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malfunction
mutants defective in pheophorbide a oxygenase or red chlorophyll catabolite reductase, e.g. acd2 mutants that exhibit a light-dependent cell death phenotype with spontaneous spreading lesions, the mutants develop a lesion mimic phenotype, due to accumulation of breakdown intermediates
evolution

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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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in chlorophyll breakdown, the basic mechanism of macrocycle cleavage appears to be the same in green algae and in angiosperms
evolution
Cleome graveolens
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Cycas sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Equisetum sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
-
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Selaginella sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family, which synthesizes a variety of phytobilin pigments, on the basis of sequence similarity, ferredoxin dependency, and the common tetrapyrrole skeleton of their substrates. The tertiary structure of RCCR is similar to those of FDBRs, strongly supporting that these enzymes evolved from a common ancestor
evolution
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the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family. RCC is bound to the pocket between the beta-sheet and the C-terminal alpha-helices, as seen in substrate-bound FDBRs, but RCC binding to RCCR is much looser than substrate binding to FDBRs
evolution
RCCR is distantly related to a family of bilin reductases
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
the enzyme belongs to the ferredoxin-dependent bilin reductase family, FDBR, and contains two conserved acidic residue sites (Glu151 and Asp288), which are involved in catalysis and/or substrate binding
evolution
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red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green algae by the formation of FCCs and NCCs
evolution
red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green alga by the formation of FCCs and NCCs
metabolism

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The key step in Chl breakdown in green plants, the cleavage reaction of the porphinoid macrocycle, is catalyzed by an oxygenase that specifically recognizes pheophorbide a (Pheide a). The conversion of Pheide a to a primary blue fluorescent catabolite (pFCC) requires the joint action of PaO and the soluble stroma-located enzyme RCC reductase that reduces the intermediary red catabolite (RCC) to pFCC, structures of breakdown products of chlorophyll, overview
metabolism
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the chlorophyll catabolic enzymes (CCEs) NYC1, NOL, PPH, PAO and RCCR interact with the light harvesting complex II, LHCII. The enzyme RCCR interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, a component of the proposed SGR-CCE-LHCII complex, in Arabidopsis thaliana chlorophyll catabolism
metabolism
the three chl catabolic enzymes, chlorophyllase, pheophorbide a oxygenase (PAO), and red chlorophyll catabolite reductase (RCCR) catalyze chlorophyll breakdown, which is very important for plant development and survival. Chlorophyll breakdown is a prerequisite to detoxify the potentially phototoxic pigment within the vacuoles in order to permit the remobilization of nitrogen from chlorophyll-binding proteins to proceed during senescence. Enzyme RCCR might be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to PAO) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to primary fluorescent chlorophyll catabolite
metabolism
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the oxygenase catalyzing porphyrin cleavage is a monooxygenase. In Chlorella, a mechanism with intermediary formation of a C4:C5 epoxide and subsequent hydrolytic cleavage and prototropic rearrangements has been proposed. Thereby, the second rearrangement at C10 has been demonstrated to be highly stereoselective. Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
opening the porphyrin macrocycle of pheophorbide a and forming the primary fluorescent chlorophyll catabolites are key steps in the chlorophyll catabolism pathway. These steps are catalyzed by pheophorbide a oxygenase and red chlorophyll catabolite reductase
metabolism
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in chlorophyll breakdown, the conversion of pheophorbide a to primary fluorescent chlorophyll catabolites is catalyzed by the joint action of the two enzymes PaO, a membrane-bound enzyme, and the soluble stroma enzyme RCCR. The former cleaves the porphyrin macrocycle oxidatively and produces a bound form of the intermediary catabolite (RCC), which seems to be reduced stereoselectively on the C20=C1 bond by the action of the reductase
metabolism
in chlorophyll breakdown, the conversion of pheophorbide a to primary fluorescent chlorophyll catabolites is catalyzed by the joint action of the two enzymes PaO, a membrane-bound enzyme, and the soluble stroma enzyme RCCR. The former cleaves the porphyrin macrocycle oxidatively and produces a bound form of the intermediary catabolite (RCC), which seems to be reduced stereoselectively on the C20=C1 bond by the action of the reductase
metabolism
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in the chlorophyll breakdown pathway, the key reaction which causes loss of green color in leaf senescence is catalyzed in a two-step reaction by pheophorbide an oxygenase and red chlorophyll catabolite reductase. Red chlorophyll catabolite, RCC, the primary product of oxygenolytic Pheide a cleavage by pheophorbide a oxygenase, PaO, is subsequently reduced to primary fluorescent chlorophyll catabolite by red chlorophyll catabolite reductase, RCCR. RCC appears not to be released from PaO, but is directly reduced to pFCC by RCCR, suggesting a close physical contact between the two protein components during catalysis and metabolic channeling of the red intermediate. Both partial reactions require reduced ferredoxin as the source of electrons, whereby ferredoxin is kept in the reduced state either by photosystem I or the pentose phosphate cycle. Since the PaO reaction is accompanied by the incorporation of two oxygen atoms and RCCR activity is sensitive to oxygen, the interaction of PaO and RCCR is a prerequisite for RCCR action
