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Literature summary for 1.3.7.5 extracted from

  • Ceron-Carrasco, J.; Jacquemin, D.; Laurent, A.
    First computational step towards the understanding of the antioxidant activity of the phycocyanobilin ferredoxin oxidoreductase in complex with biliverdin IXalpha (2016), Comput. Theoret. Chem., 1077, 58-64 .
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
quantum mechanical approaches show that the propensity of biliverdin to bind PcyA is dominated by electrostatic interactions, especially related to residues Arg149 and Lys221, while H-bonds are formed with His88 and Ser114. The antioxidant activity is dependent on the intramolecular noncovalent bond interactions. The surrounding residues increase the antioxidant character of biliverdin by 2 eV Synechocystis sp. PCC 6803

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 Q55891
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