PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Chlorophyll”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 37 records · Page 2Linked to original sources
PubMed1994

Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability.

Chlorophyll protein accumulation in barley (Hordeum vulgare L.) chloroplasts is controlled posttranscriptionally by light-induced formation of chlorophyll a. The abundance of translation initiation complexes associated with psbA, psaA, and rbcL mRNAs was measured using extension and inhibition analysis in plants grown in the dark for 4.5 d and then illuminated for up to 16 h. Light-induced accumulation of the chlorophyll proteins was not accompanied by changes in the abundance of translation initiation complexes, indicating that regulation of chlorophyll protein accumulation at this stage of development does not occur at the level of translation initiation. Translational runoff assays were performed in the presence of lincomycin, an inhibitor of translation initiation, to determine whether chlorophyll protein accumulation was regulated at the level of translation elongation. The extent of ribosome runoff of psaA and psbA mRNAs was similar in the presence or absence of chlorophyll, indicating that chlorophyll did not alter chlorophyll protein translation elongation. Polysome-associated D1 translation intermediates were radiolabeled in the presence or absence of chlorophyll, even though full-length D1 accumulated only in the presence of chlorophyll. Chlorophyll influenced the stability of D1 translation intermediates to a small extent and greatly increased D1 stability after release from ribosomes. Overall, these results demonstrate that light-induced chlorophyll biosynthesis triggers the accumulation of the chlorophyll proteins D1 and P700 in barley chloroplasts by enhancement of chlorophyll apoprotein stability.

Apoproteins↗
PubMed1992

Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts.

Accumulation of plastid-encoded chlorophyll apoproteins and chlorophyll synthesis are controlled by light in angiosperms. An in vitro system utilizing isolated and lysed barley (Hordeum vulgare L.) etioplasts revealed the specific accumulation of P700, CP47, CP43 and D2 triggered by de novo synthesis of chlorophyll. Accumulation rates of radiolabelled chlorophyll apoproteins were linear for about 30 min. Pulse/chase translation assays showed that synthesis of chlorophyll does not result in increased chlorophyll apoprotein stability. Instead turnover rates of chlorophyll apoproteins were higher in the presence than in the absence of chlorophyll. Chlorophyll-dependent accumulation of chlorophyll apoproteins must therefore be regulated on the level of translation. Translation of chlorophyll apoproteins was blocked to about 50% by addition of 30-50 microM aurintricarboxylic acid or 20 microM kasugamycin. The kinetics of chlorophyll-dependent translation indicated that the in vitro translation system is capable of translation initiation. The capability of translation initiation was lost in lysed etioplasts after preincubation for at least 5 min without chlorophyll synthesis. The results suggest that initiation is involved in chlorophyll-dependent regulation of translation.

Aminoglycosides↗
PubMed2005

Chlorophyll accumulation is enhanced by osmotic stress in graminaceous chlorophyllic cells.

We have developed a new chlorophyllic cell line ('TADH-XO') from the highly water stress tolerant grass Bouteloua gracilis (blue grama). When grown under normal (non-stress) conditions, this new cell line accumulates higher levels of chlorophyll (up to 368.1 microg total chlorophyll g(-1) FW) than a previously obtained cell line ('TIANSJ98'). Both cell lines are capable of developing substantially higher amounts of chlorophyll when subjected to osmotic stress. In order to explain these changes in the chlorophyll kinetics of the chlorophyllic cells, we analyzed the following population variables in cells subjected to polyethylene glycol 8000-induced osmotic stress: growth, viability, chlorophyll (total, 'a' and 'b'), cell size, percentage of green cells and chloroplast (number and size). Although previous studies in some chlorophyllic cells of dicots have already reported that chlorophyll increases under saline stress, in this report we show that, at least in this graminaceous cell line, the increase in chlorophyll is an immediate and proportional response to the osmotic stress applied and not the result of a progressive adaptation process. Consistent with previous studies, the increase in chlorophyll accumulation could be the result of chloroplast development (increased thylakoid number per chloroplast). On the basis of our results, the increases in chlorophyll accumulation previously observed in salt-adapted dicot cells may be the result of the osmotic shock (water deficit), rather than the ionic effect of salt on the physiology of chlorophyllic cells of dicots. Under the cell population experimental approach we followed, our study provides important insights related to the physiological behavior of chlorophyllic cells subjected to osmotic stress.

