Scopul nostru este sprijinirea şi promovarea cercetării ştiinţifice şi facilitarea comunicării între cercetătorii români din întreaga lume.
Autori: Cristina Bischin, Florina Deac, Radu Silaghi-Dumitrescu, Jonathan A. R. Worrall, Badri S. Rajagopal, Grigore Damian & Chris E. Cooper
Editorial: The official journal of the European Society for Free Radical Research (SFRR-E), Free Radical Research, 45(4), p.439-444, 2011.
The peroxidase-type reactivity of cytochrome c is proposed to play a role in free radical production and/or apoptosis. This study describes cytochrome c catalysis of peroxide consumption by ascorbate. Under conditions where the sixth coordination position at the cytochrome c heme iron becomes more accessible for exogenous ligands (by carboxymethylation, cardiolipin addition or by partial denaturation with guanidinium hydrochloride) this peroxidase activity is enhanced. A reaction intermediate is detected by stopped-flow UV-vis spectroscopy upon reaction of guanidine-treated cytochrome c with peroxide, which resembles the spectrum of globin Compound II species and is thus proposed to be a ferryl species. The ability of physiological levels of ascorbate (10–60 µM) to interact with this species may have implications for mechanisms of cell signalling or damage that are based on cytochrome c/peroxide interactions.
Cuvinte cheie: Cytochrome c , peroxide , ascorbate // Cytochrome c, peroxide, ascorbate