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At least 775 records · Page 43Linked to original sources
PubMed1998

Chemoprotection by natural chlorophylls in vivo: inhibition of dibenzo[a,l]pyrene-DNA adducts in rainbow trout liver.

Naturally occurring chlorophylls (Chl) have shown anti-mutagenic activity but little is known about their chemoprotective properties in vivo. This study examined the effect of Chl on formation in vivo of DNA adducts by the potent environmental carcinogen dibenzo[a,l]pyrene (DBP), using rainbow trout as the animal model. Fingerling trout were fed diets containing 200 p.p.m. DBP alone or with one of the following preparations incorporated at 3000 p.p.m. total chlorins: purified pheophytin a (Phe a) (94%); semi-purified Chl a (77%, 23% Phe a), commercial Chl a (88%, 12% other Chl a-related compounds); crude spinach extract (53% Chl a, 19% Chl b, 14% Phe a, 9% carotenoids); commercial Cu-chlorophyllin (55% chlorins, 45% neutral salts), as a known inhibitory control. After 2 weeks dietary treatment, the animals were killed and organs were collected. Stable DBP-DNA adducts from liver were quantified after 33P-post-labeling and separation by reversed-phase HPLC. Total DBP-DNA adducts in the DBP-only group were 2.46 +/- 0.32 adducts/10(6) nucleotides. All chlorophyll treatment groups showed significantly lower adduct levels (P < 0.001, Tukey's HSD test), as follows: crude spinach extract, 0.64 +/- 0.14; semi-pure Chl a, 0.5 +/- 0.11; commercial Chl a, 1.26 +/- 0.17; Phe a, 0.95 +/- 0.01; chlorophyllin, 0.78 +/- 0.09. The various treatments suppressed DBP-DNA adducts essentially uniformly across the HPLC profile, which is consistent with complex formation and reduced carcinogen uptake as the predominant protective mechanism. The chlorophyll-mediated reduction in DBP-DNA adducts in vivo is the first demonstration of anti-genotoxic activity of these common dietary phytochemicals in any vertebrate animal model.

Animals↗
PubMed2004

Accumulation of menaquinones with incompletely reduced side chains and loss of alpha-tocopherol in rice mutants with alternations in the chlorophyll moiety.

The rice mutants M249 and M134 accumulate chlorophyllides a and b which are esterified with incompletely reduced alcohols such as geranylgeraniol, dihydrogeranylgeraniol, and tetrahydrogeranylgeraniol. Quantities of alpha-tocopherol, phylloquinone, and menaquinones in leaves of these mutants were determined by high performance liquid chromatography (HPLC) with a fluorescence detector after post-column chemical reduction to convert quinones to fluorescent quinols. Methylnaphthoquinones, varying in the reduction state of the side chain (menaquinones), were detected in leaf segments of the rice mutants on HPLC analyses with both high selectivity and sensitivity to plant quinones. Mutant M249 preferentially accumulated menaquinone, which contains tetrahydrogeranylgeraniol as its side chain. However, mutant M134 exhibited preferential accumulation of menaquinone with a geranylgeraniol side chain. In both mutants, the accumulation patterns of menaquinones with different prenyl side chains were similar to those of chlorophyll with the corresponding prenyl side chains. The content of P700, the photosystem I primary electron donor, in the wild type was greater than that of either mutant, on both a chlorophyll and a fresh weight basis. However, the ratios of total methylnaphthoquinones to P700 were similar in both the wild type and the mutants. Since no comparative large differences in photosynthetic activity exist between the wild type and the mutants, these results suggest that the hydrogenation of the methylnaphthoquinone side chain to phytol is not an essential requirement for it to function as an electron acceptor in photosystem I. On the other hand, alpha-tocopherol was detected in fully developed leaves of the wild type, but not in those of the mutants. Accumulation of menaquinones and the loss of alpha-tocopherol in mutant leaves suggest that the reduction of chlorophyll-geranylgeraniol to phytol and that of geranylgeranyl pyrophosphate to phytyl pyrophosphate are catalysed by the same enzyme.

Chlorophyll↗
PubMed2006

3-D cell-level chlorophyll fluorescence imaging of ozone-injured sunflower leaves using a new passive light microscope system.