Cell Line↗
PubMed1990

In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts.

An in vitro translation system using lysed etioplasts was developed to test if the accumulation of plastid-encoded chlorophyll a apoproteins is dependent on the de novo synthesis of chlorophyll a. The P700 apoproteins, CP47 and CP43, were not radiolabeled in pulsechase translation assays employing lysed etioplasts in the absence of added chlorophyll precursors. When chlorophyllide a plus phytylpyrophosphate were added to lysed etioplast translation assays in the dark, chlorophyll a was synthesized and radiolabeled P700 apoproteins, CP47 and CP43, and a protein which comigrates with D1 accumulated. Chlorophyllide a or phytylpyrophosphate added separately to the translation assay in darkness did not induce chlorophyll a formation or chlorophyll a apoprotein accumulation. Chlorophyll a formation and chlorophyll a apoprotein accumulation were also induced in the lysed etioplast translation system by the photoreduction of protochlorophyllide to chlorophyllide a in the presence of exogenous phytylpyrophosphate. Accumulation of radiolabeled CP47 was detectable when very low levels of chlorophyll a were synthesized de novo (less than 0.01 nmol/10(7) plastids), and radiolabel increased linearly with increasing de novo chlorophyll a formation. Higher levels of de novo synthesized chlorophyll a were required prior to detection of radiolabel incorporation into the P700 apoproteins and CP43 (greater than 0.01 nmol/10(7) plastids). Radiolabel incorporation into the P700 apoproteins, CP47 and CP43, saturated at a chlorophyll a concentration which corresponds to 50% of the etioplast protochlorophyllide content (0.06 nmol of chlorophyll a/10(7) plastids).

Apoproteins↗
PubMed1983

[Chlorophyll-protein complexes from green algae and higher plants. Identification of chlorophyll-containing bands in gel, using Chlamydomonas reinhardii mutants].

Three types of mutants (pigment, non-photosynthesizing and pigment non-photosynthesizing ones) were used to identify the chlorophyll-containing bands in gel slices. The pigment mutants with an impaired light-harvesting chlorophyll a/b-protein complex possess photochemically active reaction centers of photosystems and are capable of phototrophic growth. Using these mutants, the heterogeneity of the chlorophyll-containing bands, LH2 and LH3, in gel slices and the dependence of LH2 on chlorophyll a-protein and that of LH3 on chlorophyll b-protein in the light-harvesting complex were established. The non-photosynthesizing mutants with an inactive photosystem I (or II) are devoid of antennae forms of chlorophyll a and are not capable of phototrophic growth. Using these mutants, it was demonstrated that in gel slices the chlorophyll-containing band, CPI, corresponds to the chlorophyll a-protein complex of photosystem I, while CPII to the chlorophyll a-protein complex of photosystem II. It was also found that the presence of the chlorophyll-containing band, LH0 (CPIa) in gel slices correlates with the preservation of the light-harvesting complex and is independent of photosystem I. The spectral properties of chlorophyll complexes in gel slices are not identical to those of native chlorophyll. It was assumed that chloroplasts contain at least 4 types of chlorophyll proteins that are controlled by independent genes.

Chlamydomonas↗
PubMed1994

Properties of synthesis of chlorophyll a from chlorophyll b in cucumber etioplasts.

