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Membranes (Biology). --- Mitochondria. --- Chloroplast membranes.

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Plant organelles. --- Cell organelles --- Plant genetics. --- Formation. --- CHLAMYDOMONAS --- ORGANELLES --- GENETICS --- HIGHER PLANTS --- PLASTIDS --- ORGANELLE MUTATIONS --- CHLOROPLAST DNA --- PLANTS --- MITOCHONDRIAL DNA --- GENE EXPRESSION --- CYTOPLASMIC MALE STERILITY --- BIOGENESIS --- CHLOROPLASTS --- PROTEIN SYNTHESIS --- MITOCHONDRIA --- PROTEINS --- GLYOXYSOMES --- STRUCTURE --- PEROXISOMES --- REVIEWS --- EVOLUTION --- CONTROL

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Although researchers can profitably investigate heme, chlorophyll, and related tetrapyrroles in a wide range of academic and medical research programs, the handling and manipulation of these delicate compounds requires considerable skill and cross-boundary knowledge. In Heme, Chlorophyll, and Bilins: Methods and Protocols, an interdisciplinary panel of hands-on investigators overcomes these limitations by describing in detail how to work successfully with chlorophyll, heme, and bilins in biological, medical, chemical, and biochemical research. Each method is presented by a researcher who actually uses it on a daily basis and includes step-by-step instructions and pertinent tricks-of-the-trade that often make the difference between laboratory success and failure. Topics range from methods for the analysis of tetrapyrroles, heme, and hemoproteins, to the biosynthesis and the analysis of chlorophyll and bilins. Timely and highly practical, Heme, Chlorophyll, and Bilins: Methods and Protocols is a gold-standard collection of readily reproducible techniques suitable for a wide range of researchers, whether it be a clinician studying photodynamic therapy, an ecologist studying the chlorophyll composition of leaves in a tropical forest, or a cell biologist investigating the function of specific hemoproteins.

Botany. --- Plant Sciences. --- Botanical science --- Phytobiology --- Phytography --- Phytology --- Plant biology --- Plant science --- Biology --- Natural history --- Plants --- Floristic botany --- Tetrapyrroles. --- Chlorophyll. --- Heme. --- Plant pigments. --- Phytochemicals --- Pigments (Biology) --- Chromatophores --- Plastids --- Hematin --- Porphyrins --- Chloroplast pigments --- Photosynthetic pigments --- Plant photoreceptors --- Tetrapyrroles --- Pigments --- Color

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An understanding of plant diversity at both the genome and phenome level is important for both biodiversity conservation and plant breeding. Recent advances in genomics have also resulted in a growth of the subject of plant functional genomics. This book brings these areas together, by reviewing aspects of plant evolution as it relates to variation in plant genomes and associated variations in plant phenomes. Topics covered include chloroplast and mitochondrial genomes, reticulate evolution. Polyploidy, population genetics within a species, the evolution of the flower, diversity in plant cell walls and in secondary metabolism, and the importance of plant diversity in ecology and agriculture. Contributors include leading authorities from Europe, the U.S., Australia, and New Zealand.

Angiosperme --- angiosperms --- Plante sauvage --- Wild plants --- Plante de culture --- Crops --- Taxonomie --- taxonomy --- Évolution --- evolution --- phenotypes --- Génotype --- genotypes --- Nombre chromosomique --- chromosome number --- Génétique des populations --- population genetics --- Morphologie végétale --- Plant morphology --- Physiologie végétale --- Plant physiology --- Plant diversity. --- Plants --- Evolution. --- GEN Genetics & Population Genetics --- Angiospermae = Angiosperms --- chloroplast DNA --- flower evolution --- genetics --- phylogeny --- polyploidy --- reticulate evolution --- secondary metabolites --- evolution.

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This Special Issue features recent data concerning thioredoxins and glutaredoxins from various biological systems, including bacteria, mammals, and plants. Four of the sixteen articles are review papers that deal with the regulation of development of the effect of hydrogen peroxide and the interactions between oxidants and reductants, the description of methionine sulfoxide reductases, detoxification enzymes that require thioredoxin or glutaredoxin, and the response of plants to cold stress, respectively. This is followed by eleven research articles that focus on a reductant of thioredoxin in bacteria, a thioredoxin reductase, and a variety of plant and bacterial thioredoxins, including the m, f, o, and h isoforms and their targets. Various parameters are studied, including genetic, structural, and physiological properties of these systems. The redox regulation of monodehydroascorbate reductase, aminolevulinic acid dehydratase, and cytosolic isocitrate dehydrogenase could have very important consequences in plant metabolism. Also, the properties of the mitochondrial o-type thioredoxins and their unexpected capacity to bind iron–sulfur center (ISC) structures open new developments concerning the redox mitochondrial function and possibly ISC assembly in mitochondria. The final paper discusses interesting biotechnological applications of thioredoxin for breadmaking.

n/a --- regeneration --- posttranslational modification --- H2O2 --- chilling stress --- thioredoxin reductase --- X-ray crystallography --- photosynthesis --- Chlamydomonas reinhardtii --- protein --- monodehydroascorbate reductase --- methionine sulfoxide --- cysteine reactivity --- symbiosis --- plant --- MALDI-TOF mass spectrometry --- thioredoxins --- redox homeostasis --- methionine sulfoxide reductases --- redox --- redox signalling --- chloroplast --- protein-protein recognition --- cyanobacteria --- specificity --- wheat --- methanoarchaea --- stress --- redox regulation --- dough rheology --- methionine sulfoxide reductase --- electrostatic surface --- Calvin cycle --- ALAD --- metazoan --- Arabidopsis thaliana --- baking --- cold temperature --- macromolecular crystallography --- protein oxidation --- function --- methionine oxidation --- development --- iron–sulfur cluster --- tetrapyrrole biosynthesis --- legume plant --- glutathionylation --- Calvin-Benson cycle --- adult stem cells --- carbon fixation --- plastidial --- methionine --- redox active site --- ROS --- water stress --- NADPH --- repair --- physiological function --- signaling --- thioredoxin --- antioxidants --- glutathione --- glutaredoxin --- flavin --- Isocitrate dehydrogenase --- thiol redox network --- ageing --- disulfide --- mitochondria --- chlorophyll --- proteomic --- cysteine alkylation --- ferredoxin-thioredoxin reductase --- SAXS --- regulation --- oxidized protein repair --- ascorbate --- redox control --- nitrosylation --- iron-sulfur cluster