The coulombic hypothesis of mitochondrial energy transduction: an attempt to quantify relationships in the energized zones.

From a consideration of (i) an assumed maximal respiration rate (ii) the ATP synthesis which can be obtained from mitochondria after respiratory inhibition and (iii) electrophoretic mobility data, the number of energized zones on the mitochondrial inner membrane has been assessed as 0.68 X 10(18)/g protein. For a single zone (representing one electron transport chain, three phosphorylating complexes and three fixed-charge cycles) in which all the cycles use molecular species doubly-charged in the energized form (b2-), the zone area will be 134 A2 and the specialized fixed charge concentration 4.

Local energized proton hypotheses of mitochondrial oxidative phosphorylation.

Two hypotheses are compared each interpreting mitochondrial energy transduction in terms of a localized form of proton activity. Their differences are seen to be profound and far-reaching. It is concluded that the "chemiosmotic/local energized proton dialogue" as conducted hitherto has offered a very incomplete and restricted analysis of the problems of mitochondrial oxidative phosphorylation.

A coulombic hypothesis of mitochondrial oxidative phosphorylation.

A coulombic hypothesis of mitochondrial oxidative phosphorylation is presented, founded upon the evidence for negative fixed charge formation during electron transport chain activity. The intermediary force is electrostatic (psi H) and not electrochemical (delta mu H). The electrochemical potential of the chemiosmotic hypothesis is identified as a "phantom" parameter which owes its delusive existence to the procedures by which it is measured.

Oxygen-pulse curves in rat liver mitochondrial suspensions. Some observations and deductions.

1. The inference, implicit in the chemiosmotic hypothesis, that protons move into the bulk phase during ATP synthesis was investigated. 2.

Studies on human alpha(s)- and kappa-casein fractions and human caseinoglycomacropeptide.

1. Fractions have been obtained from human whole casein closely resembling the alpha(s)- and kappa-fractions of cow casein. 2.