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malfunction
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a strain lacking DPOR contains about 25% of the wild-type level of photosystems PSII and PSI when cultivated under light-activated heterotrophic growth conditions. Deletion of the chlL gene abolishes activity of the DPOR enzyme. Absence of the chlL gene causes a further 20% decrease in Chl content and therefore the resulting (pCER:por)/Dpor/DchlL strain termed SynPORreg reaches only 60-70% of Chl content present in wild-type
evolution
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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
evolution
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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
evolution
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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
evolution
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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
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
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
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
evolution
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the enzyme is involved in the biosynthesis of chlorophylls and bacteriochlorophylls in gymnosperm, ferns, algae, and photosynthetic bacteria
metabolism
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chlorophyll biosynthesis is catalyzed by two multi subunit enzymes; a light-dependent and a light-independent protochlorophyllide oxidoreductase
metabolism
protochlorophyllide reduction is a key regulatory step in Chl biosynthesis
metabolism
protochlorophyllide reduction is a key regulatory step in Chl biosynthesis
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
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the three-subunit enzyme dubbed DPOR operates in the synthesis of Bchls a, b, and g
metabolism
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two independent enzymes catalyze the reduction of protochlorophyllide to chlorophyllide, which is the penultimate step in chlorophyll biosynthesis. One is light-dependent NADPH:protochlorophyllide oxidoreductase and the second type is dark-operative protochlorophyllide oxidoreductase
physiological function
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DPOR is a determinant enzyme for greening ability in the dark
physiological function
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DPOR performs reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a in a light-independent, dark-operative way of action
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
DPOR plays a key role in the ability to synthesize chlorophyll in darkness
physiological function
light-independent protochlorophyllide reductase is required for protochlorophyllide reduction in the dark
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
physiological function
the expression of NADPH:protochlorophyllide oxidoreductase A (PorA), PorB, and PorC, which catalyze a key step in chlorophyll biosynthesis, is increased in the BRM mutants, defective in a SWI2/SNF2 chromatin-remodeling ATPase
physiological function
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DPOR performs reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a in a light-independent, dark-operative way of action
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additional information
dark-grown seedlings of Pinus mugo accumulate chlorophyll and its precursor protochlorophyllide
additional information
dark-grown seedlings of Pinus sylvestris accumulate chlorophyll and its precursor protochlorophyllide
additional information
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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
additional information
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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
additional information
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the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants
additional information
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the organism contains another type of Chl, bacteriochlorophyll (Bchl) a, as compared to Chl a and Chl b of higher plants
additional information
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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
additional information
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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
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
additional information
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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