A passive light microscope system has been developed, capable of reconstructing an extended-focus 3-D cell-level image of chlorophyll fluorescence and Phi(PSII) of intact attached leaves using a limited number of focal plane images of chlorophyll fluorescence. Using this system, the relationships between the depth of the mesophyll cells in spongy tissue and the intensity of the chlorophyll fluorescence and the Phi(PSII) were investigated in sunflower leaves exposed to 300 ppb ozone for 12 h at a PPFD of 300 micromol m(-2) s(-1) actinic light. After ozone exposure, fluorescence intensity (F) largely decreased in the cells just under the epidermal cells (within approximately 20 microm of the epidermal cells), but the sites where fluorescence intensity decreased had no relationship to the position of the stomata. By contrast, the distribution of Phi(PSII) showed no change after the ozone exposure. These findings suggest that ozone-induced inhibition occurs in the cells just under the epidermal cells by reducing the light absorption of the chloroplasts, while the operating quantum efficiency of PSII photochemistry is maintained.

Algorithms↗
PubMed1986

Marked effect of cations on the separation of spinach thylakoid chlorophyll-proteins on polyacrylamide gel electrophoresis at 0 degree C in the presence of alkanolammonium dodecyl sulfates.

The separation of spinach thylakoid chlorophyll-proteins on polyacrylamide gel electrophoresis at 0 degrees C in the presence of dodecyl sulfate is markedly influenced by the kind of surfactant cation in the media used for solubilization and electrophoresis. The mode of separation can thus be modulated through the cation selection. Three kinds of alkanolammonium dodecyl sulfates were tested and their abilities as to the dissociation of the molecular assemblies of chlorophyll-proteins were found to decrease in the following order: tris(hydroxymethyl)methylammonium, triethanolammonium and triisopropanolammonium. Comparison of the electrophoretic patterns obtained with different kinds of cation may help clarify the hierarchy of the molecular assemblies of chlorophyll-proteins.

Cations↗
PubMed2003

Chlorophyll content in eucalypt vegetation at the leaf and canopy scales as derived from high resolution spectral data.

The physiological status of forest canopy foliage is influenced by a range of factors that affect leaf pigment content and function. Recently, several indices have been developed from remotely sensed data that attempt to provide robust estimates of leaf chlorophyll content. These indices have been developed from either hand-held spectroradiometer spectra or high spectral resolution (or hyperspectral) imagery. We determined if two previously published indices (Datt 1999), which were specifically developed to predict chlorophyll content in eucalypt vegetation by remote sensing at the leaf scale, can be extrapolated accurately to the canopy. We derived the two indices from hand-held spectroradiometer data of eucalypt leaves exhibiting a range of insect damage symptoms. We also derived the indices from spectra obtained from high spectral and spatial resolution Compact Airborne Spectrographic Imager 2 (CASI-2) imagery to determine if reasonable estimates at a scale of < 1 m can be achieved. One of the indices (R 850/R 710 index, where R is reflectance) derived from hand-held spectroradiometer data showed a moderate correlation with relative leaf chlorophyll content (r = 0.59, P < 0.05) for all dominant eucalypt species in the study area. The R (850)/R (710) index derived from CASI-2 imagery yielded slightly lower correlations over the entire data set (r = 0.42, P < 0.05), but correlations for individual species were high (r = 0.77, P < 0.05). A scaling analysis indicated that the R (850)/R (710) index was strongly affected by soil and water cover types when pixels were mixed, but appeared to be invariant to changes in proportions of understory, which may limit its application.

Chlorophyll↗
PubMed2005

The FLP proteins act as regulators of chlorophyll synthesis in response to light and plastid signals in Chlamydomonas.

In photosynthetic organisms the accumulation of harmful photodynamic chlorophyll precursors is prevented because of the tight regulation of the tetrapyrrole pathway. FLU is one of the regulatory factors involved in this process in land plants. We have examined the function of a Flu-like gene (FLP) from Chlamydomonas that gives rise to two FLP transcripts through alternative splicing. These transcripts are translated into a short and a long protein that differ by only 12 amino acids but that interact differently with glutamyl-tRNA reductase, an enzyme involved in an early step of the chlorophyll biosynthetic pathway. Expression of FLPs is light-regulated at the level of RNA accumulation and splicing and is altered by mutations affecting the pathway. The relative levels of the long and short forms of FLP can be correlated with the accumulation of specific porphyrin intermediates, some of which have been implicated in a signaling chain from the chloroplast to the nucleus. Reciprocally, reduction of the FLP proteins by RNA interference leads to the accumulation of several porphyrin intermediates and to photobleaching when cells are transferred from the dark to the light. Thus the FLP proteins act as regulators of chlorophyll synthesis, and their expression is controlled by light and plastid signals.

Aldehyde Oxidoreductases↗
PubMed2005

Cellular levels of glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase do not control chlorophyll synthesis in Chlamydomonas reinhardtii.

