Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin
Hemoglobin (Hb) represents a model protein to study molecular adaptation in vertebrates. Although both affinity and cooperativity of oxygen binding to Hb affect tissue oxygen delivery, only the former was thought to determine molecular adaptations of Hb. Here, we suggest that Hb affinity and coopera...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2019-10-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/47640 |
| _version_ | 1828203945350135808 |
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| author | Olga Rapp Ofer Yifrach |
| author_facet | Olga Rapp Ofer Yifrach |
| author_sort | Olga Rapp |
| collection | DOAJ |
| description | Hemoglobin (Hb) represents a model protein to study molecular adaptation in vertebrates. Although both affinity and cooperativity of oxygen binding to Hb affect tissue oxygen delivery, only the former was thought to determine molecular adaptations of Hb. Here, we suggest that Hb affinity and cooperativity reflect evolutionary and physiological adaptions that optimized tissue oxygen delivery. To test this hypothesis, we derived the relationship between the Hill coefficient and the relative affinity and conformational changes parameters of the Monod-Wymann-Changeux allosteric model and graphed the ‘biophysical Hill landscape’ describing this relation. We found that mammalian Hb cooperativity values all reside on a ridge of maximum cooperativity along this landscape that allows for both gross- and fine-tuning of tissue oxygen unloading to meet the distinct metabolic requirements of mammalian tissues for oxygen. Our findings reveal the mechanism underlying body size-related adaptation of mammalian Hb. The generality and implications of our findings are discussed. |
| first_indexed | 2024-04-12T12:14:08Z |
| format | Article |
| id | doaj.art-013727c270ea4e979cf5acb66ad7f819 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:14:08Z |
| publishDate | 2019-10-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-013727c270ea4e979cf5acb66ad7f8192022-12-22T03:33:28ZengeLife Sciences Publications LtdeLife2050-084X2019-10-01810.7554/eLife.47640Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobinOlga Rapp0Ofer Yifrach1https://orcid.org/0000-0001-9020-9745Department of Life Sciences, Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer Sheva, IsraelDepartment of Life Sciences, Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer Sheva, IsraelHemoglobin (Hb) represents a model protein to study molecular adaptation in vertebrates. Although both affinity and cooperativity of oxygen binding to Hb affect tissue oxygen delivery, only the former was thought to determine molecular adaptations of Hb. Here, we suggest that Hb affinity and cooperativity reflect evolutionary and physiological adaptions that optimized tissue oxygen delivery. To test this hypothesis, we derived the relationship between the Hill coefficient and the relative affinity and conformational changes parameters of the Monod-Wymann-Changeux allosteric model and graphed the ‘biophysical Hill landscape’ describing this relation. We found that mammalian Hb cooperativity values all reside on a ridge of maximum cooperativity along this landscape that allows for both gross- and fine-tuning of tissue oxygen unloading to meet the distinct metabolic requirements of mammalian tissues for oxygen. Our findings reveal the mechanism underlying body size-related adaptation of mammalian Hb. The generality and implications of our findings are discussed.https://elifesciences.org/articles/47640allosterycooperativitymechanismMWCevolutionadaptation |
| spellingShingle | Olga Rapp Ofer Yifrach Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin eLife allostery cooperativity mechanism MWC evolution adaptation |
| title | Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin |
| title_full | Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin |
| title_fullStr | Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin |
| title_full_unstemmed | Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin |
| title_short | Evolutionary and functional insights into the mechanism underlying body-size-related adaptation of mammalian hemoglobin |
| title_sort | evolutionary and functional insights into the mechanism underlying body size related adaptation of mammalian hemoglobin |
| topic | allostery cooperativity mechanism MWC evolution adaptation |
| url | https://elifesciences.org/articles/47640 |
| work_keys_str_mv | AT olgarapp evolutionaryandfunctionalinsightsintothemechanismunderlyingbodysizerelatedadaptationofmammalianhemoglobin AT oferyifrach evolutionaryandfunctionalinsightsintothemechanismunderlyingbodysizerelatedadaptationofmammalianhemoglobin |