Related Experiment Video
Updated: Jul 11, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Source of residual Bohr effect in hemoglobin oxidation
Abstract:
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.
Related Concept Videos
The Bohr Model
Henderson-Hasselbalch Equation
Oxidation of Alcohols
The process of oxidation in a chemical reaction is observed in any of the three forms:
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Hemoglobin
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Oxygen Transport in the Blood