Chlorophyll a accumulated when chlorophyllide b was incubated with isolated cucumber etioplasts in the dark. When [14C]chlorophyllide b was used as the substrate for chlorophyll synthesis, [14C]chlorophyll a was formed, showing that chlorophyll a was synthesized from the exogenously added chlorophyllide b, not by light-independent reduction of endogenous protochlorophyllide. The reaction studied showed an optimal pH of 7.5 and required both the soluble and membrane fractions of etioplasts together with ATP. Time course experiments showed that chlorophyll a began to accumulate later than chlorophyll b. Chlorophyllide b esterified with geranylgeraniol accumulated first, but there was little accumulation of chlorophyll a with an unhydrogenated prenyl side chain. No chlorophyllide a was detected during incubation. These observations indicate that esterified chlorophyll b was converted to chlorophyll a. This conversion would play an important role in the use of chlorophyll b for the synthesis of chlorophyll a in the reconstruction of photosystems.

Chlorophyll↗
PubMed1981

Light-harvesting systems of brown algae and diatoms. Isolation and characterization of chlorophyll a/c and chlorophyll a/fucoxanthin pigment-protein complexes.

The present study examined the protein associations and energy transfer characteristics of chlorophyll c and fucoxanthin which are the major light-harvesting pigments in the brown and diatomaceous algae. It was demonstrated that sodium dodecyl sulfate (SDS)-solubilized photosynthetic membranes of these species when subjected to SDS polyacrylamide gel electrophoresis yielded three spectrally distinct pigment-protein complexes. The slowest migrating zone was identical to complex I, the SDS-altered form of the P-700 chlorophyll a-protein. The zone of intermediate mobility contained chlorophyll c and chlorophyll a in a molar ratio of 2 : 1, possessed no fucoxanthin, and showed efficient energy transfer from chlorophyll c to chlorophyll a. The fastest migrating pigment-protein zone contained fucoxanthin and chlorophyll a, possessed no chlorophyll c, and showed efficient energy transfer from fucoxanthin to chlorophyll a. It is demonstrated that the chlorophyll a/c-protein and the chlorophyll a/fucoxanthin-protein complexes are common to the brown algae and diatoms examined, and likely share similar roles in the photosynthetic units of these species.

Carotenoids↗
PubMed1983

Chlorophyll a biosynthetic routes and chlorophyll a chemical heterogeneity in plants.

A six-branched chlorophyll a biosynthetic pathway instead of a four-branched pathway has been proposed as being responsible for the formation of chlorophyll a in green plants. The several biosynthetic routes that make up the pathway have been described as leading to the formation of ten chemically different groups of chlorophyll a species. The latter differ from one another by one or more of the following modifications: (a) by having a vinyl or ethyl group at position 4 of the macrocycle, (b) by the nature of the long-chain fatty alcohols at position 7 of the macrocycle, and (c) by having a 6-membered lactone ring instead of a 5-membered cyclopentanone ring. The chemical structure of several of the metabolic intermediates of that pathway and of some of the chlorophyll a species have now been determined by primary chemical derivatization methods coupled to spectrofluorometric, nuclear magnetic resonance and mass spectral analyses. The formation of highly organized photosynthetic membranes in which some of the chlorophyll alpha molecules are specifically oriented is ascribed to the multiplicity of chlorophyll biosynthetic routes which result in the formation of multiple chlorophyll alpha chemical species. Proper orientation of chlorophyll in the photosynthetic membranes is visualized as being controlled by peripheral group modifications that either modulate the polarity of the Chl chromophore or control the magnitude of the net positive charge on the central Mg atom. Finally it is proposed that in addition to the proper orientation of chlorophyll a, chemical heterogeneity of the chlorophyll chromophores in the photosynthetic reaction centers is mandatory for efficient charge separation, and proper vectorial electron transfer.

Chlorophyll↗
PubMed1990

Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability.