metabolism
in the chlorophyll breakdown pathway, the key reaction which causes loss of green color in leaf senescence is catalyzed in a two-step reaction by pheophorbide an oxygenase and red chlorophyll catabolite reductase. Red chlorophyll catabolite, RCC, the primary product of oxygenolytic Pheide a cleavage by pheophorbide a oxygenase, PaO, is subsequently reduced to primary fluorescent chlorophyll catabolite by red chlorophyll catabolite reductase, RCCR. RCC appears not to be released from PaO, but is directly reduced to pFCC by RCCR, suggesting a close physical contact between the two protein components during catalysis and metabolic channeling of the red intermediate. Both partial reactions require reduced ferredoxin as the source of electrons, whereby ferredoxin is kept in the reduced state either by photosystem I or the pentose phosphate cycle. Since the PaO reaction is accompanied by the incorporation of two oxygen atoms and RCCR activity is sensitive to oxygen, the interaction of PaO and RCCR is a prerequisite for RCCR action
physiological function

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the conversion of Pheide a to a primary blue fluorescent catabolite (pFCC) requires the joint action of PaO and a soluble stroma-located enzyme that reduces an intermediary red catabolite (RCC) to pFCC. Both PaO and RCC reductase require reduced ferredoxin as reductant. Although RCC reductase is present at all stages of development and in all tissues examined, PaO seems to occur in gerontoplasts exclusively
physiological function
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the key steps in the degradation pathway of chlorophylls are the ring opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by red chlorophyll catabolite reductase (RCCR). During these steps, chlorophyll catabolites lose their color and phototoxicity. Enzyme RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
physiological function
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red chlorophyll catabolite reductase (RCCR) catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite (RCC), the catabolic intermediate produced in chlorophyll degradation
physiological function
the enzyme is involved in defense responses to various stresses
physiological function
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a major goal of chlorophyll breakdown merely concerns the detoxification of the green plant pigment which may be destructive otherwise as a photosensitizer to the regulated processes that occur during senescence
physiological function
a major goal of chlorophyll breakdown merely concerns the detoxification of the green plant pigment which may be destructive otherwise as a photosensitizer to the regulated processes that occur during senescence
physiological function
the expression of BrPPH, BrPAO and BrRCCR, and the activity of Mg-dechelatase is closely associated with the chlorophyll degradation during the leaf senescence process in harvested Chinese flowering cabbages under dark conditions
physiological function
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chlorophyll degradation is an integral part of leaf senescence or fruit ripening
physiological function
Chlorophyll degradation is not only an integral part of leaf senescence or fruit ripening, but in several species, such as oilseed rape, also occurs in maturing seeds, significance of the chlorophyll breakdown pathway in respect to chlorophyll degradation during Brassica napus seed development
physiological function
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the enzyme is involved in chlorophyll catabolism in leaf senescence. Chlorophyll catabolism occurs throughout the plant life-cycle and is highly sensitive to both biotic and abiotic stresses
additional information

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Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis
additional information
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the substrate red chlorophyll catabolite is bound to the pocket between the beta-sheet and the C-terminal alpha-helices. Substrate RCC binds quiet lossely to the enzyme. The loose binding seems beneficial to the large conformational change in red chlorophyll catabolite upon reduction. Two conserved acidic residues, Glu154 and Asp291, sandwich the C20/C1 double bond of RCC, suggesting that these two residues are involved in site-specific reduction. The geometrical arrangement of RCC and the carboxy groups of Glu154 and Asp291 in RCCR is essential for the stereospecificity of the RCCR reaction, substrate binding mechanism, overview. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to F218V enzyme mutant structures, overview
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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the primary fluorescent chlorophyll catabolite Ca-FCC-2 from sweet pepper, Capsicum annuum, chromoplasts has similar optical properties, but is slightly less polar than the primary FCC from senescent cotyledons of oilseed rape, Brassica napus, determination of structure and constitution by fast-atom-bombardment mass spectra and homo- and heteronuclear magnetic resonance experiments. Two-dimensional homonuclear spectra of Ca-FCC-2 reveals it to differ from pFCC by the configuration at the methine atom C1, whose configuration results from the action of red chlorophyll catabolite reductase, RCCR. Structure analysis, overview