5-Aminolevulinic acid (ALA) is the first committed universal precursor in the tetrapyrrole biosynthesis pathway. In plants, algae, and most bacteria, ALA is generated from glutamate. First, glutamyl-tRNA synthetase activates glutamate by ligating it to tRNA(Glu). Activated glutamate is then converted to glutamate 1-semialdehyde (GSA) by glutamyl-tRNA reductase (GTR). Finally, GSA is rearranged to ALA by GSA aminotransferase (GSAT). In the unicellular green alga Chlamydomonas reinhardtii, GTR and GSAT were found in the chloroplasts and were not detected in the mitochondria by immunoblotting. The levels of both proteins (assayed by immunoblotting) and their mRNAs (assayed by RNA blotting) were approximately equally abundant in cells growing in continuous dark or continuous light (fluorescent tubes, 80 micromol photons s(-1) m(-2)), consistent with the ability of the cells to form chlorophyll under both conditions. In cells synchronized to a 12-h-light/12-h-dark cycle, chlorophyll accumulated only during the light phase. However, GTR and GSAT were present at all phases of the cycle. The GTR mRNA level increased in the light and peaked about 2-fold at 2 h into the light phase, and GTR protein levels also increased and peaked 2-fold at 4 to 6 h into the light phase. In contrast, although the GSAT mRNA level increased severalfold at 2 h into the light phase, the level of GSAT protein remained approximately constant in the light and dark phases. Under all growth conditions, the cells contained significantly more GSAT than GTR on a molar basis. Our results indicate that the rate of chlorophyll synthesis in C. reinhardtii is not directly controlled by the expression levels of the mRNAs for GTR or GSAT, or by the cellular abundance of these enzyme proteins.

Aldehyde Oxidoreductases↗
PubMed1971

Chlorophyll biosynthesis in a cell-free system from higher plants.

A crude homogenate obtained from greening cucumber (Cucumis sativus, L.) cotyledons in tris-sucrose, pH 7.7, containing coenzyme A, glutathione, potassium phosphate, pH 7.7, methyl alcohol, magnesium, nicotinamide adenine dinucleotide, and adenosine triphosphate, is able to incorporate 4-(14)C-delta-aminolevulinic acid into chlorophyll a and b in the presence of oxygen. If the homogenates are prepared from etiolated cotyledons which have been exposed to light for two and one-half hours, (14)C-chlorophyll a is synthesized. However, when the homogenates are prepared from cotyledons illuminated for four and one-half hours, both (14)C-chlorophyll a and b are produced.

Carbon Isotopes↗
PubMed1998

AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: functional comparisons with Atmrp1.

Three ATP binding cassette (ABC) transporter-like activities directed toward large amphipathic organic anions have recently been identified on the vacuolar membrane of plant cells. These are the Mg-ATP-energized, vanadate-inhibitable vacuolar accumulation of glutathione S-conjugates (GS conjugates), chlorophyll catabolites, and bile acids, respectively. Although each of these activities previously had been assigned to distinct pumps in native plant membranes, we describe here the molecular cloning, physical mapping, and heterologous expression of a gene, AtMRP2, from Arabidopsis thaliana that encodes a multispecific ABC transporter competent in the transport of both GS conjugates and chlorophyll catabolites. Unlike its isoform, AtMRP1, which transports the model Brassica napus chlorophyll catabolite transporter substrate Bn-NCC-1 at low efficiency, heterologously expressed AtMRP2 has the facility for simultaneous high-efficiency parallel transport of GS conjugates and Bn-NCC-1. The properties of AtMRP2 therefore establish a basis for the manipulation of two previously identified plant ABC transporter activities and provide an explanation for how the comparable transporter in native plant membranes would be systematically mistaken for two distinct transporters. These findings are discussed with respect to the functional organization of AtMRP2, the inability of AtMRP2 and AtMRP1 to transport the model bile acid transporter substrate taurocholate (despite the pronounced sensitivity of both to direct inhibition by this agent), the differential patterns of expression of their genes in the intact plant, and the high capacity of AtMRP2 for the transport of glutathionated herbicides and anthocyanins.

ATP-Binding Cassette Transporters↗
PubMed1992

Light-independent chlorophyll biosynthesis: involvement of the chloroplast gene chlL (frxC).

