Crystallization (Comment) | Organism |
---|---|
catalytic component NB-protein, both in thePchlide-bound and Pchlide-free states, X-ray diffraction structure determination at 2.3 A and 2.8 A resolution, respectively | Rhodobacter capsulatus |
L-protein in the MgADP-bound form, X-ray diffraction structure determination at 1.6 A resolution | Cereibacter sphaeroides |
Protein Variants | Comment | Organism |
---|---|---|
D36A | site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, D36A retains only 13% of wild-type activity | Rhodobacter capsulatus |
D36C | site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, catalytically inactive mutant | Rhodobacter capsulatus |
D36S | site-directed mutagenesis, the mutant subunit B forms a complex with subunit N, indicating that Asp36 is not necessary for complex formation, catalytically inactive mutant | Rhodobacter capsulatus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in [4Fe-4S] clusters | Cereibacter sphaeroides | |
Fe2+ | in [4Fe-4S] clusters | Chloroflexus aurantiacus | |
Fe2+ | in [4Fe-4S] clusters | Prochlorococcus marinus | |
Fe2+ | in [4Fe-4S] clusters | Heliobacterium mobile | |
Fe2+ | in [4Fe4S] clusters | Rhodobacter capsulatus | |
Fe2+ | in [4Fe4S] clusters | Chlorobaculum tepidum | |
Mg2+ | required | Cereibacter sphaeroides | |
Mg2+ | required | Rhodobacter capsulatus | |
Mg2+ | required | Chloroflexus aurantiacus | |
Mg2+ | required | Prochlorococcus marinus | |
Mg2+ | required | Chlorobaculum tepidum | |
Mg2+ | required | Heliobacterium mobile |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Cereibacter sphaeroides | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Rhodobacter capsulatus | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Chloroflexus aurantiacus | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Prochlorococcus marinus | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Chlorobaculum tepidum | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | Heliobacterium mobile | - |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Chlorobaculum tepidum | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Chloroflexus aurantiacus | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Heliobacterium mobile | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Prochlorococcus marinus | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Rhodobacter capsulatus | - |
three subunits of DPOR, encoded by genes bchL, bchN and bchB | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Cereibacter sphaeroides | |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Rhodobacter capsulatus | |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Chloroflexus aurantiacus | |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Prochlorococcus marinus | |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Chlorobaculum tepidum | |
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | reaction mechanism and structure-function relationship, overview | Heliobacterium mobile |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Cereibacter sphaeroides | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Rhodobacter capsulatus | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Chloroflexus aurantiacus | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Prochlorococcus marinus | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Chlorobaculum tepidum | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? | |
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O | - |
Heliobacterium mobile | chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview | Chloroflexus aurantiacus |
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview | Prochlorococcus marinus |
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview | Chlorobaculum tepidum |
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview | Heliobacterium mobile |
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview. The NB-cluster is unique because it is coordinated by three Cys residues from BchN (BchN-Cys26, BchN-Cys51, BchN-Cys112) and one Asp residue from BchB (BchB-Asp36) | Rhodobacter capsulatus |
More | DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchNBchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview | Cereibacter sphaeroides |
Synonyms | Comment | Organism |
---|---|---|
dark-operative Pchlide oxidoreductase | - |
Cereibacter sphaeroides |
dark-operative Pchlide oxidoreductase | - |
Rhodobacter capsulatus |
dark-operative Pchlide oxidoreductase | - |
Chloroflexus aurantiacus |
dark-operative Pchlide oxidoreductase | - |
Prochlorococcus marinus |
dark-operative Pchlide oxidoreductase | - |
Chlorobaculum tepidum |
dark-operative Pchlide oxidoreductase | - |
Heliobacterium mobile |
DPOR | - |
Cereibacter sphaeroides |
DPOR | - |
Rhodobacter capsulatus |
DPOR | - |
Chloroflexus aurantiacus |
DPOR | - |
Prochlorococcus marinus |
DPOR | - |
Chlorobaculum tepidum |
DPOR | - |
Heliobacterium mobile |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Cereibacter sphaeroides | |
ATP | - |
Rhodobacter capsulatus | |
ATP | - |
Chloroflexus aurantiacus | |
ATP | - |
Prochlorococcus marinus | |
ATP | - |
Chlorobaculum tepidum | |
ATP | - |
Heliobacterium mobile | |
Ferredoxin | - |
Cereibacter sphaeroides | |
Ferredoxin | - |
Rhodobacter capsulatus | |
Ferredoxin | - |
Chloroflexus aurantiacus | |
Ferredoxin | - |
Prochlorococcus marinus | |
Ferredoxin | - |
Chlorobaculum tepidum | |
Ferredoxin | - |
Heliobacterium mobile |
General Information | Comment | Organism |
---|---|---|
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview | Rhodobacter capsulatus |
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview | Chloroflexus aurantiacus |
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview | Prochlorococcus marinus |
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview | Chlorobaculum tepidum |
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, ooverview | Heliobacterium mobile |
evolution | cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, overview | Cereibacter sphaeroides |
metabolism | the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g | Rhodobacter capsulatus |
metabolism | the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g | Chloroflexus aurantiacus |
metabolism | the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g | Chlorobaculum tepidum |
metabolism | the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g | Heliobacterium mobile |
additional information | some purple bacteria contain Bchl b, and heliobacteria such as Heliobacillus mobilis contain Bchl g, as compared to Chl a and Chl b of higher plants | Heliobacterium mobile |
additional information | the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants | Chloroflexus aurantiacus |
additional information | the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants | Chlorobaculum tepidum |
additional information | the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants. Residue Asp36 is not necessary for enzyme complex formation but for enzyme activity. Subunit BchB possesses a unique C-terminal region consisting of approximately 100 amino acid residues (Phe422-Arg525), which is probably important for protochlorophyllide reduction | Rhodobacter capsulatus |