By E. C. Slater (auth.), John J. Lemasters, Charles R. Hackenbrock, Ronald G. Thurman, Hans V. Westerhoff (eds.)
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C reductase and of succinate oxidase. Moreover, Heron et al. c reductase above that of the same activity upon stoichiometric association of the comp1exes. c reductase, it appears unlike1y that the same step (diffusion of the Q-poo1) is rate1imiting for both NADH and succinate oxidation.
CONCLUSIONS Cytochrome c-mediated electron transport rate and collision efficiency in the mitochondrial inner membrane is greatest when the ionic strength is physiological (100-150 mM); the affinities of cytochrome ~ for its redox partners and the inner membrane surface are lowest; its concentration near the membrane surface is lowest; and it is diffusing in three dimensions at a maximal diffusion rate. These findings indicate that the rate of diffusion of cytochrome c and its concentration near the membrane surface are limiting for th~ maximal rate of electron transport.
1983) a When two va1ues are present, they represent EA above and be10w the break, respective1y. Tab1e 7. Possib1e reasons for breaks in Arrhenius plots. 1. Change in rate-1imiting step in reaction path with temperature (Dixon and Webb,1964) 2. Temperature-dependent conformationa1 change (cf. ,1966) 3. Phase change in the solvent, inc1uding a phase transition of the phospho1ipids (Raison,1972) 4. Diffusion in unstirred 1ayers (Go1dstein,1976) 5. Viscosity becoming rate-1imitinq for conformationa1 f1exibi1ity (Lenaz and Parenti Caste11i,1985) the iso1ated comp1ex in mice11ar solution exhibit a linear pattern with EA of 18 Kca1/mo1; in membranous reductase, however, (both in submitochondria1 partic1es and in bCl proteo1iposomes), the plots become biphasic with a break at about 20°C and EA of 8-10 Kca1/mo1 above and 18 Kca1/mo1 be10w the breakpoint (Tab1e 6).