The Chlamydomonas reinhardtii chloroplast gene chlL (frxC) is shown to be involved in the light-independent conversion of protochlorophyllide to chlorophyllide. The polypeptide encoded by chlL contains a striking 53% amino acid sequence identity with the bacteriochlorophyll (bch) biosynthesis bchL gene product in the photosynthetic bacterium Rhodobacter capsulatus. In a previous analysis, we demonstrated that bchL was involved in light-independent protochlorophyllide reduction, thereby implicating chlL in light-independent protochlorophyllide reduction in photosynthetic eukaryotes. To perform a functional/mutational analysis of chlL, we utilized particle gun-mediated transformation to disrupt the structural sequence of chlL at its endogenous locus in the chloroplast genome of Chlamydomonas. Transformants for which the multicopy chloroplast genome was homoplasmic for the disrupted chlL allele exhibit a "yellow-in-the-dark" phenotype that we demonstrated to be a result of the dark accumulation of protochlorophyllide. The presence of a chlL homolog in distantly related bacteria and nonflowering land plants, which are thought to be capable of synthesizing chlorophyll in the dark, was also demonstrated by cross-hybridization analysis. In contrast, we observed no cross-hybridization of a probe of chlL to DNA samples from representative angiosperms that require light for chlorophyll synthesis, in support of our conclusion that chlL is involved in light-independent chlorophyll biosynthesis. The role of chlL in protochlorophyllide reduction as well as recent evidence that both light-independent and light-dependent protochlorophyllide reductases may be of bacterial origin are discussed.

Amino Acid Sequence↗
PubMed1994

Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.

5-Aminolevulinic acid (ALA) is the universal precursor of tetrapyrroles, such as chlorophyll and heme. The major control of chlorophyll biosynthesis is at the step of ALA formation. In the chloroplasts of plants, as in Escherichia coli, ALA is derived from the glutamate of Glu-tRNA via the two-step C5 pathway. The first enzyme, Glu-tRNA reductase, catalyzes the reduction of Glu-tRNA to glutamate 1-semialdehyde with the release of intact tRNA. The second enzyme, glutamate 1-semialdehyde 2,1-aminomutase, converts glutamate 1-semialdehyde to ALA. To further examine ALA formation in plants, we isolated Arabidopsis genes that encode the enzymes of the C5 pathway via functional complementation of mutations in the corresponding genes of E. coli. The Glu-tRNA reductase gene was designated HEMA and the glutamate 1-semialdehyde 2,1-aminomutase gene, GSA1. Each gene contains two short introns (149 and 241 nucleotides for HEMA, 153 and 86 nucleotides for GSA1). The deduced amino acid sequence of the HEMA protein predicts a protein of 60 kD with substantial similarity (30 to 47% identity) to sequences derived from the known hemA genes from microorganisms that make ALA by the C5 pathway. Purified Arabidopsis HEMA protein has Glu-tRNA reductase activity. The GSA1 gene encodes a 50-kD protein whose deduced amino acid sequence shows extensive homology (55 to 78% identity) with glutamate 1-semialdehyde 2,1-aminomutase proteins from other species. RNA gel blot analyses indicated that transcripts for both genes are found in root, leaf, stem, and flower tissues and that their levels are dramatically elevated by light. Thus, light may regulate ALA, and hence chlorophyll formation, by exerting coordinated transcriptional control over both enzymes of the C5 pathway.

Aldehyde Oxidoreductases↗
PubMed1979

Chloroplast phosphoproteins. Phosphorylation of polypeptides of the light-harvesting chlorophyll protein complex.

When isolated, intact chloroplasts of pea (Pisum sativum) are incubated in the light with [32P]-orthophosphate, isotope is incorporated into several polypeptides. Among the most conspicuous phosphoproteins are two which form a very closely spaced doublet on dodecyl sulphate/polyacrylamide gels and co-electrophorese with the major polypeptide component of the light-harvesting chlorophyll a/b binding complex. Like the light-harvesting polypeptide, the phosphoprotein doublet is bound to thylakoids, sediments with the heavy particles released from thylakoids after digitonin treatment, is soluble in chloroform/methanol and has an apparent molecular weight of about 26 000. The doublet also appears in the highly purified light-harvesting chlorophyll a/b binding complex isolated from thylakoids by hydrosylapatite chromatography. I conclude that two polypeptide components of the complex are phosphorylated. One of these components may be the major light-harvesting chlorophyll a/b binding protein.

Chlorophyll↗
PubMed1980

The role of the light-harvesting chlorophyll a/b protein complex in chloroplast membrane stacking. Cation-induced aggregation of reconstituted proteoliposomes.

