CO ligation intermediates and the mechanism of hemoglobin cooperativity - PubMed (original) (raw)
. 1999 Jan 29;274(5):2605-8.
doi: 10.1074/jbc.274.5.2605.
Affiliations
- PMID: 9915786
- DOI: 10.1074/jbc.274.5.2605
Free article
CO ligation intermediates and the mechanism of hemoglobin cooperativity
M Perrella et al. J Biol Chem. 1999.
Free article
Abstract
Direct experimental resolution of the ligation intermediates for the reaction of human hemoglobin with CO reveals the distribution of ligated states as a function of saturation. At low saturation, binding of CO occurs with slightly higher affinity to the beta chains, but pairwise interactions are more pronounced between the alpha chains. At high saturation, the two chains tend to behave identically. The sequence of CO ligation reconstructed from the distribution of intermediates shows that the overall increase in CO affinity is 588-fold, but it is not distributed uniformly among the ligation steps. The affinity increases 16.5-fold in the second ligation step, 4.6-fold in the third ligation step, and 7.7-fold in the fourth ligation step. This pattern and the detailed distribution of ligated states cannot be immediately reconciled with the predictions of either the concerted allosteric model of Monod-Wyman-Changeux or the sequential model of Koshland-Nemethy-Filmer and underscore a more subtle mechanism for hemoglobin cooperativity.
Similar articles
- Modulation of the association reaction between hemoglobin and carbon monoxide by proton and chloride.
Perrella M, Ripamonti M, Caccia S. Perrella M, et al. Biochemistry. 1998 Feb 17;37(7):2017-28. doi: 10.1021/bi971669u. Biochemistry. 1998. PMID: 9485328 - The dissociation of carbon monoxide from hemoglobin intermediate.
Samaja M, Rovida E, Niggeler M, Perrella M, Rossi-Bernardi L. Samaja M, et al. J Biol Chem. 1987 Apr 5;262(10):4528-33. J Biol Chem. 1987. PMID: 3558353 - Understanding allosteric and cooperative interactions in enzymes.
Cornish-Bowden A. Cornish-Bowden A. FEBS J. 2014 Jan;281(2):621-32. doi: 10.1111/febs.12469. Epub 2013 Sep 2. FEBS J. 2014. PMID: 23910900 Review. - Tertiary and quaternary effects in the allosteric regulation of animal hemoglobins.
Ronda L, Bruno S, Bettati S. Ronda L, et al. Biochim Biophys Acta. 2013 Sep;1834(9):1860-72. doi: 10.1016/j.bbapap.2013.03.013. Epub 2013 Mar 20. Biochim Biophys Acta. 2013. PMID: 23523886 Review.
Cited by
- The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin.
Levantino M, Spilotros A, Cammarata M, Schirò G, Ardiccioni C, Vallone B, Brunori M, Cupane A. Levantino M, et al. Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14894-9. doi: 10.1073/pnas.1205809109. Epub 2012 Aug 27. Proc Natl Acad Sci U S A. 2012. PMID: 22927385 Free PMC article. - Hypoxia, red blood cells, and nitrite regulate NO-dependent hypoxic vasodilation.
Crawford JH, Isbell TS, Huang Z, Shiva S, Chacko BK, Schechter AN, Darley-Usmar VM, Kerby JD, Lang JD Jr, Kraus D, Ho C, Gladwin MT, Patel RP. Crawford JH, et al. Blood. 2006 Jan 15;107(2):566-74. doi: 10.1182/blood-2005-07-2668. Epub 2005 Sep 29. Blood. 2006. PMID: 16195332 Free PMC article. - A spin transition mechanism for cooperative adsorption in metal-organic frameworks.
Reed DA, Keitz BK, Oktawiec J, Mason JA, Runčevski T, Xiao DJ, Darago LE, Crocellà V, Bordiga S, Long JR. Reed DA, et al. Nature. 2017 Oct 5;550(7674):96-100. doi: 10.1038/nature23674. Epub 2017 Sep 11. Nature. 2017. PMID: 28892810 - Hemoglobin: Structure, Function and Allostery.
Ahmed MH, Ghatge MS, Safo MK. Ahmed MH, et al. Subcell Biochem. 2020;94:345-382. doi: 10.1007/978-3-030-41769-7_14. Subcell Biochem. 2020. PMID: 32189307 Free PMC article. Review. - Carbon Monoxide as a Potential Therapeutic Agent: A Molecular Analysis of Its Safety Profiles.
Bansal S, Liu D, Mao Q, Bauer N, Wang B. Bansal S, et al. J Med Chem. 2024 Jun 27;67(12):9789-9815. doi: 10.1021/acs.jmedchem.4c00823. Epub 2024 Jun 12. J Med Chem. 2024. PMID: 38864348 Free PMC article. Review.