EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O |
- |
Rhodobacter capsulatus |
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O |
- |
Thermosynechococcus vestitus |
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O |
ferredoxin provides a single electron to ChlL2, which in turn transfers an electron to (ChlN/ChlB)2. Hydrolysis of the two ATP molecules results in the dissociation of ChlL2 from reduced (ChlN/ChlB)2. Protochlorophyllide reduction is completed after two sequential catalytic redox cycles. Substrate recognition by (ChlN/ChlB)2 essentially involves all functional groups of the substrate, modeling of the substrate binding site of (ChlN/ChlB)2, overview. Electron transfer pathway via the various redox centers of DPOR to the substrate, overview |
Thermosynechococcus vestitus |
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O |
- |
Rhodobacter capsulatus DB176 |
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+ |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + ATP |
- |
Rhodobacter capsulatus |
protochlorophyllide + oxidized ferredoxin + ADP + phosphate |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + ATP |
- |
Auxenochlorella protothecoides |
protochlorophyllide + oxidized ferredoxin + ADP + phosphate |
- |
? |
| 1.3.7.7 | chlorophyllide a + reduced ferredoxin + ATP |
- |
Rhodobacter capsulatus DB176 |
protochlorophyllide + oxidized ferredoxin + ADP + phosphate |
- |
? |
| 1.3.7.7 | more |
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 | more |
DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer) |
Rhodobacter capsulatus |
? |
- |
? |
| 1.3.7.7 | more |
each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview |
Rhodobacter capsulatus |
? |
- |
? |
