Search Reference

1.3.7.5

Atomic-resolution structure of the phycocyanobilinferredoxin oxidoreductase I86D mutant in complex with fully protonated biliverdin

FEBS Lett.

590

3425-3434

2016

1.3.7.5

First computational step towards the understanding of the antioxidant activity of the phycocyanobilin ferredoxin oxidoreductase in complex with biliverdin IXalpha

Comput. Theoret. Chem.

1077

58-64

2016

-

1.3.7.5

A conserved histidine-aspartate pair is required for exovinyl reduction of biliverdin by a cyanobacterial phycocyanobilin:ferredoxin oxidoreductase

J. Biol. Chem.

281

3127-3136

2006

1.3.7.5

A conserved histidine-aspartate pair is required for exovinyl reduction of biliverdin by a cyanobacterial phycocyanobilin:ferredoxin oxidoreductase

J. Biol. Chem.

281

3127-3136

2006

1.3.7.5

Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli

Biochemistry

50

4890-4902

2011

1.3.7.5

Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli

Biochemistry

50

4890-4902

2011

1.3.7.5

Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion

Biochemistry

49

6070-6082

2010

1.3.7.5

Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion

Biochemistry

49

6070-6082

2010

1.3.7.5

Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates

J. Am. Chem. Soc.

126

8682-8693

2004

1.3.7.5

Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-a subunit in a heterologous host

Proc. Natl. Acad. Sci. USA

98

10560-10565

2001