According to the Bohr effect, hemoglobin's oxygen binding affinity is inversely related both to acidity and to the concentration of carbon dioxide, carbon dioxide reacts with water to form carbonic acid, an increase in CO2 results in a decrease in blood pH, resulting in hemoglobin proteins releasing their load of oxygen, conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen, all these processes have been conducted under influence of increase of unsaturated fatty acids – alpha state as first variant of basic three membrane states of a membrane - redox potentials three - state (MRPTS) within a membrane - redox potentials three - state line system reaction medium firstly described by us, which have been functioned in the framework of “Donators + membrane - redox potentials three - state line system + O2 + АDP + Pi + H+ + nH+ membrane space = (ATP + heat energy) + H2O + nH+matrix + CO2” which is belong to the the membrane redoxy potential three state dependent 9 stepped full cycle of proton conductance.