@misc{10498/23402,
year = {2020},
month = {7},
url = {http://hdl.handle.net/10498/23402},
abstract = {Catalase 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.},
publisher = {ELSEVIER},
keywords = {Docking},
keywords = {Nitration},
keywords = {S-nitrosation},
keywords = {Persulfidation},
keywords = {Post-translational modifications},
keywords = {Signaling},
title = {Plant catalases as NO and H2S targets},
doi = {10.1016/j.redox.2020.101525},
author = {Palma, José M. and Mateos Bernal, Rosa María and López-Jaramillo, Javier and Rodríguez-Ruiz, Marta and González-Gordo, Salvador and Lechuga Sancho, Alfonso María and Corpas, Francisco J.},
}