Chlorophyll apoprotein accumulation in higher plant chloroplasts is controlled by light-dependent chlorophyll formation. Dark-grown plants lack chlorophyll and chlorophyll apoproteins. However, the plastid genes encoding the chlorophyll apoproteins are transcribed; chlorophyll apoprotein mRNA accumulates and associates with polysomes in plastids of dark-grown plants. Pulse-labeling assays revealed a population of short-lived proteins in plastids of dark-grown plants. One of these transiently labeled proteins was CP43, a chlorophyll apoprotein associated with photosystem II. Pulse-chase assays showed that newly synthesized CP43 was rapidly degraded in plastids of dark-grown plants, which lack chlorophyll. In contrast, CP43 synthesized in plastids from illuminated plants was stable. The synthesis of D1, a chlorophyll apoprotein of the photosystem II reaction center, was also analyzed in plastids of dark-grown and illuminated plants. Radiolabel accumulation into full-length D1 was only detected in plastids of illuminated plants. However, D1 translation intermediates of 15-25 kDa were detected in both plastid populations. Pulse-chase assays showed that the 15- to 25-kDa D1 translation products were precursors of mature D1 in plastids of illuminated plants. In contrast, in plastids of dark-grown plants, the 15- to 25-kDa translation intermediates were converted into a 23-kDa polypeptide previously suggested to be a proteolytic product of D1. These results indicate that chlorophyll produced in illuminated plants stabilizes D1 nascent polypeptides, which allows accumulation of mature D1.

Apoproteins↗
PubMed1970

The photosynthetic response to a shift in the chlorophyll a to chlorophyll B ratio of chlorella.

The chlorophyll a:b ratio was shifted in Chlorella vannielii by varying the illuminance under which the cells were cultured-the ratio increased from 2.9, 3.0, 4.0, and 4.8 to 6.2, respectively, at 100, 300, 900, 2,700 and 6,000 foot candles. The 6,000-foot candle cells retained an optimal growth rate at the chlorophyll a:b ratio of 6.2 which was the upper limit of normal growth. Comparisons were made between the 300-and 6,000-foot candle cultures to determine the significance to the photosynthetic mechanism of a shift in the chlorophyll a:b ratio.The high light cells (6,000 foot candles) contained only one-tenth the total amount of chlorophyll of the low light cells (300 foot candles) based on dry weight. The total chlorophyll per cell of the high light cells was one-fifth of that in the low light cells. Electron micrographs indicated differences in chloroplast structure. An average of five or six thylakoids composed a granum-like region of the low light chloroplasts, whereas only a pair of thylakoids at most was found in the high light chloroplasts. The high light chloroplasts had more starch. On a dry weight basis, the high light cells had a respiration rate 3 times that of the low light cells. Based on chlorophyll, the respiration rate of the high light cells was 26 times greater. Based on dry weight, the oxygen evolution for both cultures was essentially the same at 6,000 foot candles; however, at 300 foot candles the rate for the low light cells was about 5 times faster than that of the high light cells. With chlorophyll as the index, the rates of the high light cells were higher than those of the low light cells-7 times faster at 6,000 and 2 times faster at 300 foot candles. At 10,000 foot candles, the low light-grown cells underwent photooxidation, whereas the high light grown cells photosynthesized at a rate slightly higher than at 6,000 foot candles.Action spectra of system II (oxygen evolution) from a modulated polarograph indicated photochemical participation of chlorophyll b in the high light deficient cells, although the participation was much less than in the low light cells. Enhancement was 1.11 for the low light cells, and 1.05 for the high light cells.In order to account for the energy balance in the two cultures it was concluded that perhaps oxidative phosphorylation supplemented a reduced photophosphorylation in the high light cells. Experiments with peroxyacetyl nitrate support the view that cyclic photophosphorylation is less in the chlorophyll b-deficient cells. Chlorophyll b served also to broaden absorption for the photosynthetic unit-a detrimental role when cells are illuminated above saturation.

Journal Article↗
PubMed2002

Photostabilized chlorophyll a in mesoporous silica: adsorption properties and photoreduction activity of chlorophyll a.

