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PubMed2002

Chlorophyll b inhibits the formation of photosystem I trimer in Synechocystis sp. PCC6803.

Chlorophyllide a oxygenase (CAO) catalyzes two-step oxygenation reactions and converts chlorophyllide a to chlorophyllide b. When CAO was introduced into the Synechocystis sp. PCC6803 genome, chlorophyll b was synthesized and incorporated into P700-chlorophyll a-protein complexes. Curve analysis of photosystem I particles showed that Ca687 was decreased with a concomitant increase in Cb652 suggesting that chlorophyll b was incorporated into Ca687-binding sites. When the level of chlorophyll b was high, Ca704, which is known as red chlorophyll and photosystem I trimers were decreased. Formation of photosystem I trimers is discussed in relation to red chlorophyll and chlorophyll b accumulation.

Binding Sites↗
PubMed1983

Partial characterization of six chlorophyll a-protein complexes isolated from a blue-green alga by a nondetergent method.

The chlorophyll a-protein complexes of a blue-green alga, Phormidium luridum, are resolved in the absence of detergent, by the combination of a Sepharose 4B column and sucrose density gradient centrifugation, into six chlorophyll a-containing zones. These six complexes are termed here as F15, F25, F35, F40, F60, and F65, according to their appearance in the sucrose density gradient after centrifugation. The absorption spectra of these six isolated complexes are reported, as well as the fluorescence emission spectra at room temperature and liquid-nitrogen temperature. The F60 complex was enriched in Photosystem I, while the F35 and F40 complexes contained both Photosystem I and II. The F60 complex is the predominant band and accounts for about 49% of the total chlorophyll a of the cells. The extinction coefficient of this complex is determined to be 68.7 mM-1 cm-1 at 680 nm in 50 mM tris(hydroxymethyl)amino methane buffer at pH 8.0. In addition, the effect of the detergent, sodium dodecyl sulfate, on these spectra are also reported for comparison. The chemically induced difference spectra of F35, F40, and F60 complexes also indicate the presence of the reaction center, P700, of Photosystem I. These three complexes have been shown to contain P700 in a ratio of approximately one reaction center molecule per 100 light-harvesting chlorophyll molecules. The simple exposure of the F60 fraction to sodium dodecyl sulfate results in an "apparent" enhancement of the P700 to chlorophyll ratio to one P700 per 51 light harvesting chlorophyll. Room temperature electron spin resonance measurements of photooxidized F60 are consistent with the presence of P700 and with the chlorophyll/P700 ratio observed by chemical assay. The amino acid compositions of F60 and F65 complexes are studied. Gel electrophoresis patterns of these six isolated complexes are presented and are significantly different from those reported for detergent-treated chlorophyll-protein complexes.

Centrifugation, Density Gradient↗
PubMed1986

Isolation of an intrinsic antenna chlorophyll a-protein from the photosystem I reaction center complex of the thermophilic cyanobacterium Synechococcus sp.

A chlorophyll-protein was isolated from a Synechococcus P700-chlorophyll a-protein complex free from small subunits (CP1-e) by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis after treatment with 2% 2-mercaptoethanol and 2% SDS. In contrast to CP1-e which, when electrophoresed under denaturating conditions, showed two polypeptide bands of 62 and 60 kDa, the chlorophyll-protein contained only the 60-kDa polypeptide and hence is called CP60. The yield of CP60 was maximal with 1-2% SDS and 2-4% sulfhydryl reagents because the chlorophyll-protein was denatured at higher concentrations of the reagents. The absorption spectrum of CP60, which retained more than half of the chlorophyll alpha molecules originally associated with the 60-kDa subunit of the photosystem I reaction center complex, showed a red band maximum at 672 nm and a small absorption band around 700 nm at liquid nitrogen temperature. CP60 emitted a fluorescence band at 717 to 725 nm at 77 degrees K. The temperature dependence of the far red band of CP60 was essentially the same as that of CP1-e between 77 and 273 degrees K. No photoresponse of P700 was detected in CP60. The results suggest that the two polypeptides resolved by SDS-gel electrophoresis from CP1-e are apoproteins of two distinct chlorophyll-proteins and that CP60 represents a chlorophyll-bearing 60-kDa subunit functioning as an intrinsic antenna protein of the photosystem I reaction center complex. It will also be shown that the temperature dependence of the far red fluorescence band is not related to the photosystem I photochemistry.

