Angiosperms need light to synthesize chlorophyll, but lotus (Nelumbo nucifera Gaertn.) embryo was suspected to have the ability to form chlorophyll in the dark because lotus embryo can turn into green under the covera...Angiosperms need light to synthesize chlorophyll, but lotus (Nelumbo nucifera Gaertn.) embryo was suspected to have the ability to form chlorophyll in the dark because lotus embryo can turn into green under the coverage of four layers of integuments (cotyledon, seed coat, pericarp, lotus pod) which were thought impossible for light to pass through. The authors excluded this possibility based on two experimental results: First, enclosing the young lotus pod with aluminium foil, the growth of louts embryo continued, but the chlorophyll formation was seriously inhibited. A lot of protochlorophyllide, chlorophyll precursor, were accumulated, most of which were combined with LPOR (light dependent protochlorophyllide oxidoreductase). Second, DPOR (dark or light-independent protochlorophyllide oxidoreductase) was the enzyme necessary for chlorophyll synthesis in the dark. The genes encoding DPOR were conservative in many species, but no homologues could be found in lotus genome. Taken together, authers' results clearly demonstrated that lotus embryo synthesizes chlorophyll only through the light-dependent pathway.展开更多
This research was to examine if rice (Oryza sativa L.), a monocotyledon of angiosperm, was able to synthesize chlorophyll (Chl) in complete darkness. Five-cm-tall etiolated seedlings of rice were used as starting mate...This research was to examine if rice (Oryza sativa L.), a monocotyledon of angiosperm, was able to synthesize chlorophyll (Chl) in complete darkness. Five-cm-tall etiolated seedlings of rice were used as starting materials and treated with or without various concentrations of glucose and/or δ-aminolevulinic acid (ALA) in the dark. Leaves harvested at the indicated time were determined for their contents of Chl, protoporphyrin Ⅸ (Proto), Mg-protoporphyrin Ⅸ (Mg-Proto) and protochlorophyllide (Pchlide). The mole percentage of porphyrin was calculated. The Chl content in the etiolated rice seedlings slightly increased from about 2.5 μg/g to 7.5 μg/g within 12 d in the dark, but the total Chl of dark-grown rice increased from 0.36 μg/g to 3.6 μg/g. While the mole percentages of Proto, Mg-Proto and Pchlide in the dark-grown seedlings without any treatment were about 65%, 27.5% and 7.5% at the beginning, respectively, those in the light-grown seedlings were about 42.5%, 35% and 22.5%, respectively. The mole percentage of porphyrin of etiolated seedlings resumed its normal ratio within 2 d after treatment with glucose. While the Chl content of etiolated seedlings grown in culture solution with 3% and 6% glucose increased 2.5 and 4.0 folds, respectively, those with 3% and 6% glucose and 1 mmol/L ALA increased 22 and 24 folds, respectively. It is concluded that angiosperm might be able to synthesize a small amount of Chl in complete darkness, that either glucose or ALA could stimulate dark Chl synthesis in angiosperm, and that a combination of glucose and ALA exhibited an additional effect. It is still unknown and remains to be further explored what is the mechanism of the effect of glucose and ALA on the Chl synthesis of rice in the dark.展开更多
The key step in chlorophyll biosynthesis is photoreduction of its immediate precursor, protochlorophyllide. This reaction is catalyzed by a photoenzyme, protochlorophyllide oxidoreductase (POR) and consists in the att...The key step in chlorophyll biosynthesis is photoreduction of its immediate precursor, protochlorophyllide. This reaction is catalyzed by a photoenzyme, protochlorophyllide oxidoreductase (POR) and consists in the attachment of two hydrogen atoms in positions C17 and C18 of the tetrapyrrole molecule of protochlorophyllide;the double bond is replaced with the single bond. Two hydrogen donors involved in protochloro-phyllide photoreduction are NADPH [1,2] and a conserved tyrosine residue Tyr193 of the photoenzyme POR [3]. The structure of active pigment-enzyme complex (Pchlide-POR-NADPH) ensures a favorable steric conditions for the transfer of hydride ion and proton. This review does not examine the ternary complex structure, but concentrates upon the mechanisms of primary photophysical and photochemical reactions during formation of chlorophyllide from protochlorophyllide in living objects (etiolated leaves and leaf homogenates) and model systems.展开更多
Nitrogen fixation, along with photosynthesis is the basis of all life on earth. Current understanding suggests that no plant fixes its own nitrogen. Some plants （mainly legumes） fix nitrogen via symbiotic anaerobic ...Nitrogen fixation, along with photosynthesis is the basis of all life on earth. Current understanding suggests that no plant fixes its own nitrogen. Some plants （mainly legumes） fix nitrogen via symbiotic anaerobic microorganisms （mainly rhizobia）. The nature of biological nitrogen fixation is that the dinitrogenase catalyzes the reaction-splitting triple-bond inert atmospheric nitrogen （N2） into organic ammonia molecule （NH3）. All known nitrogenases are found to be prokaryotic, multi-complex and normally oxygen liable. Not surprisingly, the engineering of autonomous nitrogen-fixing plants would be a long-term effort because it requires the assembly of a complex enzyme and provision of anaerobic conditions. However, in the light of evolving protein catalysts, the anaerobic enzyme has almost certainly been replaced in many reactions by the more efficient and irreversible aerobic version that uses O2. On the other hand, nature has shown numerous examples of evolutionary convergence where an enzyme catalyzing a highly specific, O2-requiring reaction has an oxygen-independent counterpart, able to carry out the same reaction under anoxic conditions. In this review, I attempt to take the reader on a simplified journey from conventional nitrogenase complex to a possible simplified version of a yet to be discovered light-utilizing nitrogenase.展开更多
文摘Angiosperms need light to synthesize chlorophyll, but lotus (Nelumbo nucifera Gaertn.) embryo was suspected to have the ability to form chlorophyll in the dark because lotus embryo can turn into green under the coverage of four layers of integuments (cotyledon, seed coat, pericarp, lotus pod) which were thought impossible for light to pass through. The authors excluded this possibility based on two experimental results: First, enclosing the young lotus pod with aluminium foil, the growth of louts embryo continued, but the chlorophyll formation was seriously inhibited. A lot of protochlorophyllide, chlorophyll precursor, were accumulated, most of which were combined with LPOR (light dependent protochlorophyllide oxidoreductase). Second, DPOR (dark or light-independent protochlorophyllide oxidoreductase) was the enzyme necessary for chlorophyll synthesis in the dark. The genes encoding DPOR were conservative in many species, but no homologues could be found in lotus genome. Taken together, authers' results clearly demonstrated that lotus embryo synthesizes chlorophyll only through the light-dependent pathway.
