Palma, José M.Mateos, Rosa M.López-Jaramillo, JavierRodríguez-Ruiz, MartaGonzález-Gordo, SalvadorLechuga-Sancho, Alfonso M.Corpas, Francisco J.2022-07-042022-07-042020-05-25Palma JM, Mateos RM, López-Jaramillo J, Rodríguez-Ruiz M, González-Gordo S, Lechuga-Sancho AM, et al. Plant catalases as NO and H2S targets. Redox Biol. 2020 Jul;34:101525http://hdl.handle.net/10668/3737Catalase is a powerful antioxidant metalloenzyme located in peroxisomes which also plays a central role in signaling processes under physiological and adverse situations. Whereas animals contain a single catalase gene, in plants this enzyme is encoded by a multigene family providing multiple isoenzymes whose number varies depending on the species, and their expression is regulated according to their tissue/organ distribution and the environmental conditions. This enzyme can be modulated by reactive oxygen and nitrogen species (ROS/RNS) as well as by hydrogen sulfide (H2S). Catalase is the major protein undergoing Tyr-nitration [post-translational modification (PTM) promoted by RNS] during fruit ripening, but the enzyme from diverse sources is also susceptible to undergo other activity-modifying PTMs. Data on S-nitrosation and persulfidation of catalase from different plant origins are given and compared here with results from obese children where S-nitrosation of catalase occurs. The cysteine residues prone to be S-nitrosated in catalase from plants and from bovine liver have been identified. These evidences assign to peroxisomes a crucial statement in the signaling crossroads among relevant molecules (NO and H2S), since catalase is allocated in these organelles. This review depicts a scenario where the regulation of catalase through PTMs, especially S-nitrosation and persulfidation, is highlighted.enAtribución 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/DockingNitrationS-nitrosationPersulfidationPost-translational modificationsSignalingNitraciónSimulación del acoplamiento molecularNitrosaciónProcesamiento proteico-postraduccionalSulfuro de hidrógenoMedical Subject Headings::Organisms::Eukaryota::AnimalsMedical Subject Headings::Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Oxidoreductases::Peroxidases::CatalaseMedical Subject Headings::Organisms::Eukaryota::Animals::Chordata::Vertebrates::Mammals::Artiodactyla::Ruminants::CattleMedical Subject Headings::Persons::Persons::Age Groups::ChildMedical Subject Headings::Organisms::Eukaryota::Animals::Chordata::Vertebrates::Mammals::Primates::Haplorhini::Catarrhini::Hominidae::HumansMedical Subject Headings::Chemicals and Drugs::Inorganic Chemicals::Nitrogen Compounds::Nitrogen Oxides::Nitric OxideMedical Subject Headings::Anatomy::Cells::Cellular Structures::Intracellular Space::Cytoplasm::Cytoplasmic Structures::Organelles::Cytoplasmic Vesicles::Cytoplasmic Granules::Microbodies::PeroxisomesMedical Subject Headings::Chemicals and Drugs::Inorganic Chemicals::Nitrogen Compounds::Reactive Nitrogen SpeciesMedical Subject Headings::Chemicals and Drugs::Inorganic Chemicals::Acids::Acids, Noncarboxylic::Hydrogen SulfideMedical Subject Headings::Organisms::Eukaryota::PlantsMedical Subject Headings::Analytical, Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Models, Theoretical::Models, Molecular::Molecular Docking Simulationreview article32505768open access10.1016/j.redox.2020.1015252213-2317PMC7276441