chlorophyll-a and magnesium-protoporphyrin

chlorophyll-a has been researched along with magnesium-protoporphyrin* in 15 studies

Other Studies

15 other study(ies) available for chlorophyll-a and magnesium-protoporphyrin

ArticleYear
Effects of iron deficiency and exogenous sucrose on the intermediates of chlorophyll biosynthesis in Malus halliana.
    PloS one, 2020, Volume: 15, Issue:5

    Malus halliana is an iron (Fe)-efficient apple rootstock growing in calcareous soil that shows obvious 'greenness' traits during Fe deficiency. Recent studies have shown that exogenous sugars can be involved in abiotic stress. To identify the key regulatory steps of chlorophyll (Chl) biosynthesis in M. halliana under Fe deficiency and to verify whether exogenous sucrose (Suc) is involved in Fe deficiency stress, we determined the contents of the Chl precursor and the expression of several Chl biosynthetic genes in M. halliana. The results showed that Fe deficiency caused a significant increase in the contents of protoporphyrin IX (Proto IX), Mg-protoporphyrin IX (Mg-Proto IX) and protochlorophyllide (Pchlide) in M. halliana compared to the Fe-sensitive rootstock Malus hupehensis. Quantitative real-time PCR (RT-qPCR) also showed that the expression of protoporphyrinogen oxidase (PPOX), which synthesizes Proto IX, was upregulated in M. halliana and downregulated in M. hupehensis under Fe deficiency. Exogenous Suc application prominently enhanced the contents of porphobilinogen (PBG) and the subsequent precursor, whereas it decreased the level of δ-aminolaevulinic acid (ALA), suggesting that the transformation from ALA to PBG was catalyzed in M. halliana. Additionally, the transcript level of δ-aminolevulinate acid dehydratase (ALAD) was noticeably upregulated after exogenous Suc treatment. This result, combined with the precursor contents, indicated that Suc accelerated the steps of Chl biosynthesis by modulating the ALAD gene. Therefore, we conclude that PPOX is the key regulatory gene of M. halliana in response to Fe deficiency. Exogenous Suc enhances M. halliana tolerance to Fe deficiency stress by regulating Chl biosynthesis.

    Topics: Chlorophyll; Iron; Malus; Protochlorophyllide; Protoporphyrins; Sucrose

2020
Eliminating interference by anthocyanins when determining the porphyrin ratio of red plant leaves.
    Journal of photochemistry and photobiology. B, Biology, 2018, Volume: 187

    Anthocyanins (Ants) are water-soluble secondary metabolites that are responsible for red colour of plant leaves. To determine photosynthetic pigments, 80% acetone was used to extract Ants from Ant-containing leaves of test plants. However, using the 80% acetone extraction method can lead to interference between chlorophylls (Chls) and Ants. Porphyrins, such as protoporphyrin IX (PPIX), Mg-protoporphyrin IX (MgPP), and protochlorophyllide (Pchlide), are Chl biosynthetic intermediates and demonstrate photospectrometric characteristics similar to those of Chl. Although the ether/water extraction method was able to remove Ants interference when detecting porphyrins, the porphyrins extraction efficiency was lower than that of the 80% acetone extraction method. Low Ants levels interfered with individual porphyrin ratios, and the extent of the effect was correlated with Ants concentrations. We developed the three equations could eliminate interference by Ants when determining the porphyrin molecular percentage (%) and were comprehensively applied to all tested species of Ants-containing leaves.

    Topics: Anthocyanins; Chlorophyll; Color; Ipomoea batatas; Plant Leaves; Porphyrins; Protochlorophyllide; Protoporphyrins

2018
Bisphenol A effects on the chlorophyll contents in soybean at different growth stages.
    Environmental pollution (Barking, Essex : 1987), 2017, Volume: 223