The major intrinsic protein from spinach chloroplast membranes, the light-harvesting chlorophyll a/b-protein complex, contains two distinct polypeptides of Mr 23,500 and 26,000 and 31% lipid by weight, comprising five diacyl lipids and seven chlorophylls, together with some carotenoids, per 26,000-Mr polypeptide. The chlorophyll a/b ratio is 1.1. Low-temperature fluorescence emission spectra of the light-harvesting complex revealed a major peak at 681 nm with a shoulder of variable intensity at 695 nm. The 695-nm emission has been correlated with a progressive aggregation of the complex into two-dimensional, semi-crystalline sheets. To determine the role of the light-harvesting complex in cation-dependent thylakoid stacking, the purified complex has been quantitatively incorporated into liposomes containing the four major chloroplast diacyl lipids using a simple freeze-thaw technique. The proteoliposomes appeared largely as unilamellar vesicles, with diameters between 0.1 and 0.8 micron. Freeze-fracture analysis showed intramembrane particles of 8-10 nm corresponding to the incorporated complex. Both monovalent and divalent cations caused an immediate aggregation of the proteoliposomes, which was reversed at low cation concentrations and was largely inhibited by prior trypsin treatment. Since lipid vesicles themselves showed none of these effects, it is concluded that surface-exposed polypeptide regions of the light-harvesting complex are directly involved in thylakoid stacking in vivo.

Cations↗
PubMed1985

Differences in chlorophyll-protein complexes and composition of polypeptides between thylakoids from bundle sheaths and mesophyll cells in maize.

Thylakoids from enzymatically separated bundle sheath and mesophyll tissue chloroplasts were examined for their chlorophyll-proteins by tube sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE). Differences were found in distribution of chlorophyll among peaks. The chlorophyll-protein a peak (CPa), considered to be the photosystem II (PSII) reaction centre by many authors, was seen to be absent in bundle sheath thylakoid samples. The slab SDS-PAGE revealed the absence of the polypeptides present in PSII preparations of chloroplast subfractions having only PSII activity. This finding confirms Anderson's hypothesis of the structure of grana and stroma thylakoids.

Chemical Phenomena↗
PubMed2004

Phytochrome-interacting factor 1 is a critical bHLH regulator of chlorophyll biosynthesis.

Photosynthetic organisms must achieve a delicate balance between the light energy absorbed by chlorophyll and their capacity to channel that energy into productive photochemical reactions. Release of excess absorbed energy in the cell can cause lethal photooxidative damage. We identified a basic helix-loop-helix (bHLH) transcription factor, designated PHYTOCHROME-INTERACTING FACTOR 1 (PIF1), that negatively regulates chlorophyll biosynthesis. pif1 mutant seedlings accumulate excess free protochlorophyllide when grown in the dark, with consequent lethal bleaching upon exposure to light. PIF1 interacts specifically with the photoactivated conformer of phytochromes A and B, suggesting a signaling pathway by which chlorophyll biosynthetic rates are tightly controlled during the critical initial emergence of seedlings from subterranean darkness into sunlight.

Arabidopsis↗
PubMed1968

Studies of chlorophyll-lipid-water systems.

Preliminary studies of the electronic absorption spectra of chlorophyll molecules in aqueous glycolipid and phospholipid dispersions are reported. The spectra show a shift for the red peak of chlorophyll of some 10 millimicrons to longer wavelength compared with the spectrum of chlorophyll in ether. Photochemical studies were carried out with cytochrome c incorporated into the aqueous layers separating the lipid bilayers.

Chemical Phenomena↗
PubMed1977

Biosynthesis of chlorophyll b.

Using [14C]chlorophyll a derived from a mutant of wheat lacking chlorophyll b, spinach thylakoids from very young leaves and cucumber thylakoids of irradiated, etiolated cotyledons convert chlorophyll a to b with apparent yields of 19% and 5%, respectively.

Chlorophyll↗
PubMed1997

Genetic analysis of chlorophyll biosynthesis.

During this decade, there have been major advancements in the understanding of genetic loci involved in synthesis of the family of Mg-tetrapyrroles known as chlorophylls and bacteriochlorophylls. Molecular genetic analysis of Mg-tetrapyrrole biosynthesis was initiated by the performance of detailed sequence and mutational analysis of the photosynthesis gene cluster from Rhodobacter capsulatus. These studies provided the first detailed understanding of genes involved in bacteriochlorophyll a biosynthesis. In the short time since these studies were initiated, most of the chlorophyll biosynthesis genes have been identified by virtue of their ability to complement bacteriochlorophyll a biosynthesis mutants as well as by sequence homology comparisons. This review is centered on a discussion of our current understanding of bacterial, algal, and plant genes that code for enzymes in the Mg-branch of the tetrapyrrole biosynthetic pathway that are responsible for synthesis of chlorophylls and bacteriochlorophylls.

Chlorophyll↗