Chlorophyll a was adsorbed to mesoporous silica (FSM, folded-sheet mesoporous material) to form a chlorophyll-FSM conjugate, in which a nanometer-scale interaction between chlorophyll a molecules resembles a living plant leaf. The mesopores of FSM acted as nanoscale spaces not only for an interaction between chlorophyll molecules and the silica support but also for a nanoscale interaction between the absorbed chlorophyll molecules. These interactions contribute to photostability. An increase in the amount of chlorophyll adsorbed to the pores of FSM leads to an enhancement of the photostability accompanied by a shift in the absorbance maximum to a longer wavelength. The physiological function of the chlorophyll-FSM conjugate was explored as chlorophyll-FSM exhibited the photoinduced ability to catalyze the reduction of methyl viologen (an electron carrier). The evolution of hydrogen gas was observed for 14 h without deterioration when an aqueous suspension containing chlorophyll-FSM, methyl viologen, 2-mercaptoethanol (an electron donor), and platinum was illuminated with visible light.

Adsorption↗
PubMed1996

Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 by chlorophyll a or Zn-pheophytin a.

Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 against proteolytic degradation has been investigated through in vitro synthesis of chlorophyll a or Zn-pheophytin a in intact etioplasts from barley. Stabilization of the apoproteins was dependent on the concentration of chlorophyll a or Zn-pheophytin a. Zn-pheophytin a was superior to chlorophyll a with respect to the concentration of pigment required for an equal yield of the stabilized chlorophyll a protein CP47, CP43, and P700 and for the total yield of chlorophyll a proteins. Zn-pheophytin a was most efficient for stabilizing CP47 and, at an increased concentration, efficient for stabilizing CP43, P700, and D1. Stabilization of apoproteins was highest after de novo synthesis of 90-300 pmol of Zn-pheophytin a or of about 400-600 pmol of chlorophyll a/4.2 x 10(7) etioplasts. The yield of stabilized chlorophyll proteins decreased at higher concentrations of Zn-pheophytin a, but was unaffected by higher concentrations of chlorophyll a.

Apoproteins↗
PubMed1979

Resolution of the light-harvesting chlorophyll a/b-protein of vicia faba chloroplasts into two different chlorophyll-protein complexes.

Thylakoids of Vicia faba chloroplasts disaggregated by sodium dodecyl sulfate were separated by means of different electrophoretic systems. Under the conditions of a high resolving gel system the chlorophyll containing zone previously termed chlorophyll-protein complex II or light-harvesting chlorophyll a/b-protein was found to be inhomogeneous. It represents a mixture of two distinct chlorophyll-proteins characterized by different spectral properties and different apoproteins. One chlorophyll-protein exhibits a chlorophyll a/b ratio of 0.9 and is associated with polypetides of 24,000 and 23,000 daltons. The 24,000 dalton band is proved to bind chlorophyll and has a light-harvesting function. The function of the 23,000 dalton band is unknown. The second chlorophyll-protein has a chlorophyll a/b ratio of 2.1 and an additional absorption maximum in the position of 637 nm. It is associated with only one polypeptide which has an apparent molecular weight of 23,000. The two 23,000 dalton polypeptides occurring in both complexes are not identical.

Chlorophyll↗
PubMed1979

Evidence for a structural role for chlorophyll in chlorophyll-protein complexes.

1. Chymotrypsin treatment of spinach chloroplast membranes does not change the electrophoretic mobility of either chlorophyll-protein complex 1 or 2. 2. The extraction of lipids with 80% acetone after treatment of the membranes with chymotrypsin reveals that the polypeptide components of both chlorophyll-protein complexes had been extensively digested. The extraction of carotenes with petroleum ether under the same conditions does not change the electrophoretic mobility of the chlorophyll-protein complexes. 3. Fluorescence polarisation studies of chlorophyll-protein complex 2 reveal that the chymotrypsin digestion of this complex does not result in changes of mutual orientation or distance apart of chlorophyll a, chlorophyll b or carotenoid. 4. Two polypeptide components have been detected after lipid extraction of electrophoretically purified chlorophyll-protein complexes 1 and 2. The SDS molecular weights are 24 000 and 27 000 for complex 2, and 68 000 and 64 000 for complex 1. 5. We conclude that chlorophyll performs an important structural function in both chlorophyll-protein complexes.

Chlorophyll↗
PubMed2003

Relationships between leaf chlorophyll content and spectral reflectance and algorithms for non-destructive chlorophyll assessment in higher plant leaves.

