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1.
Bioorg Chem ; 94: 103383, 2020 01.
Article in English | MEDLINE | ID: mdl-31699394

ABSTRACT

A mixture of pheophytins-a/a', metal-free forms of photosynthetically active chlorophyll(Chl)s-a/a' bearing the 132-methoxycarbonyl group, was substituted at the C132-position by bimolecular nucleophilic substitution with methyl bromoacetate or Michael addition with methyl acrylate, followed by C132-demethoxycarbonylation and magnesium insertion at the central position, to afford Chl-a/a' homologs possessing a methoxycarbonylmethyl or 2-methoxycarbonylethyl group at the C132-position, respectively. These C132-methylene- and ethylene-inserted homologs were characterized by 1D/2D 1H NMR spectroscopy, and the optical properties of their C132-epimerically pure samples are investigated using visible absorption, fluorescence emission, and circular dichroism spectroscopies. The stereochemistry at the C132-chiral center of these Chl-a/a' homologs was not inverted in a basic solution, and the Chl-a homologs were effective for the substrates for the chlorophyllase reaction, hydrolysis of the phytyl ester.


Subject(s)
Chlorophyll A/chemistry , Chlorophyll/analogs & derivatives , Carboxylic Ester Hydrolases/chemistry , Carboxylic Ester Hydrolases/metabolism , Chenopodium album/enzymology , Chlorophyll/chemical synthesis , Chlorophyll/chemistry , Chlorophyll/metabolism , Chlorophyll A/chemical synthesis , Chlorophyll A/metabolism , Molecular Conformation , Stereoisomerism
2.
Pest Manag Sci ; 74(12): 2874-2883, 2018 Dec.
Article in English | MEDLINE | ID: mdl-29790263

ABSTRACT

BACKGROUND: Herbicide hormesis may play a role in the evolution of weed resistance by increasing resistance selection. A standard herbicide rate may be subtoxic to resistant plants and make them more fit than untreated plants. If this increase in fitness is ultimately expressed in reproductive traits, resistance genes can accumulate more rapidly and exacerbate resistance evolution by magnifying the selection differential between resistant and sensitive plants. The hypothesis of hormetically enhanced reproductive fitness was studied for a photosystem II (PSII) target-site resistant (TSR) biotype of Chenopodium album exposed to the triazinone metamitron in comparison with its wild-type. RESULTS: Both biotypes showed an initial hormetic growth increase at different doses leading to fitness enhancements of between 19% and 61% above untreated plants. However, hormetic effects only resulted in higher fitness at maturity in resistant plants with a maximum stimulation in seed yield of 45% above untreated plants. Applying realistic metamitron rates, reproductive fitness of resistant plants was increased by 15-32%. CONCLUSIONS: Agronomically relevant doses of metamitron induced considerable hormesis in a PSII-TSR C. album genotype leading to enhanced relative fitness through reproductive maturity. This increase in relative fitness suggests an impact on resistance selection and can compensate for the oft-reported fitness costs of the mutation studied. Field rates of herbicides can, thus, not only select for resistant plants, but also enhance their reproductive fitness. The finding that herbicide hormesis can be eco-evolutionary important may have important implications for understanding the evolution of herbicide resistance in weeds. © 2018 Society of Chemical Industry.


Subject(s)
Chenopodium album/drug effects , Chenopodium album/genetics , Evolution, Molecular , Herbicide Resistance/genetics , Hormesis , Photosystem II Protein Complex/genetics , Weed Control , Chenopodium album/enzymology , Chenopodium album/physiology , Plant Roots/drug effects , Plant Roots/genetics , Reproduction/drug effects , Reproduction/genetics
3.
Pest Manag Sci ; 70(2): 278-85, 2014 Feb.
Article in English | MEDLINE | ID: mdl-23576399

ABSTRACT

BACKGROUND: Resistance of Chenopodium album to triazinones and triazines can be caused by two amino acid exchanges, serine-264-glycine (Ser(264) Gly) and alanine-251-valine (Ala(251) Val), in the chloroplast D1 protein. This paper describes the identification of a biotype with a leucine-218-valine (Leu(218) Val) switch found in German sugar beet fields with unsatisfactory weed control. A greenhouse experiment has been performed to compare the resistance profile of the newly identified biotype with biotypes that carry the Ser(264) Gly and Ala(251) Val mutations. RESULTS: Application rate-response curves obtained from the greenhouse experiment showed that the Leu(218) Val exchange induced significant resistance against the triazinones but not against terbuthylazine. The level of resistance against the triazinones was higher in the Ser(264) Gly and Ala(251) Val biotypes compared with the Leu(218) Val biotype. All biotypes tested were more resistant to metribuzin than to metamitron. Following terbuthylazine treatment, Ser264 Gly displayed a high level of resistance, Ala(251) Val showed moderate resistance. A PCR-RFLP assay for Ser(264) Gly has been extended to include detection of Ala251 Val and Leu(218) Val mutations. CONCLUSION: The D1 Leu(218) Val substitution in C. album confers significant resistance to triazinones. This suggests that Leu(218) Val is involved in the binding of triazinones. First establishment of the resistance profiles of the three psbA mutations suggests that these mutations have been independently selected.


