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Literature summary for 1.18.1.2 extracted from

  • Gomez-Lojero, C.; Perez-Gomez, B.; Shen, G.; Schluchter, W.M.; Bryant, D.A.
    Interaction of ferredoxin:NADP+ oxidoreductase with phycobilisomes and phycobilisome substructures of the cyanobacterium Synechococcus sp. strain PCC 7002 (2003), Biochemistry, 42, 13800-13811.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
phycobilisome enzyme is bound to phycobilisomes via the N-terminal enzyme domain to the peripheral rods of the phycobilisome, average value of 1.3 molecules of enzyme per phycobilisome, structure modeling, interaction analysis Synechococcus sp. 30089
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + NADP+ Synechococcus sp. generation of NADPH oxidized ferredoxin + NADPH
-
?

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
strain PCC 7002, gene petH
-

Purification (Commentary)

Purification (Comment) Organism
preparation of phycobilisomes by sucrose density gradient centrifugation Synechococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme binds to phycocyanin hexamers Synechococcus sp. ?
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol diaphorase activity Synechococcus sp. NADP+ + reduced 2,6-dichlorophenolindophenol
-
?
reduced ferredoxin + NADP+
-
Synechococcus sp. oxidized ferredoxin + NADPH
-
?
reduced ferredoxin + NADP+ generation of NADPH Synechococcus sp. oxidized ferredoxin + NADPH
-
?

Subunits

Subunits Comment Organism
More 3-domain-structure Synechococcus sp.

Synonyms

Synonyms Comment Organism
FNR
-
Synechococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
diaphorase activity assay at Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
Synechococcus sp.
NADP+
-
Synechococcus sp.