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Literature summary for 1.3.7.7 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)

Crystallization (Comment) Organism
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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Mg2+ required Prochlorococcus marinus

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

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus Q7VD39
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-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
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Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
?
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

Subunits Comment Organism
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

Synonyms Comment Organism
dark-operative protochlorophyllide oxidoreductase
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Prochlorococcus marinus
DPOR
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Prochlorococcus marinus
protochlorophyllide oxidoreductase complex
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Prochlorococcus marinus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Prochlorococcus marinus
Ferredoxin
-
Prochlorococcus marinus

General Information

General Information Comment Organism
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
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
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