1. The effects of uncoupling of mitochondria1 oxidative phosphorylation on the efficiency of energy conservation during oxidation of amino acids, fatty acids, glycerol, glucose and 101 food proteins have been examined in order to compare how uncoupling at coupling site 1 affects energy yields compared with uncoupling at sites 2 + 3 and uncoupling by proton leakage. The effects of uncoupling by each mechanism on the isodynamic equivalents of carbohydrate, fat and protein at the level of cytoplasmic ATP yield have been estimated.2. Energy conservation during amino acid oxidation decreases relative to that for glucose as uncoupling by all three mechanisms increases. This effect is least when uncoupling is at site 1 and is associated with a fall in the isodynamicequivalent for protein: glucose of 4%maximally, and a fall in the cytoplasmic ATP yield for glucose of 25% (15–30% when accounting for uncertainty in the choice of proton stoichiometries).3. Variation in the efficiency of energy conservation for the different amino acids is large for both highly coupled and uncoupled mitochondria but the range of efficiencies for the oxidation of 101 food proteins is relatively small (less than 6% of the mean) for a tightly coupled system. This range increases absolutely (minimally fourfold) and relatively (minimally 44% of the mean value) with severely uncoupled mitochondria but is nearly constant (changes by less than 1% relative to the mean) within the probable physiologically relevant range of uncoupling in the whole body and in the full range of uncoupling at site 1. The rank order position of particular proteins within the range of values is found to change most for gelatin which is oxidized with least energy conservation in a severely (unphysiologically) uncoupled system and most efficiently in a fully coupled system when oxidation of protein is considered to be direct, i.e. not via gluconeogenesis.4. For medium- and long-chain fatty acids, uncoupling at site 1 elevates the efficiency of energy conservation relative to that for glucose (maximally 4%) whereas uncoupling by other mechanisms decreases this relative efficiency. The pattern of effects for short-chain fatty acids resembles that for the amino acids.5. The changes in the isodynamic equivalents of protein:glucose and of fat:glucose are small when uncoupling occurs at site I and tend to cancel for a mixed diet but are additive in the effect on food energy values when uncoupling is by the other mechanisms. Hence changes in the efficiency of oxidative energy coupling at site 1 in association with Luft's disease or dietary changes would result in effects which are of little true dietetic significance on the isodynamic equivalents of nutrients at the level of cytoplasmic ATP yield in vivo.
Gas chromatography-mass spectrometry of lysinoalanine and the related crosslinked amino acids in alkali-treated food proteins.