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Literature summary for 1.3.7.7 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)

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

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

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 [4Fe–4S] clusters Rhodobacter capsulatus
Fe2+ in [4Fe–4S] 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/ Products (Substrates)

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

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

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 and Products (Substrate)

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

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 BchN–BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview Cereibacter sphaeroides

Synonyms

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

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

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