1,720,979 research outputs found
Different Fe molecular species mediate selective H2O2-damage to different moieties of F0F1ATPsynthase in intact cells, isolated mitochondria or proteoliposomes
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Iron binding to additional sites of bacterial and mammalian F1ATPases: structure stabilisation vs. pro-oxidant side-effects
No full textGlutathione status and malondialdheyde production as markers of oxidative stress occurred during erythroid differentiation
No full textIn vivo changes in work rate of F0F1ATPsynthase during reactive hyperaemia and ischemic preconditioning in goat heart
No full textInteraction of the inhibitor protein IF1 with F0F1ATPsynthase from ox heart under different pH and aggregation states
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Fe(III) binding to the nucleotide-independent site located in beta subunit of mitochondrial F1ATPase affects protein structure and function
No full textMammalian ATPsynthase monomer versus dimer profiled by blue native PAGE and activity stain
No full texties into the effects of oligomerization on F(0)F(1)ATPsynthase function are contradictory. We optimized the in-gel ATPase assay to investigate the functional differences of monomers versus dimers. In Triton X-100 extracts of heavy bovine heart mitochondria (HBHM) and mitoplasts, but not submitochondrial particles (MgATP-SMP), dimers had greater specific activity than monomers: at 30 degrees C, the dimer/monomer activity ratios were 2.3, 1.4, and 1.0, respectively. These differences in HBHM and mitoplasts extracts were enhanced at 37 degrees C but lost at 20 degrees C. In mitoplasts but not in MgATP-SMP, dimers were selectively shielded from limited chymotrypsin degradation of F(1) alpha subunit, possibly due to interactions with other proteins or ligands in the native inner membrane. Despite these differences, all three preparations had similar percentages of dimers and similar contents of the native inhibitor IF(1) in Vm (monomer) and (dimer) Vd. These results suggest that, in native membrane, monomers and dimers are functionally distinct
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