期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：3
页码：801-805
DOI：10.1073/pnas.74.3.801
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