    Bisphenol A (BPA), a suspected endocrine disruptor, can modify normal plant growth and development. Photosynthesis provides material and energy for the growth and development of plants, in which chlorophyll (Chl) plays a significant role. Many studies have shown that the growth and metabolism of plants vary at different growth stages. Thus the sensitivity of plant's responses to environmental pollution is correspondingly different. We studied the effects of BPA on the Chl contents of soybean (Glycine Max L.) at different growth stages (seedling, flowering and podding, seed-filling and maturation) by measuring the contents of essential intermediates (5-aminolevulinic acid, porphobilinogen, protoporphyrin IX, magnesium protoporphyrin and protochlorophyll) and the activities of key enzymes (5-aminolaevulinic acid dehydratase, porphobilinogen deaminase, uroporphyrinogen III synthase, magnesium chelatase) in chlorophyll synthesis. Low-dose (1.5 mg/L) BPA exposure increased the activities of key enzymes in addition to the contents of intermediates in Chl synthesis at different growth stages, resulting in increases in Chl contents and net photosynthetic rate. In contrast, medium and high-dose (17.2, 50.0 mg/L) BPA exposure produced inhibitory effects on the indices. Following the withdrawal of BPA exposure, the indices recovered to a degree that was related to the plant growth stage. The effect level (high to low) of BPA on these indices at different growth stages was: seedling stage > maturation stage > flowering and podding stage > seed-filling stage. The reverse effect was observed following the withdrawal of BPA exposure. The responses of key enzymes in plant Chl synthesis to BPA illustrate how BPA affects Chl contents. The effects of BPA show clear differences at different plant growth stages.

    Topics: Benzhydryl Compounds; Biosynthetic Pathways; Chlorophyll; Endocrine Disruptors; Environmental Pollutants; Flowers; Glycine max; Phenols; Protoporphyrins; Seedlings; Seeds

2017
Effects of bisphenol A on chlorophyll synthesis in soybean seedlings.
    Environmental science and pollution research international, 2015, Volume: 22, Issue:8

    Bisphenol A (BPA), as an emerging environmental pollutant, is potentially harmful to plant growth. Chlorophyll (Chl) is critical in photosynthesis that provides matter and energy for plant growth. How BPA affects the chlorophyll content remains largely unknown. Here, the effects of BPA on Chl synthesis in soybean seedlings were investigated. Exposure to 1.5 mg/L BPA decreased the 5-aminolevulinic acid (ALA) content and increased protoporphyrin IX (Proto IX), magnesium protoporphyrin, and protochlorophyll contents and 5-aminolaevulinic acid dehydratase, porphobilinogen deaminase, uroporphyrinogen III synthase, uroporphyrinogen III decarboxylase, and protoporphyrinogen oxidase activities. Exposure to 17.2 and 50.0 mg/L BPA exerted the opposite effects on these four intermediates and five enzymes. Following the withdrawal of BPA exposure, the aforementioned parameters gradually recovered, except magnesium protoporphyrin content in exposure to 50.0 mg/L BPA. Our findings revealed that exposure to low-concentration BPA increased the Chl content in soybean seedlings through improving Chl synthesis, especially the conversion from ALA to Proto IX, whereas exposure to high-concentration BPA decreased the Chl content through inhibiting Chl synthesis, especially the conversion from ALA to Proto IX. The dual effects of BPA were largely reversed following the withdrawal of BPA exposure.

    Topics: Aminolevulinic Acid; Analysis of Variance; Benzhydryl Compounds; Biosynthetic Pathways; Chlorophyll; Environmental Pollutants; Glycine max; Hydroxymethylbilane Synthase; Phenols; Photosynthesis; Plant Leaves; Porphobilinogen Synthase; Protoporphyrinogen Oxidase; Protoporphyrins; Seedlings; Spectrometry, Fluorescence; Uroporphyrinogen Decarboxylase; Uroporphyrinogen III Synthetase

2015
LCAA, a novel factor required for magnesium protoporphyrin monomethylester cyclase accumulation and feedback control of aminolevulinic acid biosynthesis in tobacco.
    Plant physiology, 2012, Volume: 160, Issue:4

    Low Chlorophyll Accumulation A (LCAA) antisense plants were obtained from a screen for genes whose partial down-regulation results in a strong chlorophyll deficiency in tobacco (Nicotiana tabacum). The LCAA mutants are affected in a plastid-localized protein of unknown function, which is conserved in cyanobacteria and all photosynthetic eukaryotes. They suffer from drastically reduced light-harvesting complex (LHC) contents, while the accumulation of all other photosynthetic complexes per leaf area is less affected. As the disturbed accumulation of LHC proteins could be either attributable to a defect in LHC biogenesis itself or to a bottleneck in chlorophyll biosynthesis, chlorophyll synthesis rates and chlorophyll synthesis intermediates were measured. LCAA antisense plants accumulate magnesium (Mg) protoporphyrin monomethylester and contain reduced protochlorophyllide levels and a reduced content of CHL27, a subunit of the Mg protoporphyrin monomethylester cyclase. Bimolecular fluorescence complementation assays confirm a direct interaction between LCAA and CHL27. 5-Aminolevulinic acid synthesis rates are increased and correlate with an increased content of glutamyl-transfer RNA reductase. We suggest that LCAA encodes an additional subunit of the Mg protoporphyrin monomethylester cyclase, is required for the stability of CHL27, and contributes to feedback-control of 5-aminolevulinic acid biosynthesis, the rate-limiting step of chlorophyll biosynthesis.

