BRENDA - Enzyme Database show

EPR study of 1Asp-3Cys ligated 4Fe-4S iron-sulfur cluster in NB-protein (BchN-BchB)2 of a dark-operative protochlorophyllide reductase complex

Kondo, T.; Nomata, J.; Fujita, Y.; Itoh, S.; FEBS Lett. 585, 214-218 (2011)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.3.7.7
D36C
catalytically inactive
Rhodobacter capsulatus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.3.7.7
Rhodobacter capsulatus
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
712026
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
712026
Rhodobacter capsulatus
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.3.7.7
D36C
catalytically inactive
Rhodobacter capsulatus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
712026
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
712026
Rhodobacter capsulatus
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?