NDLI: Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.

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Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.

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Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ackers, G. K. Shea, M. A. Johnson, J. A. Licata, V. J. Turner, G. J. Daugherty, M. A.
Description	Author Affiliation: Daugherty MA ( Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.);
Abstract	The 10 ligation species of human cyanomethemoglobin were previously found to distribute into three discrete cooperative free energy levels according to a combinatorial code (i.e., dependent on both the number and configuration of ligated subunits). Analysis of this distribution showed that the hemoglobin tetramer occupies a third allosteric state in addition to those of the unligated (T) and fully ligated (R) species. To determine the nature of the intermediate allosteric state, we have studied the effects of pH, temperature, and single-site mutations on its free energy of quaternary assembly, in parallel with corresponding data on the deoxy (T) and fully ligated (R) species. Results indicate that the intermediate allosteric tetramer has the deoxy (T) quaternary structure. This finding, together with the resolved energetic distribution of the 10 microstates reveals a symmetry rule for quaternary switching--i.e., switching from T to R occurs whenever a binding step creates a tetramer with one or more ligated subunits on each side of the alpha 1 beta 2 intersubunit contact. These studies also reveal significant cooperativity within each alpha 1 beta 1 dimer of the T-state tetramer. The ligand-induced tertiary free energy alters binding affinity within the T structure by 170-fold prior to quaternary switching.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hemoglobin A Metabolism Methemoglobin Analogs & Derivatives Allosteric Site Amino Acid Sequence Kinetics Molecular Sequence Data Thermodynamics Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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