    Topics: Amino Acid Sequence; Aminolevulinic Acid; Chlorophyll; Chlorophyll A; Conserved Sequence; Evolution, Molecular; Feedback, Physiological; Fluorescence; Gene Expression Regulation, Plant; Intramolecular Oxidoreductases; Light-Harvesting Protein Complexes; Molecular Sequence Data; Nicotiana; Oxidation-Reduction; Phenotype; Photosynthesis; Plant Proteins; Plastids; Protein Transport; Protoporphyrins; RNA, Antisense; Sequence Alignment; Tetrapyrroles

2012
Comparative functional analysis of two hypothetical chloroplast open reading frames (ycf) involved in chlorophyll biosynthesis from Synechocystis sp. PCC6803 and plants.
    Journal of plant physiology, 2011, Aug-15, Volume: 168, Issue:12

    Hypothetical chloroplast open reading frames (ycfs) are highly conserved and interspecifically occurring genes in plastomes of plants and algae with significant functions in gene expression and photosynthesis. However, the function of many ycfs is still in vain so that attention is directed to other chloroplast functions such as metabolism of co-factors, protein translocation and protection against abiotic stress. We provide a comprehensive functional description of ycf53 and ycf59, two genes involved in chlorophyll biosynthesis. While ycf59 encodes an essential enzymatic component of Mg protoporphyrin monomethylester cyclase, ycf53 encodes a posttranslational regulator of chlorophyll biosynthesis. Their roles in tetrapyrrole biosynthesis were compared by using cyanobacterial and plant mutants with modulated expression of these two genes. Our work provides indications for diverse effects of these homologous gene products in plants and cyanobacteria on tetrapyrrole biosynthesis and photosynthesis.

    Topics: Biosynthetic Pathways; Chlorophyll; Chloroplasts; Esters; Gene Knockout Techniques; Models, Biological; Open Reading Frames; Phylogeny; Plant Proteins; Plants; Protein Subunits; Protoporphyrins; Synechocystis; Tetrapyrroles

2011
Chlorophyll-deficient mutants of Chlamydomonas reinhardtii that accumulate magnesium protoporphyrin IX.
    Plant molecular biology, 2010, Volume: 72, Issue:6

    Two Chlamydomonas reinhardtii mutants defective in CHLM encoding Mg-protoporphyrin IX methyltransferase (MgPMT) were identified. The mutants, one with a missense mutation (chlM-1) and a second mutant with a splicing defect (chlM-2), do not accumulate chlorophyll, are yellow in the dark and dim light, and their growth is inhibited at higher light intensities. They accumulate Mg-protoporphyrin IX (MgProto), the substrate of MgPMT and this may be the cause for their light sensitivity. In the dark, both mutants showed a drastic reduction in the amounts of core proteins of photosystems I and II and light-harvesting chlorophyll a/b-binding proteins. However, LHC mRNAs accumulated above wild-type levels. The accumulation of the transcripts of the LHC and other genes that were expressed at higher levels in the mutants during dark incubation was attenuated in the initial phase of light exposure. No regulatory effects of the constitutively 7- to 18-fold increased MgProto levels on gene expression were detected, supporting previous results in which MgProto and heme in Chlamydomonas were assigned roles as second messengers only in the transient activation of genes by light.

    Topics: Algal Proteins; Base Sequence; Carotenoids; Chlamydomonas reinhardtii; Chlorophyll; Gene Expression Regulation; Heme; Light; Light-Harvesting Protein Complexes; Methyltransferases; Molecular Sequence Data; Mutation; Mutation, Missense; Protoporphyrins; RNA Splicing; RNA, Messenger; Tetrapyrroles

2010
Tobacco Mg protoporphyrin IX methyltransferase is involved in inverse activation of Mg porphyrin and protoheme synthesis.
    The Plant journal : for cell and molecular biology, 2005, Volume: 41, Issue:2

