Reprint

Thioredoxin and Glutaredoxin Systems

Edited by
May 2019
280 pages
  • ISBN978-3-03897-836-7 (Paperback)
  • ISBN978-3-03897-837-4 (PDF)

This book is a reprint of the Special Issue Thioredoxin and Glutaredoxin Systems that was published in

Biology & Life Sciences
Summary

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.

Format
  • Paperback
License
© 2019 by the authors; CC BY-NC-ND license
Keywords
methionine; methionine sulfoxide; methionine sulfoxide reductase; physiological function; protein; plant; repair; redox homeostasis; signaling; stress; mitochondria; thioredoxin; iron–sulfur cluster; redox regulation; ALAD; tetrapyrrole biosynthesis; redox control; thioredoxins; posttranslational modification; chlorophyll; redox regulation; thioredoxin; ferredoxin-thioredoxin reductase; chloroplast; H2O2; redox signalling; development; regeneration; adult stem cells; metazoan; cyanobacteria; thioredoxin; photosynthesis; redox active site; thioredoxin; disulfide; flavin; NADPH; X-ray crystallography; SAXS; methanoarchaea; chilling stress; cold temperature; posttranslational modification; regulation; ROS; thiol redox network; thioredoxin; thioredoxin; Calvin-Benson cycle; photosynthesis; carbon fixation; chloroplast; macromolecular crystallography; protein-protein recognition; electrostatic surface; Chlamydomonas reinhardtii; thioredoxin; glutaredoxin; legume plant; symbiosis; redox homeostasis; stress; thioredoxin; monodehydroascorbate reductase; water stress; protein oxidation; antioxidants; ascorbate; glutathione; wheat; thioredoxin; thioredoxin reductase; baking; redox; dough rheology; protein oxidation; methionine oxidation; methionine sulfoxide reductases; oxidized protein repair; ageing; Chlamydomonas reinhardtii; cysteine alkylation; cysteine reactivity; MALDI-TOF mass spectrometry; thioredoxin; X-ray crystallography; Isocitrate dehydrogenase; glutathionylation; nitrosylation; glutaredoxin; Arabidopsis thaliana; thioredoxins; plastidial; specificity; function; proteomic; photosynthesis; Calvin cycle; n/a