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Title

Plant catalases as NO and H2S targets

AuthorsPalma Martínez, José Manuel; Mateos, R.M.; López-Jaramillo, Javier; Rodríguez-Ruiz, Marta; González-Gordo, Salvador; Lechuga-Sancho, A. M.; Corpas, Francisco J.
KeywordsDocking
Nitration
S-nitrosation
Persulfidation
Post-translational modifications
Signaling
Issue Date2020
PublisherElsevier
CitationRedox Biology 34: 101525 (2020)
AbstractCatalase 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 (HS). 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 HS), 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 version (URL)http://dx.doi.org/10.1016/j.redox.2020.101525
URIhttp://hdl.handle.net/10261/218290
DOIhttp://dx.doi.org/10.1016/j.redox.2020.101525
Identifiersdoi: 10.1016/j.redox.2020.101525
issn: 2213-2317
Appears in Collections:(EEZ) Artículos
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