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PMID: 265575 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Mechanism of tertiary structural change in hemoglobin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 3 ·1977-03-00 ·Pages 801-5

Gelin BR, Karplus M

Abstract

A reaction path is presented by which the effects of oxygen binding in hemoglobin are transmitted from a heme group to the surface of its subunit. Starting from the known deoxy geometry, it is shown by calculations with empirical energy functions and comparisons with available data how the change in heme geometry on ligation introduces a perturbation that leads to the tertiary structural alterations essential for cooperatively. It is found that there is little strain on the unliganded heme; instead, the reduced oxygen affinity of hemoglobin results from the strain on the liganded subunit in a tetramer with the deoxy quarternary structure.

MeSH Terms
Amino Acid Sequence Globins Heme Hemoglobins Histidine Humans Ligands Models, Biological Models, Molecular Oxyhemoglobins Protein Conformation Thermodynamics Valine
Chemicals
Hemoglobins Ligands Oxyhemoglobins Heme Histidine Globins Valine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gelin B R
Karplus M
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23 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
DOI
10.1073/pnas.74.3.801
Published
1977-03-00
Pages
801-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430479
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.3.801 PMC Full Text View journal details
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