additional information
the primary fluorescent chlorophyll catabolite Ca-FCC-2 from sweet pepper, Capsicum annuum, chromoplasts has similar optical properties, but is slightly less polar than the primary FCC from senescent cotyledons of oilseed rape, Brassica napus, determination of structure and constitution by fast-atom-bombardment mass spectra and homo- and heteronuclear magnetic resonance experiments. Two-dimensional homonuclear spectra of Ca-FCC-2 reveals it to differ from pFCC by the configuration at the methine atom C1, whose configuration results from the action of red chlorophyll catabolite reductase, RCCR. Structure analysis, overview
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primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + acceptor
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three different primary fluorescent chlorophyll catabolites are produced, two of which could be identified as the stereoisomeric pFCCs from canola (Brassica napus) (pFCC-1) and sweet pepper (Capsicum annuum) (pFCC-2), respectively
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red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
additional information
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primary fluorescent chlorophyll catabolite + NADP+

red chlorophyll catabolite + NADPH + H+
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stereospecific reaction
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
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r
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
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stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
formation of a stereospecific product, overview
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
a red tetrapyrrole
two different fluorescent chlorophyll catabolites are formed from red chlorophyll catabolite and identified as primary fluorescent chlorophyll catabolite and its C1 epimer, 1-epi-pFCC
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
loose substrate binding allows for conformation change during the reaction, stereospcific reaction, mechanism, overview
formation of a stereospecific product, overview
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
reduction of the C20/C1 double bond of red chlorophyll catabolite is catalyzed by RCCR in a stereospecific manner forming the C1 isomer pFCC-1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
product epimer Bn-FCC-2
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
a red tetrapyrrole
two different fluorescent chlorophyll catabolites are formed from red chlorophyll catabolite and identified as primary fluorescent chlorophyll catabolite and its C1 epimer, 1-epi-pFCC
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen, stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
i.e. Ca-pFCC-2, or 1-epi-FCC, or (1zeta,132R,17S,18S)-31,32-didehydro-1,4,5,10,17,18,20,22-octahydro-132-(methoxycarbonyl)-4,5-dioxo-4,5-secophytoporphyrin
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
two products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cleome graveolens
-
-
catabolite pFCC-0, possible representing a modified version of either pFCC-1 or -2
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cycas sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Equisetum sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
stereospecificity towards reduction of C1
three products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1, and pFCC-3 with undetermined structure
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Selaginella sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-0, possible representing a modified version of either pFCC-1 or -2
-
?
red chlorophyll catabolite + reduced acceptor

primary fluorescent chlorophyll catabolite + oxidized acceptor
-
chlorophyll catabolism, leaf senescence, ring-opening activity, a reduction destroys the residual conjugated bond system to yield the colourless product
pFCC, the fate of primary fluorescent chlorophyll catabolite is to be conjugated, imported into the vacuole and tautomerized to accumulate there as non-fluorescent chlorophyll catabolites and possibly other terminal catabolites
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
-
the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites
-
?
additional information

?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
-
-
-
additional information
?
-
-
with Arabidopsis RCCR, the C1 isomer pFCC-1 is formed. RCCR could be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to pheophorbide a oxygenase) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to blue-fluorescing intermediate
-
-
-
additional information
?
-
-
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown in senescent Arabidopsis leaves
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key reaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
-
strongly interacts with catabolic enzymes (CCEs), NONYELLOW COLORING1 (NYC1), pheophorbide a oxygenase (PAO), NYC1-LIKE (NOL) and pheophytinase
-
-
-
additional information
?
-
the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay and in Arabidopsis thaliana chlorophyll catabolism
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
the enzyme is involved in breakdown of chlorophyll
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
Cleome graveolens
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Cycas sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Equisetum sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
barley RCCR produces the C1 isomer pFCC-1
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key eaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Selaginella sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
with tomato RCCR, the C1 isomer pFCC-2 is formed
-
-
-
additional information
?
