tailieunhanh - Báo cáo khoa học: Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack

Reactionof certainpeptides andproteinswithsingletoxygen (generated by visible light in the presence of rose bengal dye) yields long-lived peptide and protein peroxides. Incubation of these peroxides with glyceraldehyde-3-phosphate dehy-drogenase, in the absence of addedmetal ions, results in loss of enzymatic activity. Comparative studies with a range of peroxides have shown that this inhibition is concentration, peroxide, and time dependent, with H2O2less e cient than some peptide peroxides. | Eur. J. Biochem. 269 1916-1925 2002 FEBS 2002 doi Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack Philip E. Morgan1 Roger T. Dean2 and Michael J. Davies1 1EPR and 2Cell Biology Groups The Heart Research Institute Sydney New South Wales Australia Reaction of certain peptides and proteins with singlet oxygen generated by visible light in the presence of rose bengal dye yields long-lived peptide and protein peroxides. Incubation of these peroxides with glyceraldehyde-3-phosphate dehydrogenase in the absence of added metal ions results in loss of enzymatic activity. Comparative studies with a range of peroxides have shown that this inhibition is concentration peroxide and time dependent with H2O2 less efficient than some peptide peroxides. Enzyme inhibition correlates with loss of both the peroxide and enzyme thiol residues with a stoichiometry of two thiols lost per peroxide consumed. Blocking the thiol residues prevents reaction with the peroxide. This stoichiometry the lack of metal-ion dependence and the absence of electron paramagnetic resonance EPR -detectable species is consistent with a molecular nonradical reaction between the active-site thiol of the enzyme and the peroxide. A number of low-molecular-mass compounds including thiols and ascorbate but not Trolox C can prevent inhibition by removing the initial peroxide or species derived from it. In contrast glutathione reductase and lactate dehydrogenase are poorly inhibited by these peroxides in the absence of added Fe2 -EDTA. The presence of this metal-ion complex enhanced the inhibition observed with these enzymes consistent with the occurrence of radical-mediated reactions. Overall these studies demonstrate that singlet oxygen-mediated damage to an initial target protein can result in selective subsequent damage to other proteins as evidenced by loss of enzymatic activity via the formation and .

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