Chlorophyll↗
PubMed1980

Further studies of the relationship between cation-induced chlorophyll fluorescence and thylakoid membrane stacking changes.

Salt-induced changes in thylakoid stacking and chlorophyll fluorescence do not occur with granal membranes obtained by treatment of stacked thylakoids with digitonin. In contrast to normal untreated thylakoids, digitonin prepared granal membranes remain stacked under all ionic conditions and exhibit a constant high level of chlorophyll fluorescence. However, unstacking of these granal membranes is possible if they are pretreated with either acetic anhydride or linolenic acid. Trypsin treatment of the thylakoids inhibits the salt induced chlorophyll fluorescence and stacking changes but stacking of these treated membranes does occur when the pH is lowered, with the optimum being at about pH 4.5. This type of stacking is due to charge neutralization and does not require the presence of the 2000 dalton fragment of the polypeptide associated with the chlorophyll a/chlorophyll b light harvesting complex and known to be lost during treatment with trypsin (Mullet, J.E. and Arntzen, C.J. (1980) Biochim. Biophys. Acta 589, 100-117). Using the method of 9-aminoacridine fluorescence quenching it is argued that the surface charge density, on a chlorophyll basis, of unstacked thylakoid membranes is intermediate between digitonin derived granal and stromal membranes, with granal having the lowest value. The results are discussed in terms of the importance of surface negative charges in controlling salt induced chlorophyll fluorescence and thylakoid stacking changes. In particular, emphasis is placed on a model involving lateral diffusion of different types of chlorophyll protein complex within the thylakoid lipid matrix.

Aminoacridines↗
PubMed1980

The relationship between thylakoid stacking and salt induced chlorophyll fluorescence changes.

Salt induced chlorophyll fluorescence increase and thylakoid stacking have been measured under various conditions. 1. Aging of pea chloroplasts led to a loss of salt induced chlorophyll fluorescence increase and thylakoid stacking which is suggested to be due to a decrease in membrane fluidity as measured by 1,6-diphenylhextriene fluorescence polarization. 2. The aging treatment was accompanied by a decreased in surface charge density as indicated by chloroplast electrophoretic mobility measurements. 3. Lowering of the temperature to about 0 degrees C retarded the time courses of salt induced stacking and chlorophyll fluorescence increase. 4. Like aging, addition of linolenic acid led to an inhibition of the salt induced fluorescence and stacking phenomena but in this case there was a concomitant increase in electrophoretic mobility without any detectable change in the polarization of 1,6-diphenylhextriene fluorescence. 5. Maximum stacking occurred in both aged and fresh chloroplasts in a low salt medium at about pH 4.3 and the time course for the pH induced process was rapid and relatively temperature insensitive when compared with salt induced stacking. 6. The chlorophyll a/chlorophyll b ratio was lower for salt induced 'grana' than for pH induced 'grana'. 7. The results are discussed in terms of the hypothesis that changes in the lateral interaction of membrane pigment-protein complexes underlie the salt induced chlorophyll fluorescence increase and thylakoid stacking. It is argued that electrostatic screening by cations leads to the formation of domains of low-charge, fluorescent pigment-protein complexes, seggregated from domains of high-charge, quenching complexes, resulting in a increase in chlorophyll fluorescence yield and stacking at low-charge regions on adjacent membranes. In contrast to this, it is argued that the pH induced stacking occurs because of electrostatic neutralization, a mechanism which would not be expected to induce domain formation and associated chlorophyll fluorescence changes.

Chlorophyll↗
PubMed1980

P-700 content and polypeptide profile of chlorophyll-protein complexes of spinach and barley thylakoids.

