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1 n the formation of 5-aminolevulinic acid and protochlorophyllide.
2 nsistent with their inability to photoreduce protochlorophyllide.
3 IX), Mg-proto, Mg-proto MME and 3,8-divinyl protochlorophyllide a (DV-Pchlide) levels, but this was
4 t cells secrete large amounts of 3,8-divinyl-protochlorophyllide a into the growth medium and have a
6 approximately 50% identity with Rieske-type protochlorophyllide a oxygenases (PTC52) from higher pla
9 fluorescence as result of elevated levels of protochlorophyllide and four red fluorescent in the dark
10 on protein, is required for the synthesis of protochlorophyllide and therefore is a candidate subunit
11 wn plants led to the reduced accumulation of protochlorophyllide and transcripts for the two committe
13 isomer of the substrate [C8-ethyl-C13(2)-(R)-protochlorophyllide] demonstrate that the enzyme photoac
14 his mutant also synthesized small amounts of protochlorophyllide dihydrogeranylgeraniol ester (protoc
15 e reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls
16 ric O2 levels, AcsFI synthesizes 3,8-divinyl protochlorophyllide from Mg-protoporphyrin IX monomethyl
19 orphyrin monomethylester and contain reduced protochlorophyllide levels and a reduced content of CHL2
20 ) were grown in darkness, the phycobilin and protochlorophyllide levels decreased upon deletion of sc
22 green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase (DPOR), a nitrogenase
26 ing skotomorphogenesis in angiosperms, NADPH:protochlorophyllide oxidoreductase (POR) forms an aggreg
27 with highly purified, recombinant pea NADPH:protochlorophyllide oxidoreductase (POR) heterologously
30 he gene coding for the light-dependent NADPH:protochlorophyllide oxidoreductase (POR) was interrupted
32 discrete set of genes in the dark, including protochlorophyllide oxidoreductase (POR), ferrochelatase
39 e light-dependent step is catalysed by NADPH:protochlorophyllide oxidoreductase (POR, EC.1.6.99.1), w
42 light-adapted plants and catalyzed by NADPH:protochlorophyllide oxidoreductase B (PORb) has been ana
43 yll biosynthesis, the light-activated enzyme protochlorophyllide oxidoreductase catalyzes trans addit
45 catalytic cycle of the light-driven enzyme, protochlorophyllide oxidoreductase, have been investigat
47 and porB) encoding the light-dependent NADPH:protochlorophyllide oxidoreductases (PORs) in loblolly p
48 tosynthetic competence through the action of protochlorophyllide oxidoreductases (PORs) that convert
49 small amounts of two unusual tetrapyrroles, protochlorophyllide (PChlide) b and pheophorbide (pheide
51 ll synthesis, the light-induced reduction of protochlorophyllide (PChlide) into chlorophyllide (Chlid
52 e reductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) into chlorophyllide (Chlid
53 ) catalyzes the light-dependent reduction of protochlorophyllide (Pchlide) into chlorophyllide in the
55 forms an aggregate of photolabile NADPH-POR-protochlorophyllide (Pchlide) ternary complexes localize
56 doreductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
57 doreductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
58 oreductase (POR, EC.1.6.99.1), which reduces protochlorophyllide (Pchlide) to chlorophyllide (Chlide)
59 POR) catalyzes the light-driven reduction of protochlorophyllide (Pchlide) to chlorophyllide, providi
60 f hydrogen across the C17-C18 double bond of protochlorophyllide (Pchlide), which is a key step in ch
61 ly conserved cysteine residues implicated in protochlorophyllide (Pchlide)-binding and catalysis.
62 to the dark-specific isoform PORA (pPORA) is protochlorophyllide (Pchlide)-dependent and due to the o
64 activity, but resulted in a decrease in the protochlorophyllide-(PChlide)-binding capacity of POR.
65 einhardtii has been shown to be incapable of protochlorophyllide photoconversion in vivo and is thoug
66 on light exposure, the chlorophyll precursor protochlorophyllide produces reactive oxygen species (RO
67 The L protein (BchL) of the dark-operative protochlorophyllide reductase (DPOR) from Rhodobacter sp
71 eening is the result of severe repression of protochlorophyllide reductase (POR) genes by far-red lig
72 emonstrate that pc-1 was in fact a defect in protochlorophyllide reductase activity and provide the f
73 the first reproducible demonstration of dark protochlorophyllide reductase activity from purified pro
74 ted protochlorophyllide, suggesting that the protochlorophyllide reductase activity is affected by ex
77 s Mg-protoporphyrin IX methyltransferase and protochlorophyllide reductase are significantly impaired
79 the major (36 kDa) immunodetectable form of protochlorophyllide reductase consistent with their inab
80 d sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein
85 on within the fourth and fifth codons of the protochlorophyllide reductase precursor that causes a sh
88 , encoding subunits of the light-independent protochlorophyllide reductase were detected in the cotyl
92 olutely necessary for the second step of the protochlorophyllide reduction reaction, "dark" conversio
93 r a polypeptide needed for light-independent protochlorophyllide reduction) were grown in darkness, t
94 ediated POR; repression from light-dependent protochlorophyllide reduction, two processes that normal
97 opper concentrations, the mutant accumulated protochlorophyllide, suggesting that the protochlorophyl
98 r these conditions of inhibited reduction of protochlorophyllide, the accumulation kinetics of this i
99 porphyrin IX methyl ester and only traces of protochlorophyllide, the product of the cyclase, were de
101 ization of PORs to trigger the conversion of protochlorophyllide to chlorophyllide in developing seed
102 ms the strictly light-dependent reduction of protochlorophyllide to chlorophyllide is catalyzed by NA
104 phyllide oxidoreductases (PORs) that convert protochlorophyllide to chlorophyllide, reducing ROS prod
105 pif1 mutant seedlings accumulate excess free protochlorophyllide when grown in the dark, with consequ
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