    Protoporphyrin, a metabolic intermediate of tetrapyrrole biosynthesis, is metabolized by Mg chelatase and ferrochelatase and is directed into the Mg-branch for chlorophyll synthesis and in the Fe-branch for protoheme synthesis respectively. Regulation of the enzyme activities at the beginning of this branchpoint ensures accurate partition of protoporphyrin, but is still not entirely understood. Transgenic tobacco plants were generated that express antisense or sense RNA for inhibited and excessive expression of Mg protoporphyrin methyltransferase (MgPMT) respectively. This enzyme accepts Mg protoporphyrin from Mg chelatase and catalyses the transfer of a methyl group to the carboxyl group of the C13-propionate side chain. Low MgPMT activity is correlated with reduced Mg chelatase activity and a low synthesis rate of 5-aminolevulinate, but with enhanced ferrochelatase activity. In contrast, high MgPMT activity leads to inverse activity profiles: high activities of Mg chelatase and for 5-aminolevulinate synthesis, but reduced activity of ferrochelatase, indicating a direct influence of MgPMT in combination with Mg chelatase on the metabolic flux of ALA and the distribution of protoporphyrin into the branched pathway. The modified enzyme activities in tetrapyrrole biosynthesis in the transgenic plants can be explained with changes of certain corresponding mRNA contents: increased 5-aminolevulinate synthesis and Mg chelatase activity correlate with enhanced transcript levels of the HemA, Gsa, and CHLH gene encoding glutamyl-tRNA reductase, glutamate-1-semialdehyde aminotransferase and a Mg chelatase subunit respectively. It is proposed that reduced and increased MgPMT activity in chloroplasts is communicated to the cytoplasm for modulating transcriptional activities of regulatory enzymes of the pathway.

    Topics: Chlorophyll; Gene Expression; Heme; Lyases; Methyltransferases; Nicotiana; Plants, Genetically Modified; Protoporphyrins; Tetrapyrroles; Transgenes

2005
Recombinant water-soluble chlorophyll protein from Brassica oleracea var. Botrys binds various chlorophyll derivatives.
    Biochemistry, 2003, Jun-24, Volume: 42, Issue:24

    A gene coding for water-soluble chlorophyll-binding protein (WSCP) from Brassica oleracea var. Botrys has been used to express the protein, extended by a hexahistidyl tag, in Escherichia coli. The protein has been refolded in vitro to study its pigment binding behavior. Recombinant WSCP was found to bind two chlorophylls (Chls) per tetrameric protein complex but no carotenoids in accordance with previous observations with the native protein [Satoh, H., Nakayama, K., Okada, M. (1998) J. Biol. Chem. 273, 30568-30575]. WSCP binds Chl a, Chl b, bacteriochlorophyll a, and the Zn derivative of Chl a but not pheophytin a, indicating that the central metal ion in Chl is essential for binding. WSCP also binds chlorophyllides a and b and even the more distant Chl precursor Mg-protoporphyrin IX; however, these pigments fail to induce oligomerization of the protein. We conclude that the phytol group in bound Chl plays a role in the formation of tetrameric WSCP complexes. If WSCP in fact binds Chl or its derivative(s) in vivo, the lack of carotenoids in pigmented WSCP raises the question of how photooxidation, mediated by triplet-excited Chl and singlet oxygen, is prohibited. We show by spin-trap electron-paramagnetic resonance that the light-induced singlet-oxygen formation of WSCP-bound Chl is lower by a factor of about 4 than that of unbound Chl. This as-yet-unknown mechanism of WSCP to protect its bound Chl against photooxidation supports the notion that WSCP may function as a transient carrier of Chl or its derivatives.

    Topics: Brassica; Carotenoids; Chlorophyll; Chlorophyllides; Circular Dichroism; DNA, Plant; Electron Spin Resonance Spectroscopy; Light; Light-Harvesting Protein Complexes; Oxidation-Reduction; Photochemistry; Photosynthetic Reaction Center Complex Proteins; Protein Folding; Protoporphyrins; Recombinant Proteins; Singlet Oxygen; Solubility; Spectrophotometry; Spin Labels; Water

2003
Root-shoot interaction in the greening of wheat seedlings grown under red light.
    Plant physiology, 1995, Volume: 107, Issue:2

    Wheat seedlings grown with roots exposed to constant red light (300-500 micromoles m-2 s-1) did not accumulate chlorophyll in the leaves. In contrast, seedlings grown with their roots shielded from light accumulated chlorophylls. Chlorophyll biosynthesis could be induced in red-light-grown chlorophyll-deficient yellow plants by either reducing the red-light intensity at the root surface to 100 micromoles m-1 s-1 or supplementing with 6% blue light. The inhibition of chlorophyll biosynthesis was due to impairment of the Mg-chelatase enzyme working at the origin of the Mg-tetrapyrrole pathway. The root-perceived photomorphogenic inhibition of shoot greening demonstrates root-shoot interaction in the greening process.

