Information on EC 1.3.7.7 - ferredoxin:protochlorophyllide reductase (ATP-dependent) and Organism(s) Prochlorococcus marinus and UniProt Accession Q7VD39
for references in articles please use BRENDA:EC1.3.7.7
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Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
The taxonomic range for the selected organisms is: Prochlorococcus marinus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
the homodimeric ChlL2 subunit carrying a [4Fe-4S] cluster transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, which also possesses a redox active [4Fe-4S] cluster
dependent on, the homodimeric subunit ChlL2 functions as an ATP-dependent switch protein, triggering the transient interaction of ChlL2 and heterotetrameric catalytic subunit (ChlN/ChlB)2
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
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
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
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
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
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
the homodimeric subunit ChlL2 transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, transfer of a single electron from the [4Fe-4S] cluster of ChlL2 onto a second [4Fe-4S] cluster located on (ChlN/ChlB)2
transient protein-protein interaction of ChlL2 and (ChlN/ChlB)2 is essential for the ATP-dependent electron transfer processes catalyzed by DPOR. Efficient octameric (ChlN/ChlB)2(ChlL2)2 enzyme complex formation required the presence of protochlorophyllide. Complete ATP hydrolysis is a prerequisite for intersubunit electron transfer
(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
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the ternary DPOR enzyme holocomplex comprising subunits ChlN, ChlB, and ChlL is trapped as an octameric (ChlN/ChlB)2(ChlL2)2 complex after incubation with the nonhydrolyzable ATP analogues adenosine 5'-(gamma-thio)triphosphate, adenosine 5'-(beta,gamma-imido)triphosphate, or MgADP in combination with AlF4-, complex structure, overview. A mutant ChlL2 protein, with a deleted Leu153 in the switch II region also allows for the formation of a stable octameric complex
Broecker, M.J.; Waetzlich, D.; Saggu, M.; Lendzian, F.; Moser, J.; Jahn, D.
Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase