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Literature summary for 1.3.7.7 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

Protein Variants Comment Organism
D36C catalytically inactive Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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?
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
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?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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
ADP
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Rhodobacter capsulatus