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1 nsistent with their inability to photoreduce protochlorophyllide.
2 ly regulated by ERFVIIs, thereby suppressing protochlorophyllide.
3 n the formation of 5-aminolevulinic acid and protochlorophyllide.
4 IX), Mg-proto, Mg-proto MME and 3,8-divinyl protochlorophyllide a (DV-Pchlide) levels, but this was
5 t cells secrete large amounts of 3,8-divinyl-protochlorophyllide a into the growth medium and have a
7 approximately 50% identity with Rieske-type protochlorophyllide a oxygenases (PTC52) from higher pla
11 fluorescence as result of elevated levels of protochlorophyllide and four red fluorescent in the dark
12 on protein, is required for the synthesis of protochlorophyllide and therefore is a candidate subunit
13 wn plants led to the reduced accumulation of protochlorophyllide and transcripts for the two committe
14 vels of the phototoxic chlorophyll precursor protochlorophyllide are influenced by sensing of atmosph
15 n the POR active site that are important for protochlorophyllide binding, photosensitization and phot
16 e site facilitates light-driven reduction of protochlorophyllide by localized hydride transfer from N
18 isomer of the substrate [C8-ethyl-C13(2)-(R)-protochlorophyllide] demonstrate that the enzyme photoac
19 his mutant also synthesized small amounts of protochlorophyllide dihydrogeranylgeraniol ester (protoc
20 e reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls
21 es reduction of the C17 = C18 double bond in protochlorophyllide during the dark chlorophyll biosynth
22 ltitudinal clines for steady-state levels of protochlorophyllide, expression of inactivation complex
23 ric O2 levels, AcsFI synthesizes 3,8-divinyl protochlorophyllide from Mg-protoporphyrin IX monomethyl
26 orphyrin monomethylester and contain reduced protochlorophyllide levels and a reduced content of CHL2
27 ) were grown in darkness, the phycobilin and protochlorophyllide levels decreased upon deletion of sc
28 ctural models and simulations of the ternary protochlorophyllide-NADPH-POR complex identify multiple
29 shots of the nitrogenase-like dark-operative protochlorophyllide oxidoreductase (DPOR) during substra
31 green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase (DPOR), a nitrogenase
33 d accumulation of the light-dependent enzyme protochlorophyllide oxidoreductase (LPOR) and a delay in
39 ing skotomorphogenesis in angiosperms, NADPH:protochlorophyllide oxidoreductase (POR) forms an aggreg
40 reduced transcriptional activity of the two protochlorophyllide oxidoreductase (POR) genes involved
41 with highly purified, recombinant pea NADPH:protochlorophyllide oxidoreductase (POR) heterologously
44 hat has no prolamellar body (PLB) and normal PROTOCHLOROPHYLLIDE OXIDOREDUCTASE (POR) levels, was use
45 he gene coding for the light-dependent NADPH:protochlorophyllide oxidoreductase (POR) was interrupted
47 discrete set of genes in the dark, including protochlorophyllide oxidoreductase (POR), ferrochelatase
49 LATED1 (DET1), to transcriptionally regulate PROTOCHLOROPHYLLIDE OXIDOREDUCTASE (POR), PHYTOCHROME IN
55 e light-dependent step is catalysed by NADPH:protochlorophyllide oxidoreductase (POR, EC.1.6.99.1), w
58 light-adapted plants and catalyzed by NADPH:protochlorophyllide oxidoreductase B (PORb) has been ana
59 yll biosynthesis, the light-activated enzyme protochlorophyllide oxidoreductase catalyzes trans addit
61 ably led to a significant reduction in NADPH-protochlorophyllide oxidoreductase in the yellow sectors
64 catalytic cycle of the light-driven enzyme, protochlorophyllide oxidoreductase, have been investigat
67 and porB) encoding the light-dependent NADPH:protochlorophyllide oxidoreductases (PORs) in loblolly p
68 tosynthetic competence through the action of protochlorophyllide oxidoreductases (PORs) that convert
69 small amounts of two unusual tetrapyrroles, protochlorophyllide (PChlide) b and pheophorbide (pheide
71 ll synthesis, the light-induced reduction of protochlorophyllide (PChlide) into chlorophyllide (Chlid
72 e reductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) into chlorophyllide (Chlid
73 ) catalyzes the light-dependent reduction of protochlorophyllide (Pchlide) into chlorophyllide in the
75 forms an aggregate of photolabile NADPH-POR-protochlorophyllide (Pchlide) ternary complexes localize
76 doreductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
77 chlorophyll biosynthesis is the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
78 doreductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
79 oreductase (POR, EC.1.6.99.1), which reduces protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
80 POR) catalyzes the light-driven reduction of protochlorophyllide (Pchlide) to chlorophyllide, providi
81 f hydrogen across the C17-C18 double bond of protochlorophyllide (Pchlide), which is a key step in ch
82 ly conserved cysteine residues implicated in protochlorophyllide (Pchlide)-binding and catalysis.
