05206nam 22013693a 450 991034667130332120250203235426.09783038978374303897837X10.3390/books978-3-03897-837-4(CKB)4920000000094954(oapen)https://directory.doabooks.org/handle/20.500.12854/60894(ScCtBLL)e0c9ea8b-0a2b-4a34-91c7-03e4a16b337b(OCoLC)1117848127(oapen)doab60894(EXLCZ)99492000000009495420250203i20192019 uu engurmn|---annantxtrdacontentcrdamediacrrdacarrierThioredoxin and Glutaredoxin SystemsMirko Zaffagnini, Jean-Pierre JacquotMDPI - Multidisciplinary Digital Publishing Institute2019Basel, Switzerland :MDPI,2019.1 electronic resource (280 p.)9783038978367 3038978361 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.Biology, life sciencesbicsscregenerationposttranslational modificationH2O2chilling stressthioredoxin reductaseX-ray crystallographyphotosynthesisChlamydomonas reinhardtiiproteinmonodehydroascorbate reductasemethionine sulfoxidecysteine reactivitysymbiosisplantMALDI-TOF mass spectrometrythioredoxinsredox homeostasismethionine sulfoxide reductasesredoxredox signallingchloroplastprotein-protein recognitioncyanobacteriaspecificitywheatmethanoarchaeastressredox regulationdough rheologymethionine sulfoxide reductaseelectrostatic surfaceCalvin cycleALADmetazoanArabidopsis thalianabakingcold temperaturemacromolecular crystallographyprotein oxidationfunctionmethionine oxidationdevelopmentiron-sulfur clustertetrapyrrole biosynthesislegume plantglutathionylationCalvin-Benson cycleadult stem cellscarbon fixationplastidialmethionineredox active siteROSwater stressNADPHrepairphysiological functionsignalingthioredoxinantioxidantsglutathioneglutaredoxinflavinIsocitrate dehydrogenasethiol redox networkageingdisulfidemitochondriachlorophyllproteomiccysteine alkylationferredoxin-thioredoxin reductaseSAXSregulationoxidized protein repairascorbateredox controlnitrosylationBiology, life sciencesZaffagnini Mirko1311267Jacquot Jean-PierreScCtBLLScCtBLLBOOK9910346671303321Thioredoxin and Glutaredoxin Systems3030074UNINA