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Literature summary extracted from

  • Moser, J.; Lange, C.; Krausze, J.; Rebelein, J.; Schubert, W.D.; Ribbe, M.W.; Heinz, D.W.; Jahn, D.
    Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex (2013), Proc. Natl. Acad. Sci. USA, 110, 2094-2098.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.33 the X-ray crystallographic structure of the substrate-bound, ADP-aluminium fluoride-stabilized (ADP-AlF3-stabilized) transition state complex between the DPOR components L2 and (NB)2 from the marine cyanobacterium Prochlorococcus marinus is reported Prochlorococcus marinus
1.3.7.7 substrate-bound, ADP-aluminium fluoride-stabilized transition state complex between the DPOR components L2 and (NB)2, sitting drops by vapor diffusion, mixing of 0.001 ml of protein solution containing 7.5 mg/ml protein in 100 mM HEPES/NaOH, pH 7.5, 150 mM NaCl, 10 mM MgCl2, 50 mM NaF, and 2 mM AlCl3,with 0.001 ml of reservoir solution containing 0.1 M KCl, 0.1 M Tris, pH 8.5, and 3% wt/v PEG 6000, 17°C, X-ray diffraction structure determination and analysis at 2.1 A resolution Prochlorococcus marinus

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.33 H394A mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring Prochlorococcus marinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.7.7 Fe2+ two redox-active [4Fe-4S] clusters, both [4Fe-4S] clusters are centered around the extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from subunit N and one aspartate residue from subunit B Prochlorococcus marinus
1.3.7.7 Mg2+ required Prochlorococcus marinus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.33 360000
-
-
 Prochlorococcus marinus

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 Prochlorococcus marinus
-
 chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Prochlorococcus marinus Q7VD39
-
-
1.3.7.7 Prochlorococcus marinus Q7VD39
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.7 purification by immobilization of GST-tagged subunit L2 on glutathione resin, complex formation with purified subunits NB, and proteolytical cleavage Prochlorococcus marinus

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 dynamic switch mechanism of DPOR, catalytic mechanism and structure-function analysis, detailed overview Prochlorococcus marinus
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
-
 Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O DPOR catalyzes the formation of chlorophyllide a through ATP-dependent, stereospecific reduction of the C-17=C-18 double bond of Pchlide ring D Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.33 octamer heterooctameric complex: subunits N and B are structurally homologous, generating a pseudo-2fold symmetry axis that is colinear with the molecular twofold axis of L2. Both [4Fe-4S] clusters are centered around this extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from N and one aspartate residue from B Prochlorococcus marinus
1.3.7.7 octamer (L2)2(NB)2 enzyme complex with perfect symmetry. Subunits L2 and NifH2 both contain a subunit-bridging [4Fe-4S] cluster, whereas the [4Fe-4S] cluster at the N/B subunit interface of (NB)2 is located in an analogous position as the [8Fe-7S] P-cluster at the NifD/NifK subunit interface of (NifDK)2 Prochlorococcus marinus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 dark-operative protochlorophyllide oxidoreductase
-
 Prochlorococcus marinus
1.3.1.33 DPOR
-
 Prochlorococcus marinus
1.3.7.7 dark-operative protochlorophyllide oxidoreductase
-
 Prochlorococcus marinus
1.3.7.7 DPOR
-
 Prochlorococcus marinus
1.3.7.7 protochlorophyllide oxidoreductase complex
-
 Prochlorococcus marinus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.7 ATP
-
 Prochlorococcus marinus
1.3.7.7 Ferredoxin
-
 Prochlorococcus marinus

General Information

EC Number General Information Comment Organism
1.3.7.7 evolution protein-protein interaction surfaces for transition state complexes of DPOR and nitrogenase, using PDB ID code 1M34, analysis of catalytic differences and similarities between DPOR and nitrogenase, overview Prochlorococcus marinus
1.3.7.7 additional information upon complex formation, substantial ATP-dependent conformational rearrangements of L2 trigger the protein-protein interactions with (NB)2 as well as the electron transduction via redox-active [4Fe-4S] clusters, dynamic interplay between L2 and (NB)2. Asp155 is responsible for positioning and/or activating a specific water molecule for the subsequent ATP hydrolysis, whereas Lys37 of the P-loop possibly assists the release of gamma-phosphate upon ATP hydrolysis Prochlorococcus marinus
1.3.7.7 physiological function during chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energytransduction processes of photosynthesis Prochlorococcus marinus