Subject(s)
Amino Acid Substitution , Chenopodium album/enzymology , Chenopodium album/genetics , Herbicide Resistance/genetics , Mutation , Photosystem II Protein Complex/chemistry , Photosystem II Protein Complex/genetics , Binding Sites , Chenopodium album/drug effects , Environment, Controlled , Enzyme Inhibitors/metabolism , Enzyme Inhibitors/toxicity , Herbicides/metabolism , Herbicides/toxicity , Photosystem II Protein Complex/antagonists & inhibitors , Polymerase Chain Reaction , Polymorphism, Restriction Fragment Length , Restriction Mapping
4.
Biochem Biophys Res Commun ; 412(4): 522-5, 2011 Sep 09.
Article in English | MEDLINE | ID: mdl-21763282

ABSTRACT

Thermal stability of antioxidant defense enzymes superoxide dismutase (SOD, EC 1.15.1.1) and ascorbate peroxidase (APX, EC 1.11.1.11) was studied in chloroplasts and mitochondria of leaf and inflorescence in heat adaptive weed Chenopodium album. Leaf samples were taken in March (31°C/14°C) and young inflorescence (INF) was sampled at flowering in April (40°C/21°C). Leaf and INF chloroplast and mitochondrial fractions were subjected to elevated temperatures in vitro (5-100°C) for 30'. SOD and APX showed activity even after boiling treatment in both chloroplast and mitochondria of leaf and INF. SOD was more heat stable than APX in both chloroplasts and mitochondria in both the tissues. Chloroplast contained more heat stable SOD and APX isozymes than mitochondria in both leaf and INF. To the best of our knowledge this is the first report showing presence of thermostable APX isozymes (100°C for 30') in chloroplasts and mitochondria in C. album. Heat stable isozymes of SOD and APX in chloroplasts and mitochondria in leaves and inflorescence may contribute to heat tolerance in C. album.


Subject(s)
Ascorbate Peroxidases/chemistry , Chenopodium album/enzymology , Chloroplasts/enzymology , Hot Temperature , Mitochondria/enzymology , Plant Proteins/chemistry , Superoxide Dismutase/chemistry , Enzyme Stability , Heat-Shock Response , Inflorescence/enzymology , Isoenzymes/chemistry , Plant Leaves/enzymology
5.
Plant Cell Physiol ; 44(1): 96-101, 2003 Jan.
Article in English | MEDLINE | ID: mdl-12552153

ABSTRACT

Chlorophyllases (Chlases), cloned so far, contain a lipase motif with the active serine residue of the catalytic triad of triglyceride lipases. Inhibitors specific for the catalytic serine residue in serine hydrolases, which include lipases effectively inhibited the activity of the recombinant Chenopodium album Chlase (CaCLH). From this evidence we assumed that the catalytic mechanism of hydrolysis by Chlase might be similar to those of serine hydrolases that have a catalytic triad composed of serine, histidine and aspartic acid in their active site. Thus, we introduced mutations into the putative catalytic residue (Ser162) and conserved amino acid residues (histidine, aspartic acid and cysteine) to generate recombinant CaCLH mutants. The three amino acid residues (Ser162, Asp191 and His262) essential for Chlase activity were identified. These results indicate that Chlase is a serine hydrolase and, by analogy with a plausible catalytic mechanism of serine hydrolases, we proposed a mechanism for hydrolysis catalyzed by Chlase.


Subject(s)
Carboxylic Ester Hydrolases/metabolism , Serine Endopeptidases/metabolism , Amino Acid Sequence , Aspartic Acid/genetics , Binding Sites/genetics , Carboxylic Ester Hydrolases/antagonists & inhibitors , Carboxylic Ester Hydrolases/genetics , Catalysis , Chenopodium album/enzymology , Chenopodium album/genetics , Enzyme Inhibitors/pharmacology , Histidine/genetics , Hydrolysis , Isoflurophate/pharmacology , Lipase/metabolism , Molecular Sequence Data , Morpholines/pharmacology , Mutagenesis, Site-Directed , Mutation , Phenylmethylsulfonyl Fluoride/pharmacology , Sequence Homology, Amino Acid , Serine/genetics , Serine Endopeptidases/drug effects , Serine Endopeptidases/genetics , p-Chloromercuribenzoic Acid/pharmacology
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