Of the six chlorophyll-protein complexes of spinach and barley resolved by mild gel electrophoresis, two were chlorophyll a-protein complexes of PS I, namely CP1a and CP1, which accounted for up to 30% of the total chlorophyll. Both of these complexes had one P-700 per 120 chlorophyll a molecules. Since spinach and barley thylakoids have some 400 chlorophyll molecules per P-700, these complexes may not have lost any of the chlorophyll associated with them in vivo. This may account for CP1a and CP1 having the characteristic low-temperature fluorescence normally associated with PS I in vivo, which is not found in complexes with low chlorophyll/P-700 ratios. Two-dimensional electrophoresis showed that all of the chlorophyll a and P-700 of CP1 was bound to 70 kilodalton polypeptides. The PS I reaction centre complex of lowest mobility, CP1a, contained CP1 and four additional low molecular weight polypeptides. The three light-harvesting complexes resolved had major 25 and 23 kilodalton polypeptides. The presumed reaction centre complex of PS II contained major 50 and 47 kilodalton polypeptides.

Chlorophyll↗
PubMed1980

Influence of lecithin liposomes on chlorophyllase-catalyzed chlorophyll hydrolysis: comparison of intramembraneous and solubilized Phaeodactylum chlorophyllase.

1.Chlorophyllase-catalyzed chlorophyll hydrolysis is greatly enhanced by the addition of divalent cations (Mg2+) combined with a reducing agent (dithiothreitol, ascorbate). A similar effect is obtained by the addition of lecithin. In the presence of lecithin, dithiothreitol has only slight or no influence on chlorophyll hydrolysis. Mg2+ eliminates the activating effect of lecithin. 2. In the absence of Mg2+ + dithiothreitol or of lecithin, Triton X-100 has a slight activating effect on chlorophyllase-catalyzed chlorophyll hydrolysis, but only at low concentrations (0.01--0.02%). In the presence of Mg2+ and dithiothreitol or of lecithin, Triton X-100 (greater than or equal to 0.02%) inhibits this reaction. 3. Whereas chlorophyllase combines with chlorophyll, no combination of chlorophyllase and lecithin could be detected. 4. Solubilized chlorophyllase is stabilized by its substrate, chlorophyll. Enzyme stabilization is eliminated by lecithin, whereas in the absence of chlorophyll, denaturation is somewhat increased by dithiothreitol. 5. No clear difference was found between the actions of intramembraneous and solubilized chlorophyllase. The results suggest that chlorophyllase is situated within membranes in such a way that the active group protrudes into the aqueous medium surrounding the membrane. 6. A hypothesis explaining the activating effects which Mg2+ combined with a reducing agent and lecithin have upon chlorophyllase-catalyzed chlorophyll hydrolysis is presented.

Chlorophyll↗
PubMed1977

Orientation of chlorophylls within chloroplasts as shown by optical and electrochromic properties of the photosynthetic membrane.

The effects on the optical properties of photosynthetic membranes caused by several types of chlorophyll differing in resonance frequency and in spatial disposition are theoretically analyzed. Using a method of moments and the linear dichroism spectrum of the lamellae, we evaluated the mean angle (phi) between the transition moment of each chlorophyll and the normal to the lamellae. We have confirmed that at about 695 nm the transition moment is in the plane of the lamellae, and outside it for chlorophyll b (phi approximately 48.6 degrees). By integrating over frequency the absorption variations affected by ionophores, we show that they may be ascribed to a Stark effect, and we analyze the dependence of this effect on the orientation of the chlorophylls. From this dependence and the degree of polarization of the Stark effect, we calculate the spatial fluctuations of the angle phi. The calculation shows that a definite value of phi corresponds to each resonance frequency of chlorophyl a found in vivo. This proves that the chlorophylls a are not oriented partly random. For chlorophylls b, on the other hand, phi may fluctuate by some 10 degrees about its mean value. The structural consequences of these results are discussed.

Chlorophyll↗
PubMed1997

Antigenotoxic activity of natural chlorophylls.

