Thioredoxin and Glutaredoxin Systems
Zaffagnini, Mirko
Thioredoxin and Glutaredoxin Systems - MDPI - Multidisciplinary Digital Publishing Institute 2019 - 1 electronic resource (280 p.)
Open Access
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.
Creative Commons
English
books978-3-03897-837-4 9783038978374 9783038978367
10.3390/books978-3-03897-837-4 doi
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
Thioredoxin and Glutaredoxin Systems - MDPI - Multidisciplinary Digital Publishing Institute 2019 - 1 electronic resource (280 p.)
Open Access
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.
Creative Commons
English
books978-3-03897-837-4 9783038978374 9783038978367
10.3390/books978-3-03897-837-4 doi
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