| Reverso | 1. Low pH and Protonation of Histidine (His146):When the pH drops (becomes more acidic), a specific amino acid residue, histidine (His146) on the beta (β) chains of hemoglobin, becomes protonated (gains a hydrogen ion).This protonation contributes to stabilizing hemoglobin in its T state (tense state), which has a lower affinity for oxygen.2. Impact of Carbon Dioxide (CO2):During tissue metabolism, cells produce carbon dioxide (CO2) as a byproduct. The more exercise we do, the lower the pH is so the more CO2 we produce. CO2 can bind to hemoglobin, forming carbaminohemoglobin. This binding further stabilizes the T state.3. Stabilization of the T State:The combined effect of low pH (protonation of His146) and CO2 binding makes the T state of hemoglobin more stable.When hemoglobin is in the T state, it releases oxygen more readilyThese conditions (low pH and increased CO2) promote the release of oxygen from hemoglobin, ensuring that more oxygen is delivered to tissues that are actively metabolizing and in need of oxygen.
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