Question: as co concentrations increase what happens to oxygen binding to hemoglobin

title: Bohr effect
text: The Bohr effect hinges around allosteric interactions between the hemes of the haemoglobin tetramer , a mechanism first proposed by Max Perutz in 1970 . Haemoglobin exists in two conformations : a high - affinity R state and a low - affinity T state . When oxygen concentration levels are high , as in the lungs , the R state is favored , enabling the maximum amount of oxygen to be bound to the hemes . In the capillaries , where oxygen concentration levels are lower , the T state is favored , in order to facilitate the delivery of oxygen to the tissues . The Bohr effect is dependent on this allostery , as increases in CO and H help stabilize the T state and ensure greater oxygen delivery to muscles during periods of elevated cellular respiration . This is evidenced by the fact that myoglobin , a monomer with no allostery , does not exhibit the Bohr effect . Haemoglobin mutants with weaker allostery may exhibit a reduced Bohr effect . For example , in Hiroshima variant haemoglobinopathy , allostery in haemoglobin is reduced , and the Bohr effect is diminished . As a result , during periods of exercise , the mutant haemoglobin has a higher affinity for oxygen and tissue may suffer minor oxygen starvation .