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PMID: 1070000 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Rate of quaternary structure change in hemoglobin measured by modulated excitation.

Ferrone FA, Hopfield JJ

Abstract

Using a novel technique of modulated photo-dissociation of carbon monoxide from hemoglobin, we have obtained the rates for conversion between the two quaternary states, R, and T, at 3-fold ligation. Our measurements at pH 7 and 22 degrees give rates of 780 +/- 40 sec-1 for going from R to T, and 2500 +/- 200 sec-1 from T to R. This yields an equilibrium constant of 0.31 +/- 0.04, which is in good agreement with previous estimates. The degree of agreement between this equilibrium constant and that predicted from the allosteric model provides a new, quantitative test of the allosteric description. A sequential model for the change in structure was found incompatible with the data, even if kinetic subunit inequivalence was assumed. The technique described here is quite general and can be used as long as the system under investigation can be repetitively excited in a regime in which it responds linearly to the excitation.

MeSH Terms
Allosteric Regulation Carboxyhemoglobin Hemoglobin A/metabolism Hemoglobins/metabolism Humans Kinetics Ligands/metabolism Methods Models, Biological Protein Conformation Spectrum Analysis Structure-Activity Relationship
Chemicals
Hemoglobins Ligands Hemoglobin A Carboxyhemoglobin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ferrone F A
Hopfield J J
References (11)
11 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1976-12-00
Pages
4497-501
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431515
Subset
IM
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