Source of residual Bohr effect in hemoglobin oxidation.
The hemoglobin oxidation Bohr effect is larger than the ligation Bohr effect, even when the former is corrected for any ionization of the water molecule bound to the ferric iron of methemoglobin. This residual oxidation Bohr effect is here shown to be solely caused by the influence of the positively charged ferriheme, and is abolished when the oxidized heme binds an anion. This result frees the formal equivalence of hemoglobin ligation and oxidation from the last apparent experimental discrepancy.
D000838:Anions; D002263:Carboxyhemoglobin / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008706:Methemoglobin / Q000378:metabolism*; D009211:Myoglobin / Q000378:metabolism; D009994:Osmolar Concentration; D010084:Oxidation-Reduction; D010108:Oxyhemoglobins / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000838:Anions; D006454:Hemoglobins; D008024:Ligands; D009211:Myoglobin; D010108:Oxyhemoglobins; D006418:Heme; D008706:Methemoglobin; D002263:Carboxyhemoglobin