Final answer:
2,3-bisphosphoglycerate (2,3-BPG) interacts with the beta chains on hemoglobin (Hb) by binding to the positively charged amino acid residues, stabilizing the low-affinity state and promoting oxygen release.
Step-by-step explanation:
2,3-bisphosphoglycerate (2,3-BPG) interacts with hemoglobin (Hb) by binding to specific sites on the beta chains of the hemoglobin molecule. Specifically, 2,3-BPG binds in the central cavity of the hemoglobin tetramer and interacts with positively charged amino acid residues of the beta chains. This binding, which forms a salt bridge with the amino terminal of the beta chains, stabilizes the hemoglobin in its low-affinity state for oxygen (deoxyhemoglobin), facilitating the release of oxygen to the tissues. 2,3-BPG does not bind directly to the iron center, the heme group, or the oxygen molecules.