World Library  
Flag as Inappropriate
Email this Article

Bohr effect

Article Id: WHEBN0000618291
Reproduction Date:

Title: Bohr effect  
Author: World Heritage Encyclopedia
Language: English
Subject: Respiratory physiology, Haldane effect, Common octopus, Hemoglobin, Carbaminohemoglobin
Collection: Respiratory Physiology
Publisher: World Heritage Encyclopedia

Bohr effect

Not to be confused with the Bohr Equation

Hemoglobin Dissociation Curve. Dotted red line corresponds with shift to the right caused by Bohr effect

The Bohr effect is a physiological phenomenon first described in 1904 by the Danish physiologist Christian Bohr, stating that hemoglobin's oxygen binding affinity (see Oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide.[1] Id est, an increase in blood CO2 concentration which leads to a decrease in blood pH will result in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen. Since carbon dioxide reacts with water to form carbonic acid, an increase in CO2 results in a decrease in blood pH.


  • Mechanism 1
  • Physiological role 2
  • Effects of allostery 3
  • See also 4
  • References 5
  • External links 6


In deoxyhemoglobin, the N-terminal amino groups of the α-subunits and the C-terminal histidine of the β-subunits participate in ion pairs. The formation of ion pairs causes them to decrease in acidity. Thus, deoxyhemoglobin binds one proton (H+) for every two O2 released. In oxyhemoglobin, these ion pairings are absent and these groups increase in acidity. Consequentially, a proton is released for every two O2 bound. Specifically, this reciprocal coupling of protons and oxygen is the Bohr effect.[2]

Additionally, carbon dioxide reacts with the N-terminal amino groups of α-subunits to form carbamates:[3]

R−NH2 + CO2 \rightleftharpoons R−NH−COO + H+

Deoxyhemoglobin binds to CO2 more readily to form a carbamate than oxyhemoglobin. When CO2 concentration is high (as in the capillaries), the protons released by carbamate formation further promotes oxygen release. Although the difference in CO2 binding between the oxy and deoxy states of hemoglobin accounts for only 5% of the total blood CO2, it is responsible for half of the CO2 transported by blood. This is because 10% of the total blood CO2 is lost through the lungs in each circulatory cycle.[4]

Physiological role

This effect facilitates oxygen transport as hemoglobin binds to oxygen in the lungs, but then releases it in the tissues, particularly those tissues in most need of oxygen. When a tissue's metabolic rate increases, its carbon dioxide production increases. Carbon dioxide forms bicarbonate through the following reaction:

CO2 + H2O \rightleftharpoons H2CO3 \rightleftharpoons H+ + HCO3

Although the reaction usually proceeds very slowly, the enzyme family of carbonic anhydrase, which is present in red blood cells, accelerates the formation of bicarbonate and protons.[4] This causes the pH of tissues to decrease, and so, promotes the dissociation of oxygen from hemoglobin to the tissue, allowing the tissue to obtain enough oxygen to meet its demands. Conversely, in the lungs, where oxygen concentration is high, binding of oxygen causes hemoglobin to release protons, which combine with bicarbonate to drive off carbon dioxide in exhalation. Since these two reactions are closely matched, there is little change in blood pH.

The dissociation curve shifts to the right when carbon dioxide or hydrogen ion concentration is increased. This facilitates increased oxygen dumping. This mechanism allows for the body to adapt the problem of supplying more oxygen to tissues that need it the most. When muscles are undergoing strenuous activity, they generate CO2 and lactic acid as products of cellular respiration and lactic acid fermentation. In fact, muscles generate lactic acid so quickly that pH of the blood passing through the muscles will drop to around 7.2. As lactic acid releases its protons, pH decreases, which causes hemoglobin to release ~10% more oxygen.[4]

Effects of allostery

The Bohr effect is dependent on allosteric interactions between the hemes of the hemoglobin tetramer. This is evidenced by the fact that myoglobin, a monomer with no allostery, does not exhibit the Bohr effect. Hemoglobin mutants with weaker allostery may exhibit a reduced Bohr effect.

In the Hiroshima variant hemoglobinopathy, allostery in hemoglobin is reduced, and the Bohr effect is diminished. During periods of exercise, the mutant hemoglobin has a higher affinity for oxygen and tissue may suffer minor oxygen starvation.[5]

See also


  1. ^ Bohr; Hasselbalch, Krogh. "Concerning a Biologically Important Relationship - The Influence of the Carbon Dioxide Content of Blood on its Oxygen Binding". 
  2. ^ Murray, Robert K.; Darryl K. Granner; Peter A. Mayes; Victor W. Rodwell (2003). Harper’s Illustrated Biochemistry (LANGE Basic Science) (26th ed.). McGraw-Hill Medical. pp. 44–45.  
  3. ^ Lehninger, Albert L.; Nelson, David L.; Cox, Michael M. (2008). Principles of Biochemistry (5th ed.). New York, NY: W.H. Freeman and Company. p. 166.  
  4. ^ a b c Voet, Donald; Judith G. Voet; Charlotte W. Pratt (2013). Fundamentals of Biochemistry: Life at the Molecular Level (4th ed.). John Wiley & Sons, Inc. p. 189. 
  5. ^ Olson, JS; Gibson QH; Nagel RL; Hamilton HB (December 1972). "The ligand-binding properties of hemoglobin Hiroshima ( 2 2 146asp )". The Journal of Biological Chemistry 247 (23): 7485–93.  

External links

  • Impact of training
This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.