Chlorophyllin, a man-made water-soluble form of chlorophyll, is a focus of intensive studies from many laboratories for its antimutagenic and anticarcinogenic properties. Natural chlorophylls, in contrast, have been little studied in this regard. Since yellow-green vegetables are implicated to be protective against human cancers by epidemiological studies, it is important to explore the antigenotoxic properties of natural chlorophylls. Previously, we reported that a chlorophyll sample prepared from Chlorella vulgaris inhibited the mutagenicity of 3-hydroxyamino-1-methyl-5H-pyrido[4,3-b]indole, a direct-acting mutagen, in Salmonella, and that the chlorophyll also showed inhibition of wing spot formation in Drosophila induced by 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2). We have now prepared several samples of chlorophyll from spinach and chlorella, and studied their effect on the genotoxicity of 4-nitroquinoline 1-oxide (4NQO) in Drosophila. The results showed that the genotoxicity of orally given 4NQO was suppressed by simultaneous administration of the chlorophylls. The mechanisms of this inhibition are discussed.

4-Nitroquinoline-1-oxide↗
PubMed1976

Molecular topology of the photosynthetic light-harvesting pigment complex, peridinin-chlorophyll a-protein, from marine dinoflagellates.

The photosynthetic light-harvesting complex, peridinin-chlorophyll a-protein, was isolated from several marine dinoflagellates including Glenodinium sp. by Sephadex and ion-exchange chromatography. The carotenoid (peridinin)-chlorophyll a ratio in the complex is estimated to be 4:1. The fluorescence excitation spectrum of the complex indicates that energy absorbed by the carotenoid is transferred to the chlorophyll a molecule with 100% efficiency. Fluorescence lifetime measurements indicate that the energy transfer is much faster than fluorescence emission from chlorophyll a. The four peridinin molecules within the complex appear to form two allowed exciton bands which split the main absorption band of the carotenoid into two circular dichronic bands (with negative ellipticity band at 538 nm and positive band at 463 nm in the case of peridinin-chlorophyl a-protein complex from Glenodinium sp.). The fluorescence polarization of chlorophyll a in the complex at 200 K is about 0.1 in both circular dichroic excitation bands of the carotenoid chromophore. From these circular dichroic and fluorescence polarization data, a possible molecular arrangement of the four peridinin and chlorophyll molecules has been deduced for the complex. The structure of the complex deduced is also consistent with the magnitude of the exciton spliting (ca. greater than 3000 cm-1) at the intermolecular distance in the dimer pair of peridinin (ca. 12 A). This structural feature accounts for the efficient light-harvesting process of dinoflagellates as the exciton interaction lengthens the lifetime of peridinin (radiative) and the complex topology increases the energy transfer probability. The complex is, therefore, a useful molecular model for elucidating the mechanism and efficiency of solar energy conversion in vivo as well as in vitro.

Animals↗
PubMed1975

Segregation of chlorophyll a incorporated into lipid bilayers.

Absorption and fluorescence spectra are reported for chlorophyll a incorporated into a number of aqueous phospholipid dispersions. Absorption spectra show that in dipalmitoylphosphatidylcholine bilayers, monomeric and oligomeric forms of chlorophyll a are present in both the gel and liquid crystalline phases. The formation of aggregates of chlorophyll a is reflected in the fluorescence spectra by a marked concentration quenching. In bilayers conatining small proportions of chlorophyll a, a marked increase in aggregation occurs at the transition temperatures that can be detected calorimetrically. At higher concentrations (greater than 1 chlorophyll:100 lipid), the "pretransition" is abolished in the phosphatidylcholines, and the main transition is broadened, consistent with an orientation for the chlorophyll a with the chlorine ring in the head group region and the phytol chain in the fatty acid chain region of the bilayer. In mixtures of saturated and unsaturated lipids, there is no preferential segregation of the chlorophyll a into the unsaturated lipid.

Binding Sites↗
PubMed2003

Effect of harvesting and drying conditions on chlorophyll levels of soybean (Glycine max L. Merr).

