KINETIC MECHANISM OF ACTION OF AN UNCOUPLER OF OXIDATIVE-PHOSPHORYLATION
KINETIC MECHANISM OF ACTION OF AN UNCOUPLER OF OXIDATIVE-PHOSPHORYLATION
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DOI:
10.1007/bf01940940
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发表时间:
1977-01-01
影响因子:
2.4
通讯作者:
MCLAUGHLIN, S
中科院分区:
文献类型:
--
作者:
COHEN, FS;EISENBERG, M;MCLAUGHLIN, S
The chemiosmotic hypothesis predicts that the mechanism by which weak acids uncouple oxidative phosphorylation in mitochondria is identical to the mechanism by which they transport H across artificial bilayer membranes. The results of a kinetic study of uncoupler-mediated H transport across bilayer membranes is reported. Electrical relaxation measurements were made on black lipid membranes exposed to the substituted benzimidazole 5,6-dichloro-2-trifluoromethylbenzimidazole. The simplest model consistent with the experimental data allowed values for adsorption coefficients and rate constants to be deduced. The back diffusion of the neutral species is the rate limiting step for the steady state transport of H, the neutral and charged forms of the uncoupler adsorb strongly to the interfaces and the reactions at the membrane-solution interfaces occur sufficiently rapidly for equilibrium to be maintained. Independent measurements of the adsorption coefficients of the neutral and anionic forms of the weak acid and of the membrane permeability to the neutral form agreed well with the values deduced from the kinetic study.