Explain the biochemical basis for the Bohr effect on oxygen binding to hemoglobin protons attach to a C-terminal histidine, forming a salt bridge which stabilizes the T state protons compete for the oxygen binding site protons produce a phosphorylation even that causes hemoglobin to not bind oxygen protons cause hemoglobin to switch from the R state to the T state protons perform redox chemistry with the iron in the heme group, rendering the heme unable to bind oxygen