    Topics: Chlorophyll; Dose-Response Relationship, Radiation; Evaluation Studies as Topic; Germination; Light; Lighting; Lyases; Plant Leaves; Plant Roots; Plant Shoots; Protochlorophyllide; Protoporphyrins; Triticum

1995
Spectrofluorometric estimation of intermediates of chlorophyll biosynthesis: protoporphyrin IX, Mg-protoporphyrin, and protochlorophyllide.
    Analytical biochemistry, 1992, Volume: 206, Issue:1

    A highly sensitive spectrofluorometric method for quantitative estimation of certain precursors of chlorophyll biosynthesis from the mixtures of plant tetrapyrroles having overlapping fluorescence emission spectra is developed. At room temperature (293 degrees K) protoporphyrin IX is monitored from its emission maximum, 633 nm, when excited at 400 nm (E400/F633). Protochlorophyllide is estimated at 638 nm, while being excited at 440 nm (E440/F638). Mg-protoporphyrin+Mg-protoporphyrin monoester pool has emission around 589-592 nm. Therefore the integration value of the emission band that extends from 580 to 610 nm is taken to calibrate its concentration. This spectrofluorometric method designed for the determination of protoporphyrin IX, esterified and nonesterified Mg-protoporphyrin pool, and protochlorophyllide is far superior to available spectrophotometric methods and estimates as low as 1 nM concentration of plant pigments. As minute quantities of individual pigments can be quantitatively analyzed from their mixtures, this method eliminates analytical uncertainties due to recovery losses caused by chromatography. However, only dilute samples can be estimated by this spectrofluorometric method as the quantitative relation between fluorescence and concentration deviates from linearity at high, i.e., above 150 nM, concentrations of pigment to be quantified.

    Topics: Acetone; Chemistry Techniques, Analytical; Chlorophyll; Chlorophyllides; Fluorescence; Hexanes; Kinetics; Mathematical Computing; Protochlorophyllide; Protoporphyrins; Sensitivity and Specificity; Spectrometry, Fluorescence

1992
Chloroplast biogenesis: quantitative determination of monovinyl and divinyl Mg-protoporphyrins and protochlorophyll(ides) by spectrofluorometry.
    Analytical biochemistry, 1985, Aug-15, Volume: 149, Issue:1

    General equations which permit the determination of the amounts of any two closely related fluorescent compounds which can be distinguished by 77 degrees K but not by 293 degrees K spectrofluorometry have been described. This was achieved in the presence or absence of a third interfering compound, without prior separation of the fluorescent species. The adaptation of the generalized equations to the determination of the amounts of monovinyl (MV) and divinyl (DV) Mg-protoporphyrins or of MV and DV protochlorophyll(ides) in the presence or absence of Mg-Protos [Mg-protoporphyrin IX (Mg-Proto), Mg-Proto monoester, Mg-Proto diester or a mixture of those three tetrapyrroles] interference, was then demonstrated over a wide range of MV/DV tetrapyrrole proportions. These equations are likely to be very useful for the study of the intermediary metabolism of the monovinyl and divinyl chlorophyll biosynthetic routes in plants.

    Topics: Chlorophyll; Chloroplasts; Mathematics; Photosynthesis; Plants; Porphyrins; Protochlorophyllide; Protoporphyrins; Pyrroles; Spectrometry, Fluorescence; Temperature; Tetrapyrroles

1985
THE BIOSYNTHESIS OF COPROPORPHYRINOGEN, MAGNESIUM PROTOPORPHYRIN MONOMETHYL ESTER AND BACTERIOCHLOROPHYLL BY RHODOPSEUDOMONAS CAPSULATA.
    The Biochemical journal, 1963, Volume: 89

    Topics: Bacteriochlorophylls; Chlorophyll; Coproporphyrinogens; Culture Media; Esters; Glycine; Iron; Magnesium; Metabolism; Porphyrins; Protoporphyrins; Research; Rhodobacter capsulatus; Rhodopseudomonas; Succinates; Surface-Active Agents

1963
Magnesium protoporphyrin monoester and protoporphyrin monomethyl ester in chlorophyll biosynthesis.
    The Journal of biological chemistry, 1961, Volume: 236

    Topics: Chlorophyll; Porphyrins; Protoporphyrins

1961
Magnesium protoporphyrin as a precursor of chlorophyll in Chlorella.
    The Journal of biological chemistry, 1948, Volume: 175, Issue:1

    Topics: Chlorella; Chlorophyll; Protoporphyrins

1948