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Literature summary extracted from

  • Kondo, T.; Nomata, J.; Fujita, Y.; Itoh, S.
    EPR study of 1Asp-3Cys ligated 4Fe-4S iron-sulfur cluster in NB-protein (BchN-BchB)2 of a dark-operative protochlorophyllide reductase complex (2011), FEBS Lett., 585, 214-218.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.7 D36C catalytically inactive Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.7 Rhodobacter capsulatus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.7 additional information although chlorophyllide c binds to the substrate-binding pocket in the NB-protein, the C17-C18 double bond on the D-ring of chlorophyllide c is not reduced by the DPOR Rhodobacter capsulatus ?
-
 ?
1.3.7.7 protochlorophyllide + oxidized ferredoxin + ADP + phosphate DPOR catalyzes the stereo-specific reduction of C17-C18 double bond on the D-ring of protochlorophyllide Rhodobacter capsulatus chlorophyllide a + reduced ferredoxin + ATP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.7.7 dark-operative Pchlide oxidoreductase
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 Rhodobacter capsulatus
1.3.7.7 dark-operative protochlorophyllide reductase
-
 Rhodobacter capsulatus
1.3.7.7 DPOR DPOR consists of two components, the L-protein and the NB-protein Rhodobacter capsulatus
1.3.7.7 light-independent Pchlide oxidoreductase
-
 Rhodobacter capsulatus
1.3.7.7 light-independent protochlorophyllide oxidoreductase
-
 Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.7 4Fe-4S-center the L-protein carries a [4Fe-4S] cluster between the protomers that is very similar to that of the nitrogenase Fe protein. The NB-protein also carries a [4Fe-4S] cluster that mediates electrons from the L-cluster to the protochlorophyllide molecule Rhodobacter capsulatus
1.3.7.7 ADP
-
 Rhodobacter capsulatus