AI Article Synopsis
- The study used fluorescein isothiocyanate (FITC) to label coupled mitochondria and found that a significant portion of the dye is associated with mitochondrial proteins, particularly those within the inner membrane.
- FITC binding experiments suggest that mitochondrial proteins behave like polyelectrolytes, with a dissociation constant around 10(-7), and show competition between H+ and K+ ions for binding at neutral pH.
- The results also indicate that the deprotonation of matrix proteins occurs slowly and is linked to the equilibrium between matrix and medium protons, potentially affecting mitochondrial respiration rates under specific conditions.
Article Abstract
Preparations of coupled mitochondria were labeled with fluorescein isothiocyanate (FITC). Comparison of characteristics of FITC bound to mitochondria versus azolectin liposomes indicates that a significant part of the probe is bound to mitochondrial proteins including proteins of the matrix side of the inner membrane. The experiments with the probe indicate that mitochondrial proteins resemble typical polyelectrolytes with constant of dissociation close to 10(-7).H+ and K+ compete for binding to mitochondrial proteins at neutral pH. The slow deprotonation of matrix proteins is observed during equilibration of matrix protons with medium protons. This process is not restricted to the transmembrane proton transfer. The data are explained by the theory of immobilized buffer. Under certain conditions the extent of dissociation of the matrix immobilized buffer correlates with the rate of mitochondrial respiration in state 3P according to chance.
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