-
-
spinach RCCR produces the C1 isomer pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
additional information
?
-
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q8LDU4
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q1ELT7
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q1ELT7
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
V5K6J8
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cleome graveolens
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cycas sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Equisetum sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q9MTQ6
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Selaginella sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + reduced acceptor

primary fluorescent chlorophyll catabolite + oxidized acceptor
-
chlorophyll catabolism, leaf senescence, ring-opening activity, a reduction destroys the residual conjugated bond system to yield the colourless product
pFCC, the fate of primary fluorescent chlorophyll catabolite is to be conjugated, imported into the vacuole and tautomerized to accumulate there as non-fluorescent chlorophyll catabolites and possibly other terminal catabolites
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
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the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites
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cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
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with Arabidopsis RCCR, the C1 isomer pFCC-1 is formed. RCCR could be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to pheophorbide a oxygenase) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to blue-fluorescing intermediate
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RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
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Q8LDU4
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
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the enzyme is involved in chlorophyll breakdown in senescent Arabidopsis leaves
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the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key reaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
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Q8LDU4
the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay and in Arabidopsis thaliana chlorophyll catabolism
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in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
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the enzyme is involved in breakdown of chlorophyll
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in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
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barley RCCR produces the C1 isomer pFCC-1
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the enzyme is involved in chlorophyll breakdown
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additional information
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the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key eaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
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with tomato RCCR, the C1 isomer pFCC-2 is formed
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Hörtensteiner, S.
Chlorophyll degradation during senescence
Annu. Rev. Plant Biol.
57
55-77
2006
Arabidopsis sp., Hordeum vulgare, Solanum lycopersicum, Spinacia oleracea
brenda
Hörtensteiner, S.; Wüthrich, K.L.; Matile, P.; Ongania, K.H.; Kräutler, B.
The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase
J. Biol. Chem.
273
15335-15339
1998
Brassica napus (Q1ELT7)
brenda
Hörtensteiner, S.; Rodoni, S.; Schellenberg, M.; Vicentini, F.; Nandi, O.I.; Qui, Y.L.; Matile, P.
Evolution of chlorophyll degradation: the significance of RCC reductase
Plant Biol.
2
63-67
2000
Angiopteris, Auxenochlorella protothecoides, Carex, Cleome graveolens, Cycas sp., Equisetum sp., Euptelea, Ginkgo biloba, Hordeum vulgare (Q9MTQ6), Metasequoia, Picea, Psilotum, Selaginella sp., Solanum lycopersicum, Spinacia oleracea, Taxus baccata, Taxus sp., Tropaeolum majus
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brenda
Pruzinska, A.; Anders, I.; Aubry, S.; Schenk, N.; Tapernoux-Lüthi, E.; Müller, T.; Kräutler, B.; Hörtensteiner, S.
In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown
Plant Cell
19
369-387
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q8LDU4)
brenda
Wüthrich, K.L.; Bovet, L.; Hunziker, P.E.; Donnison, I.S.; Hörtensteiner, S.
Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism
Plant J.
21
189-198
2000
Arabidopsis thaliana, Hordeum vulgare, Hordeum vulgare (Q9MTQ6)
brenda
Rodoni, S.; Mühlecker, W.; Anderl, M.; Kräutler, B.; Moser, D.; Thomas, H.; Matile, P.; Hörtensteiner, S.
Chlorophyll breakdown in senescent chloroplasts (cleavage of pheophorbide a in two enzymic steps)
Plant Physiol.
115
669-676
1997
Brassica napus
brenda
Rodoni, S.; Vicentini, F.; Schellenberg, M.; Matile, P.; Hörtensteiner, S.
Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown
Plant Physiol.
115
677-682
1997
Hordeum vulgare
brenda
Pruzinska, A.; Tanner, G.; Aubry, S.; Anders, I.; Moser, S.; Müller, T.; Ongania, K.H.; Kräutler, B.; Youn, J.Y.; Liljegren, S.J.; Hörtensteiner, S.
Chlorophyll breakdown in senescent Arabidopsis leaves. Characterization of chlorophyll catabolites and of chlorophyll catabolic enzymes involved in the degreening reaction
Plant Physiol.
139
52-63
2005
Arabidopsis thaliana
brenda
Mach, J.M.; Castillo, A.R.; Hoogstraten, R.; Greenberg, J.T.