83 to the dark-specific isoform PORA (pPORA) is protochlorophyllide (Pchlide)-dependent and due to the o
85 activity, but resulted in a decrease in the protochlorophyllide-(PChlide)-binding capacity of POR.
86 einhardtii has been shown to be incapable of protochlorophyllide photoconversion in vivo and is thoug
87 on light exposure, the chlorophyll precursor protochlorophyllide produces reactive oxygen species (RO
88 The L protein (BchL) of the dark-operative protochlorophyllide reductase (DPOR) from Rhodobacter sp
92 eening is the result of severe repression of protochlorophyllide reductase (POR) genes by far-red lig
93 emonstrate that pc-1 was in fact a defect in protochlorophyllide reductase activity and provide the f
94 the first reproducible demonstration of dark protochlorophyllide reductase activity from purified pro
95 ted protochlorophyllide, suggesting that the protochlorophyllide reductase activity is affected by ex
98 s Mg-protoporphyrin IX methyltransferase and protochlorophyllide reductase are significantly impaired
100 the major (36 kDa) immunodetectable form of protochlorophyllide reductase consistent with their inab
101 d sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein
106 on within the fourth and fifth codons of the protochlorophyllide reductase precursor that causes a sh
109 , encoding subunits of the light-independent protochlorophyllide reductase were detected in the cotyl
110 e-associated biosynthetic complex containing protochlorophyllide reductase, chlorophyll synthase, ger
114 olutely necessary for the second step of the protochlorophyllide reduction reaction, "dark" conversio
115 r a polypeptide needed for light-independent protochlorophyllide reduction) were grown in darkness, t
116 defective ATP-binding site does not support protochlorophyllide reduction, illustrating nucleotide b
117 ediated POR; repression from light-dependent protochlorophyllide reduction, two processes that normal
121 e importance of active-site architecture and protochlorophyllide structure in driving POR photochemis
122 opper concentrations, the mutant accumulated protochlorophyllide, suggesting that the protochlorophyl
123 e dark, including those encoding enzymes for protochlorophyllide synthesis and PIN-LIKES3 for auxin-d
124 r these conditions of inhibited reduction of protochlorophyllide, the accumulation kinetics of this i
125 porphyrin IX methyl ester and only traces of protochlorophyllide, the product of the cyclase, were de
127 ization of PORs to trigger the conversion of protochlorophyllide to chlorophyllide in developing seed
128 ms the strictly light-dependent reduction of protochlorophyllide to chlorophyllide is catalyzed by NA
130 chlorophyll biosynthesis is the reduction of protochlorophyllide to chlorophyllide, catalyzed by dark
131 phyllide oxidoreductases (PORs) that convert protochlorophyllide to chlorophyllide, reducing ROS prod
132 duction of the photosensitizer and substrate protochlorophyllide to form the pigment chlorophyllide.
133 pif1 mutant seedlings accumulate excess free protochlorophyllide when grown in the dark, with consequ