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Literature summary for 1.3.7.5 extracted from

  • Iijima, E.; Gleeson, M.; Unno, M.; Mori, S.
    QM/MM investigation for protonation states in a bilin reductase PcyA-biliverdin IXalpha complex (2018), ChemPhysChem, 19, 1809-1813 .
    View publication on PubMed
Search for more literature for 1.3.7.5

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in cofactor ferredoxin Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biliverdin IXalpha + 4 reduced ferredoxin Synechocystis sp. PCC 6803
-
 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 Q55891
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biliverdin IXalpha + 4 reduced ferredoxin
-
 Synechocystis sp. PCC 6803 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?
biliverdin IXalpha + 4 reduced ferredoxin via reaction intermediate 181,182-difydrobiliverdin (18EtBV) Synechocystis sp. PCC 6803 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
bilin reductase
-
 Synechocystis sp. PCC 6803
PcyA
-
 Synechocystis sp. PCC 6803
phycocyanobilin:ferredoxin oxidoreductase
-
 Synechocystis sp. PCC 6803

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Synechocystis sp. PCC 6803

General Information

General Information Comment Organism
evolution phycocyanobilin:ferredoxin oxidoreductase (PcyA) is a member of the ferredoxin-dependent bilin reductase (FDBR) family Synechocystis sp. PCC 6803
additional information quantum mechanical/molecular mechanical (QM/MM) studies investigating the most probable protonation states of active site amino acids and bound substrate based on a recently reported neutron diffraction structure of phycocyanobilin: ferredoxin oxidoreductase (PcyA), overview. The hydronium ion (H3O+) is energetically unfavorable, preferentially protonating the neighboring His88 residue and that the C-ring of BV is not protonated. The hydronium ion forms hydrogen bonds with His88 (Nepsilon), His74 (Ndelta) and Leu243 (Carbonyl O) residues Synechocystis sp. PCC 6803
physiological function phycocyanobilin (PCB) is synthesized by phycocyanobilin:ferredoxin oxidoreductase (PcyA). The reaction of PcyA starts from biliverdin IXalpha (BV), which is a product of the heme oxygenase-mediated cleavage of the heme macrocycle, to PCB through four-electron reduction Synechocystis sp. PCC 6803