The Arabidopsis-accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
Proc. Natl. Acad. Sci. USA
98
771-776
2001
Arabidopsis sp.
brenda
Sugishima, M.; Kitamori, Y.; Noguchi, M.; Kohchi, T.; Fukuyama, K.
Crystal structure of red chlorophyll catabolite reductase: enlargement of the ferredoxin-dependent bilin reductase family
J. Mol. Biol.
389
376-387
2009
Arabidopsis thaliana, Arabidopsis thaliana (Q8LDU4)
brenda
Ougham, H.; Hoertensteiner, S.; Armstead, I.; Donnison, I.; King, I.; Thomas, H.; Mur, L.
The control of chlorophyll catabolism and the status of yellowing as a biomarker of leaf senescence
Plant Biol.
10 Suppl 1
4-14
2008
Arabidopsis thaliana (Q8LDU4)
brenda
Sugishima, M.; Okamoto, Y.; Noguchi, M.; Kohchi, T.; Tamiaki, H.; Fukuyama, K.
Crystal structures of the substrate-bound forms of red chlorophyll catabolite reductase: implications for site-specific and stereospecific reaction
J. Mol. Biol.
402
879-891
2010
Arabidopsis thaliana, Arabidopsis thaliana (Q8LDU4)
brenda
Sakuraba, Y.; Schelbert, S.; Park, S.Y.; Han, S.H.; Lee, B.D.; Andres, C.B.; Kessler, F.; Hoertensteiner, S.; Paek, N.C.
STAY-GREEN and chlorophyll catabolic enzymes interact at light-harvesting complex II for chlorophyll detoxification during leaf senescence in Arabidopsis
Plant Cell
24
507-518
2012
Arabidopsis thaliana
brenda
Liu, F.; Guo, F.
Nitric oxide deficiency accelerates chlorophyll breakdown and stability loss of thylakoid membranes during dark-induced leaf senescence in Arabidopsis
PLoS ONE
8
e56345
2013
Arabidopsis thaliana
brenda
Sakuraba, Y.; Kim, Y.S.; Yoo, S.C.; Hoertensteiner, S.; Paek, N.C.
7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling of chlorophyll breakdown intermediates during leaf senescence
Biochem. Biophys. Res. Commun.
430
32-37
2013
Arabidopsis thaliana (Q8LDU4)
brenda
Hoertensteiner, S.
Chlorophyll degradation during senescence
Annu. Plant Biol.
57
55-77
2006
Arabidopsis thaliana (Q8LDU4)
brenda
Hoertensteiner, S.
Chlorophyll breakdown in higher plants and algae
Cell. Mol. Life Sci.
56
330-347
1999
Auxenochlorella protothecoides, Brassica napus, Capsicum annuum, Festuca pratensis, Hordeum vulgare (Q9MTQ6), Parachlorella kessleri, Phaseolus vulgaris
brenda
Xiao, H.J.; Jin, J.H.; Chai, W.G.; Gong, Z.H.
Cloning and expression analysis of pepper chlorophyll catabolite reductase gene CaRCCR
Genet. Mol. Res.
14
368-379
2015
Capsicum annuum (V5K6J8)
brenda
Muehlecker, W.; Kraeutler, B.; Moser, D.; Matile, P.; Hoertensteiner, S.
Breakdown of chlorophyll: A fluorescent chlorophyll catabolite from sweet pepper (Capsicum annuum)
Helv. Chim. Acta
83
278-286
2000
Brassica napus (Q1ELT7), Capsicum annuum (V5K6J8)
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brenda
Zhang, X.; Zhang, Z.; Li, J.; Wu, L.; Guo, J.; Ouyang, L.; Xia, Y.; Huang, X.; Pang, X.
Correlation of leaf senescence and gene expression/activities of chlorophyll degradation enzymes in harvested Chinese flowering cabbage (Brassica rapa var. parachinensis)
J. Plant Physiol.
168
2081-2087
2011
Brassica rapa (G0YWA4)
brenda
Hoertensteiner, S.; Kraeutler, B.
Chlorophyll breakdown in oilseed rape
Photosyn. Res.
64
137-146
2000
Arabidopsis thaliana (Q8LDU4), Brassica napus, Brassica napus (Q1ELT7)
brenda
Roca, M.; James, C.; Pruzinska, A.; Hoertensteiner, S.; Thomas, H.; Ougham, H.
Analysis of the chlorophyll catabolism pathway in leaves of an introgression senescence mutant of Lolium temulentum
Phytochemistry
65
1231-1238
2004
Lolium temulentum
brenda