Chlorophyll in soybean represents a downgrading factor for the crops. Five Brazilian cultivars were harvested between R(6) and R(8) stage of development (Fehr & Caviness scale) and dried at 25 degrees and 40 degrees C. The effect of maturity stages and two drying conditions after harvest were studied to achieve reduction of moisture and chlorophylls to acceptable levels. When seeds were dried at 25 degrees C, even harvesting at early stages of development such as R(6), the green pigments were almost degraded, and 16 ppm of chlorophyll were found at maximum, accompanied by loss of moisture. Moisture and chlorophyll declines as seed matures, but at intermediary stages (R(6)-R(7)), chlorophyll degrades first, so the rate of moisture loss should not be used to predict chlorophyll contents. At 40 degrees C, complete degradation of chlorophyll pigments is only achieved when seeds are swathed from R(7) stage up, otherwise the seed quality could be compromised. Slow drying allows almost complete removal of green pigments, even when seeds are swathed a few days before the physiological maturity stage.

Agriculture↗
PubMed2001

Design, synthesis and properties of synthetic chlorophyll proteins.

A chemoselective method is described for coupling chlorophyll derivatives with an aldehyde group to synthetic peptides or proteins modified with an aminoxyacetyl group at the epsilon-amino group of a lysine residue. Three template-assembled antiparallel four-helix bundles were synthesized for the ligation of one or two chlorophylls. This was achieved by coupling unprotected peptides to cysteine residues of a cyclic decapeptide by thioether formation. The amphiphilic helices were designed to form a hydrophobic pocket for the chlorophyll derivatives. Chlorophyll derivatives Zn-methyl-pheophorbide b and Zn-methyl-pyropheophorbide d were used. The aldehyde group of these chlorophyll derivatives was ligated to the modified lysine group to form an oxime bond. The peptide-chlorophyll conjugates were characterized by electrospray mass spectrometry, analytical HPLC, and UV/visible spectroscopy. Two four-helix bundle chlorophyll conjugates were further characterized by size-exclusion chromatography, circular dichroism, and resonance Raman spectroscopy.

Amino Acid Sequence↗
PubMed2004

Green vegetables, red meat and colon cancer: chlorophyll prevents the cytotoxic and hyperproliferative effects of haem in rat colon.

Diets high in red meat and low in green vegetables are associated with increased colon cancer risk. This association might be partly due to the haem content of red meat. In rats, dietary haem is metabolized in the gut to a cytotoxic factor that increases colonic cytotoxicity and epithelial proliferation. Green vegetables contain chlorophyll, a magnesium porphyrin structurally analogous to haem. We studied whether green vegetables inhibit the unfavourable colonic effects of haem. First, rats were fed a purified control diet or purified diets supplemented with 0.5 mmol haem/kg, spinach (chlorophyll concentration 1.2 mmol/kg) or haem plus spinach (n = 8/group) for 14 days. In a second experiment we also studied a group that received haem plus purified chlorophyll (1.2 mmol/kg). Cytotoxicity of faecal water was determined with a bioassay and colonic epithelial cell proliferation was quantified in vivo by [methyl-(3)H]thymidine incorporation into newly synthesized DNA. Exfoliation of colonocytes was measured as the amount of rat DNA in faeces. In both studies haem increased cytotoxicity of the colonic contents approximately 8-fold and proliferation of the colonocytes almost 2-fold. Spinach or an equimolar amount of chlorophyll supplement in the haem diet inhibited these haem effects completely. Haem clearly inhibited exfoliation of colonocytes, an effect counteracted by spinach and chlorophyll. Finally, size exclusion chromatography showed that chlorophyll prevented formation of the cytotoxic haem metabolite. We conclude that green vegetables may decrease colon cancer risk because chlorophyll prevents the detrimental, cytotoxic and hyperproliferative colonic effects of dietary haem.

Animals↗
PubMed1975

Chlorophylls attached to lipid and protein globules, absorption and fluorescence spectra, photo-oxidation.

The precipitation of chlorophylls upon lipid and protein globules suspended in an aqueous buffer yields a partial model of photosynthetic membranes. The absorption and fluorescence spectra of the model are investigated as well as the photo-oxidation of the chlorophylls (bleaching) by dissolved oxygen. It is shown that pigment--pigment interactions occur in such systems, by (a) the appearance of absorption bands characteristic of crystalline or highly ordered chlorophyll at high pigment concentrations, (b) the chlorophyll a-type of fluorescence of systems containing chlorophyll a and chlorophyll b where the latter is selectively excited, and (c) the kinetics of photo-oxidation which suggest that chlorophylls can only be bleached when they are dimerized.

