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A simple question to think about when considering the hemoglobin function
Author(s) -
RuizLarrea M. Begoña
Publication year - 2002
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.2002.494030040101
Subject(s) - hemoglobin , protein quaternary structure , myoglobin , oxygen , oxygen transport , chemistry , biophysics , biochemistry , protein subunit , biology , organic chemistry , gene
Hemoglobin is a complex protein formed by various subunits interacting with each other. These non‐covalent interactions, quaternary structure, are responsible for hemoglobin functioning as an excellent oxygen transporter, loading up with oxygen in the lungs and delivering it to tissues, where the oxygen pressure is lower. The communications between subunits make hemoglobin bind oxygen in a cooperative way, displaying sigmoidal saturation curves. In addition to oxygen, hemoglobin also transports H + , CO 2 , and 2,3‐bisphosphoglycerate, and these molecules regulate the transport of oxygen. The quaternary structure of hemoglobin accounts for the different behavior with respect to another oxygen‐binding protein, myoglobin, a monomeric protein, thus lacking quaternary structure, whose function is mainly to store oxygen. A simple question, “What consequences would the loss of the hemoglobin quaternary structure have on oxygenation?” helps the student to think about the behavior of hemoglobin and to integrate and relate all the elements affecting its binding with oxygen.