Leaf chlorophyll content provides valuable information about physiological status of plants. Reflectance measurement makes it possible to quickly and non-destructively assess, in situ, the chlorophyll content in leaves. Our objective was to investigate the spectral behavior of the relationship between reflectance and chlorophyll content and to develop a technique for non-destructive chlorophyll estimation in leaves with a wide range of pigment content and composition using reflectance in a few broad spectral bands. Spectral reflectance of maple, chestnut, wild vine and beech leaves in a wide range of pigment content and composition was investigated. It was shown that reciprocal reflectance (R lambda)-1 in the spectral range lambda from 520 to 550 nm and 695 to 705 nm related closely to the total chlorophyll content in leaves of all species. Subtraction of near infra-red reciprocal reflectance, (RNIR)-1, from (R lambda)-1 made index [(R lambda)(-1)-(RNIR)-1] linearly proportional to the total chlorophyll content in spectral ranges lambda from 525 to 555 nm and from 695 to 725 nm with coefficient of determination r2 > 0.94. To adjust for differences in leaf structure, the product of the latter index and NIR reflectance [(R lambda)(-1)-(RNIR)-1]*(RNIR) was used; this further increased the accuracy of the chlorophyll estimation in the range lambda from 520 to 585 nm and from 695 to 740 nm. Two independent data sets were used to validate the developed algorithms. The root mean square error of the chlorophyll prediction did not exceed 50 mumol/m2 in leaves with total chlorophyll ranged from 1 to 830 mumol/m2.

Algorithms↗
PubMed2005

Chlorophyll biomass in the global oceans: airborne lidar retrieval using fluorescence of both chlorophyll and chromophoric dissolved organic matter.

For three decades airborne laser-induced fluorescence has demonstrated value for chlorophyll biomass retrieval in wide-area oceanic field experiments, satellite validation, and algorithm development. A new chlorophyll biomass retrieval theory is developed using laser-induced and water Raman normalized fluorescence of both (a) chlorophyll and (b) chromophoric dissolved organic matter (CDOM). This airborne lidar retrieval theory is then independently confirmed by chlorophyll biomass obtained from concurrent (1) ship-cruise retrievals, (2) satellite inherent optical property (IOP) biomass retrievals, and (3) satellite standard band-ratio chlorophyll biomass retrievals. The new airborne lidar chlorophyll and CDOM fluorescence-based chlorophyll biomass retrieval is found to be more robust than prior lidar methods that used chlorophyll fluorescence only. Future research is recommended to further explain the underlying influence of CDOM on chlorophyll production.

Algorithms↗
PubMed1992

Regulation of chlorophyll apoprotein expression and accumulation. Requirements for carotenoids and chlorophyll.

Chlorophyll apoprotein accumulation and expression were examined in mutants of Chlamydomonas reinhardtii blocked at specific steps of carotenoid or chlorophyll synthesis. In the absence of carotenoids: 1) apoproteins of the core and light-harvesting complexes of photosystem I (CCI and LHCI, respectively) and photosystem II (CCII and LHCII, respectively) do not accumulate; 2) mRNAs for the CCI, CCII, and LHCII apoproteins accumulate to normal levels; and 3) synthesis of the chlorophyll apoproteins is differentially affected, or in some cases, not affected. In the absence of chlorophylls: 1) the apoproteins fail to accumulate; 2) mRNA levels for CCI and CCII apoproteins are relatively unchanged; 3) levels of LHCII apoprotein mRNA, but not rates of LHCII mRNA synthesis, are reduced in a light-dependent chlorophyll-synthesis mutant (ya12); and 4) synthesis of chlorophyll apoproteins is differentially affected or not affected in the case of several chloroplast-encoded apoproteins. These results demonstrate a direct role for carotenoids as well as chlorophylls in the stabilization of certain chlorophyll apoproteins and, for others, possibly in their translation. The data also indicate a role for chlorophyll synthesis in the stability of LHCII mRNA.

Animals↗