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Gene Review:

slr0116 - phycocyanobilin:ferredoxin oxidoreductase

Synechocystis sp. PCC 6803

This record was discontinued.

Hagiwara, Y. et al., Hagiwara, Y. et al.

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Disease relevance of slr0116

Phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the sequential reduction of the vinyl group of the D-ring and the A-ring of biliverdin IXalpha (BV) using ferredoxin to produce phycocyanobilin, a pigment used for light-harvesting and light-sensing in red algae and cyanobacteria [1].

High impact information on slr0116

Phycocyanobilin:ferredoxin oxidoreductase (PcyA), one such FDBR, is a new class of radical enzymes that require neither cofactors nor metals and serially reduces the vinyl group of the D-ring and A-ring of BV using four electrons from ferredoxin to produce phycocyanobilin, one of the phytobilins [2].
Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin [2].

References

Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form. Hagiwara, Y., Sugishima, M., Takahashi, Y., Fukuyama, K. FEBS Lett. (2006) [Pubmed]
Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin. Hagiwara, Y., Sugishima, M., Takahashi, Y., Fukuyama, K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]

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