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Literature summary extracted from

  • Reinbothe, C.; El Bakkouri, M.; Buhr, F.; Muraki, N.; Nomata, J.; Kurisu, G.; Fujita, Y.; Reinbothe, S.
    Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction (2010), Trends Plant Sci., 15, 614-624.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.7.7 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
1.3.7.7 L-protein in the MgADP-bound form, X-ray diffraction structure determination at 1.6 A resolution Cereibacter sphaeroides

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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

EC Number Metals/Ions Comment Organism Structure
1.3.7.7 Fe2+ in [4Fe-4S] clusters Cereibacter sphaeroides
1.3.7.7 Fe2+ in [4Fe-4S] clusters Chloroflexus aurantiacus
1.3.7.7 Fe2+ in [4Fe-4S] clusters Prochlorococcus marinus
1.3.7.7 Fe2+ in [4Fe-4S] clusters Heliobacterium mobile
1.3.7.7 Fe2+ in [4Fe–4S] clusters Rhodobacter capsulatus
1.3.7.7 Fe2+ in [4Fe–4S] clusters Chlorobaculum tepidum
1.3.7.7 Mg2+ required Cereibacter sphaeroides
1.3.7.7 Mg2+ required Rhodobacter capsulatus
1.3.7.7 Mg2+ required Chloroflexus aurantiacus
1.3.7.7 Mg2+ required Prochlorococcus marinus
1.3.7.7 Mg2+ required Chlorobaculum tepidum
1.3.7.7 Mg2+ required Heliobacterium mobile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Cereibacter sphaeroides
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Rhodobacter capsulatus
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Chloroflexus aurantiacus
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Prochlorococcus marinus
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Chlorobaculum tepidum
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Heliobacterium mobile
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.7 Cereibacter sphaeroides
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
1.3.7.7 Chlorobaculum tepidum
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
1.3.7.7 Chloroflexus aurantiacus
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
1.3.7.7 Heliobacterium mobile
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
1.3.7.7 Prochlorococcus marinus
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
1.3.7.7 Rhodobacter capsulatus
-
 three subunits of DPOR, encoded by genes bchL, bchN and bchB
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.7.7 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
a
1.3.7.7 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
a
1.3.7.7 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
a
1.3.7.7 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
a
1.3.7.7 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
a
1.3.7.7 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Cereibacter sphaeroides chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Rhodobacter capsulatus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Chloroflexus aurantiacus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Chlorobaculum tepidum chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
 Heliobacterium mobile chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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 Cereibacter sphaeroides

Synonyms

EC Number Synonyms Comment Organism
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Cereibacter sphaeroides
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Rhodobacter capsulatus
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Chloroflexus aurantiacus
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Prochlorococcus marinus
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Chlorobaculum tepidum
1.3.7.7 dark-operative Pchlide oxidoreductase
-
 Heliobacterium mobile
1.3.7.7 DPOR
-
 Cereibacter sphaeroides
1.3.7.7 DPOR
-
 Rhodobacter capsulatus
1.3.7.7 DPOR
-
 Chloroflexus aurantiacus
1.3.7.7 DPOR
-
 Prochlorococcus marinus
1.3.7.7 DPOR
-
 Chlorobaculum tepidum
1.3.7.7 DPOR
-
 Heliobacterium mobile

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.7 ATP
-
 Cereibacter sphaeroides
1.3.7.7 ATP
-
 Rhodobacter capsulatus
1.3.7.7 ATP
-
 Chloroflexus aurantiacus
1.3.7.7 ATP
-
 Prochlorococcus marinus
1.3.7.7 ATP
-
 Chlorobaculum tepidum
1.3.7.7 ATP
-
 Heliobacterium mobile
1.3.7.7 Ferredoxin
-
 Cereibacter sphaeroides
1.3.7.7 Ferredoxin
-
 Rhodobacter capsulatus
1.3.7.7 Ferredoxin
-
 Chloroflexus aurantiacus
1.3.7.7 Ferredoxin
-
 Prochlorococcus marinus
1.3.7.7 Ferredoxin
-
 Chlorobaculum tepidum
1.3.7.7 Ferredoxin
-
 Heliobacterium mobile

General Information

EC Number General Information Comment Organism
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 metabolism the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g Rhodobacter capsulatus
1.3.7.7 metabolism the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g Chloroflexus aurantiacus
1.3.7.7 metabolism the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g Chlorobaculum tepidum
1.3.7.7 metabolism the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g Heliobacterium mobile
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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
1.3.7.7 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