.; Chung, J.S.; Hass, M.A.; Kim, S.K.; Hirasawa, M.; Tripathy, J.N.; Knaff, D.B.; Ubbink, M.
    Ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy (2009), J. Am. Chem. Soc., 131, 17576-17582.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
paramagnetic NMR spectroscopy study on the ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin. FTR uses distinct sites to bind ferredoxin and thioredoxin simultaneously to form a noncovalent ternary complex. Either a modest or major rotational movement of thioredoxin must take place when the noncovalent binary complex proceeds to the covalent complex Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
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PCC 6803
-