A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans
This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional...
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ftunivadelaidedl:oai:digital.library.adelaide.edu.au:2440/67455 2023-05-15T15:12:20+02:00 A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans Yuan, Y. Shen, T. Gupta, P. Ho, N. Simplaceanu, V. Tam, T. Hofreiter, M. Cooper, A. Campbell, K. Ho, C. 2011 http://hdl.handle.net/2440/67455 https://doi.org/10.1021/bi200777j en eng Amer Chemical Soc Biochemistry, 2011; 50(34):7350-7360 0006-2960 1520-4995 http://hdl.handle.net/2440/67455 doi:10.1021/bi200777j Cooper, A. [0000-0002-7738-7851] © 2011 American Chemical Society Animals Elephants Humans Phosphates Oxygen Alkanesulfonic Acids Morpholines Hemoglobins Hemoglobin A2 Blood Substitutes Buffers Temperature Amino Acid Sequence Hydrogen-Ion Concentration Molecular Sequence Data Biophysical Phenomena Mammoths Journal article 2011 ftunivadelaidedl https://doi.org/10.1021/bi200777j 2023-02-05T19:31:04Z This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional properties of recombinant hemoglobins (rHb) from woolly mammoth (rHb WM) and Asian elephant (rHb AE) in relation to human hemoglobins Hb A and Hb A(2) (a minor component of human blood). We have obtained oxygen equilibrium curves and calculated O(2) affinities, Bohr effects, and the apparent heat of oxygenation (ΔH) in the presence and absence of allosteric effectors [inorganic phosphate and inositol hexaphosphate (IHP)]. Here, we show that the four Hbs exhibit distinct structural properties and respond differently to allosteric effectors. In addition, the apparent heat of oxygenation (ΔH) for rHb WM is less negative than that of rHb AE, especially in phosphate buffer and the presence of IHP, suggesting that the oxygen affinity of mammoth blood was also less sensitive to temperature change. Finally, (1)H NMR spectroscopy data indicates that both α(1)(β/δ)(1) and α(1)(β/δ)(2) interfaces in rHb WM and rHb AE are perturbed, whereas only the α(1)δ(1) interface in Hb A(2) is perturbed compared to that in Hb A. The distinct structural and functional features of rHb WM presumably facilitated woolly mammoth survival in the Arctic environment. Yue Yuan, Tong-Jian Shen, Priyamvada Gupta, Nancy T. Ho, Virgil Simplaceanu, Tsuey Chyi S. Tam, Michael Hofreiter, Alan Cooper, Kevin L. Campbell and Chien Ho Article in Journal/Newspaper Arctic The University of Adelaide: Digital Library Arctic Biochemistry 50 34 7350 7360 |
institution |
Open Polar |
collection |
The University of Adelaide: Digital Library |
op_collection_id |
ftunivadelaidedl |
language |
English |
topic |
Animals Elephants Humans Phosphates Oxygen Alkanesulfonic Acids Morpholines Hemoglobins Hemoglobin A2 Blood Substitutes Buffers Temperature Amino Acid Sequence Hydrogen-Ion Concentration Molecular Sequence Data Biophysical Phenomena Mammoths |
spellingShingle |
Animals Elephants Humans Phosphates Oxygen Alkanesulfonic Acids Morpholines Hemoglobins Hemoglobin A2 Blood Substitutes Buffers Temperature Amino Acid Sequence Hydrogen-Ion Concentration Molecular Sequence Data Biophysical Phenomena Mammoths Yuan, Y. Shen, T. Gupta, P. Ho, N. Simplaceanu, V. Tam, T. Hofreiter, M. Cooper, A. Campbell, K. Ho, C. A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
topic_facet |
Animals Elephants Humans Phosphates Oxygen Alkanesulfonic Acids Morpholines Hemoglobins Hemoglobin A2 Blood Substitutes Buffers Temperature Amino Acid Sequence Hydrogen-Ion Concentration Molecular Sequence Data Biophysical Phenomena Mammoths |
description |
This study is aimed at investigating the molecular basis of environmental adaptation of woolly mammoth hemoglobin (Hb) to the harsh thermal conditions of the Pleistocene ice ages. To this end, we have carried out a comparative biochemical-biophysical characterization of the structural and functional properties of recombinant hemoglobins (rHb) from woolly mammoth (rHb WM) and Asian elephant (rHb AE) in relation to human hemoglobins Hb A and Hb A(2) (a minor component of human blood). We have obtained oxygen equilibrium curves and calculated O(2) affinities, Bohr effects, and the apparent heat of oxygenation (ΔH) in the presence and absence of allosteric effectors [inorganic phosphate and inositol hexaphosphate (IHP)]. Here, we show that the four Hbs exhibit distinct structural properties and respond differently to allosteric effectors. In addition, the apparent heat of oxygenation (ΔH) for rHb WM is less negative than that of rHb AE, especially in phosphate buffer and the presence of IHP, suggesting that the oxygen affinity of mammoth blood was also less sensitive to temperature change. Finally, (1)H NMR spectroscopy data indicates that both α(1)(β/δ)(1) and α(1)(β/δ)(2) interfaces in rHb WM and rHb AE are perturbed, whereas only the α(1)δ(1) interface in Hb A(2) is perturbed compared to that in Hb A. The distinct structural and functional features of rHb WM presumably facilitated woolly mammoth survival in the Arctic environment. Yue Yuan, Tong-Jian Shen, Priyamvada Gupta, Nancy T. Ho, Virgil Simplaceanu, Tsuey Chyi S. Tam, Michael Hofreiter, Alan Cooper, Kevin L. Campbell and Chien Ho |
format |
Article in Journal/Newspaper |
author |
Yuan, Y. Shen, T. Gupta, P. Ho, N. Simplaceanu, V. Tam, T. Hofreiter, M. Cooper, A. Campbell, K. Ho, C. |
author_facet |
Yuan, Y. Shen, T. Gupta, P. Ho, N. Simplaceanu, V. Tam, T. Hofreiter, M. Cooper, A. Campbell, K. Ho, C. |
author_sort |
Yuan, Y. |
title |
A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
title_short |
A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
title_full |
A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
title_fullStr |
A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
title_full_unstemmed |
A biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
title_sort |
biochemical-biophysical study of hemoglobins from woolly mammoth, asian elephant, and humans |
publisher |
Amer Chemical Soc |
publishDate |
2011 |
url |
http://hdl.handle.net/2440/67455 https://doi.org/10.1021/bi200777j |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_relation |
Biochemistry, 2011; 50(34):7350-7360 0006-2960 1520-4995 http://hdl.handle.net/2440/67455 doi:10.1021/bi200777j Cooper, A. [0000-0002-7738-7851] |
op_rights |
© 2011 American Chemical Society |
op_doi |
https://doi.org/10.1021/bi200777j |
container_title |
Biochemistry |
container_volume |
50 |
container_issue |
34 |
container_start_page |
7350 |
op_container_end_page |
7360 |
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1766343033788301312 |