Bohr effect

The decrease in hemoglobin’s oxygen affinity caused by increased carbon dioxide or acidity, which promotes oxygen release in metabolically active tissues.

Hemoglobin: Hemoglobin is a red blood cell protein that binds oxygen reversibly and transports it through the blood. Its changing oxygen affinity is the basis of the Bohr effect.
Carbon dioxide: A gas produced by cellular metabolism and transported in blood to the lungs for exhalation. Rising carbon dioxide contributes to the conditions that lower hemoglobin’s oxygen affinity.
Oxygen delivery: The rate at which oxygen is transported by blood and made available to tissues. The Bohr effect supports oxygen unloading where tissue carbon dioxide and acidity are elevated.
Christian Bohr: A Danish physiologist who studied respiratory physiology and described carbon dioxide’s effect on oxygen binding. His experiments gave the effect its name and established its defining relationship.
Oxygen–hemoglobin dissociation curve: A graph showing how hemoglobin oxygen saturation varies with oxygen partial pressure. The Bohr effect shifts this curve to the right as acidity or carbon dioxide rises.
Blood pH: A measure of hydrogen ion activity in blood, normally maintained within a narrow range. Lower pH increases proton binding to hemoglobin and strengthens the Bohr effect.
Tissue metabolism: The chemical reactions by which cells obtain energy and build or maintain cellular components. Active metabolism produces carbon dioxide and acids that promote local oxygen release.
Bohr–Hasselbalch equation: An equation relating pH, acid dissociation, and the ratio of conjugate base to acid concentrations. It shares Bohr’s name but describes acid–base equilibrium rather than hemoglobin oxygen affinity.
Hemoglobin allostery: The regulation of hemoglobin’s ligand binding through structural changes transmitted between its subunits. The effect arises when protons and carbon dioxide favor hemoglobin’s lower-affinity conformation.
Bohr model of hemoglobin: A model describing how protonation changes hemoglobin’s oxygen-binding equilibrium. It expresses the effect as linked equilibria between protons and oxygen binding.

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