文摘This research was to examine if rice (Oryza sativa L.), a monocotyledon of angiosperm, was able to synthesize chlorophyll (Chl) in complete darkness. Five-cm-tall etiolated seedlings of rice were used as starting materials and treated with or without various concentrations of glucose and/or δ-aminolevulinic acid (ALA) in the dark. Leaves harvested at the indicated time were determined for their contents of Chl, protoporphyrin Ⅸ (Proto), Mg-protoporphyrin Ⅸ (Mg-Proto) and protochlorophyllide (Pchlide). The mole percentage of porphyrin was calculated. The Chl content in the etiolated rice seedlings slightly increased from about 2.5 μg/g to 7.5 μg/g within 12 d in the dark, but the total Chl of dark-grown rice increased from 0.36 μg/g to 3.6 μg/g. While the mole percentages of Proto, Mg-Proto and Pchlide in the dark-grown seedlings without any treatment were about 65%, 27.5% and 7.5% at the beginning, respectively, those in the light-grown seedlings were about 42.5%, 35% and 22.5%, respectively. The mole percentage of porphyrin of etiolated seedlings resumed its normal ratio within 2 d after treatment with glucose. While the Chl content of etiolated seedlings grown in culture solution with 3% and 6% glucose increased 2.5 and 4.0 folds, respectively, those with 3% and 6% glucose and 1 mmol/L ALA increased 22 and 24 folds, respectively. It is concluded that angiosperm might be able to synthesize a small amount of Chl in complete darkness, that either glucose or ALA could stimulate dark Chl synthesis in angiosperm, and that a combination of glucose and ALA exhibited an additional effect. It is still unknown and remains to be further explored what is the mechanism of the effect of glucose and ALA on the Chl synthesis of rice in the dark.
文摘The key step in chlorophyll biosynthesis is photoreduction of its immediate precursor, protochlorophyllide. This reaction is catalyzed by a photoenzyme, protochlorophyllide oxidoreductase (POR) and consists in the attachment of two hydrogen atoms in positions C17 and C18 of the tetrapyrrole molecule of protochlorophyllide;the double bond is replaced with the single bond. Two hydrogen donors involved in protochloro-phyllide photoreduction are NADPH [1,2] and a conserved tyrosine residue Tyr193 of the photoenzyme POR [3]. The structure of active pigment-enzyme complex (Pchlide-POR-NADPH) ensures a favorable steric conditions for the transfer of hydride ion and proton. This review does not examine the ternary complex structure, but concentrates upon the mechanisms of primary photophysical and photochemical reactions during formation of chlorophyllide from protochlorophyllide in living objects (etiolated leaves and leaf homogenates) and model systems.
文摘Nitrogen fixation, along with photosynthesis is the basis of all life on earth. Current understanding suggests that no plant fixes its own nitrogen. Some plants （mainly legumes） fix nitrogen via symbiotic anaerobic microorganisms （mainly rhizobia）. The nature of biological nitrogen fixation is that the dinitrogenase catalyzes the reaction-splitting triple-bond inert atmospheric nitrogen （N2） into organic ammonia molecule （NH3）. All known nitrogenases are found to be prokaryotic, multi-complex and normally oxygen liable. Not surprisingly, the engineering of autonomous nitrogen-fixing plants would be a long-term effort because it requires the assembly of a complex enzyme and provision of anaerobic conditions. However, in the light of evolving protein catalysts, the anaerobic enzyme has almost certainly been replaced in many reactions by the more efficient and irreversible aerobic version that uses O2. On the other hand, nature has shown numerous examples of evolutionary convergence where an enzyme catalyzing a highly specific, O2-requiring reaction has an oxygen-independent counterpart, able to carry out the same reaction under anoxic conditions. In this review, I attempt to take the reader on a simplified journey from conventional nitrogenase complex to a possible simplified version of a yet to be discovered light-utilizing nitrogenase.