Animals↗
PubMed1978

The plastid membranes of barley (Hordeum vulgare). Light-induced appearance of mRNA coding for the apoprotein of the light-harvesting chlorophyll a/b protein.

Illumination of dark-grown barley plants induces a massive insertion of the light-harvesting chlorophyll a/b protein into the developing thylakoid membrane. In addition to the onset of chlorophyll synthesis, light induces specifically the appearance of a prominent mRNA species which codes for a polypeptide of Mr 29500. This component was identified as a precursor of the apoprotein of the light-harvesting chlorophyll a/b protein. The precursor has an Mr larger than the authentic protein by approximately 4000. Studies of the chlorophyll-b-less mutant chlorina f2 of barley offer the first clue to the mechanism which controls the light-dependent mRNA formation. The induction of the mRNA coding for the aproprotein of the light-harvesting chlorophyll a/b protein does not seem to be linked directly to the assembly process of the light-harvesting structure and does not require chlorophyll b. It is proposed that light exerts its influence on the mRNA formation by a reaction which is different from the phototransformation of protochlorophyll(ide) to chlorophyll(ide).

Cell Membrane↗
PubMed1981

Biosynthesis of the light-harvesting chlorophyll a/b protein. Polypeptide turnover in darkness.

1. When etiolated pea seedlings were exposed to continuous light for 24 h and then returned to darkness, 38% of the chlorophyll a, 74% of the chlorophyll b and 84% of the light-harvesting chlorophyll a/b protein that had accumulated under illumination proved to be unstable in darkness. The unstable chlorophyll displayed a half-life of about 90 min. In contrast, alpha and beta subunits of the chloroplast coupling factor and the large and small subunits of ribulose 1,5-biphosphate carboxylase continued to accumulate in darkness, although at a slower rate than in plants maintained under light. 2. Short-term labelling in vivo with L-[35S]methionine showed that leaves continued to synthesize the light-harvesting protein and the small subunit of ribulose 1,5-biphosphate carboxylase for up to 48 h after transfer of plants from light and darkness. However, after long-term labelling (16 h), the light-harvesting chlorophyll a/b protein was found to be labelled to high specific activity only in illuminated leaves. 3. I conclude that the light-harvesting chlorophyll a/b protein is subject to turnover after transfer of plants from light to darkness. The site of breakdown appears to be the photosynthetic membrane. I suggest that turnover of the protein is part of the normal physiological mechanism for co-ordinating the accumulation of the pigment and protein components of the light-harvesting chlorophyll a/b complex.

Chlorophyll↗
PubMed1987

Purification and characterization of a light-harvesting chlorophyll-a/b-protein of photosystem I of Lemna gibba.

The photosystem I (PSI) complex of Lemna gibba, isolated by deriphat/polyacrylamide gel electrophoresis of thylakoids solubilized in glycosidic surfactants, has been fractionated into its two chlorophyll-protein complexes: a core component (CCI) and a light-harvesting component (LHCI), using either non-denaturing gel electrophoresis or ion-exchange chromatography/sucrose gradient centrifugation. Both methods yielded an LHCI component that contained only one apoprotein of approximately 20 kDa. All the chlorophyll b and lutein of the PSI complex is associated with this LHCI preparation. The chlorophyll a/b ratio of this chlorophyll-protein is 2.5, and lutein is essentially the only carotenoid present. While the purified LHCI from Lemna cross-reacts with antibodies raised against spinach LHCPIb of Lam et al. [FEBS Lett. 168, 10-14 (1984)], no cross-reactivity occurred between it and the major light-harvesting chlorophyll-a/b-protein of PSII, LHCII beta. This and a comparison of the amino acid and pigment compositions of the apoproteins of the LHCI and LHCII beta chlorophyll-proteins indicate that these are two distinct but similar chlorophyll-proteins.

Amino Acids↗