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DOI | 10.1073/pnas.2023936118 |
Evolved increases in hemoglobin-oxygen affinity and the Bohr effect coincided with the aquatic specialization of penguins | |
Signore A.V.; Tift M.S.; Hoffmann F.G.; Schmitt T.L.; Moriyama H.; Storz J.F. | |
发表日期 | 2021 |
ISSN | 00278424 |
卷号 | 118期号:13 |
英文摘要 | Dive capacities of air-breathing vertebrates are dictated by onboard O2 stores, suggesting that physiologic specialization of diving birds such as penguins may have involved adaptive changes in convective O2 transport. It has been hypothesized that increased hemoglobin (Hb)-O2 affinity improves pulmonary O2 extraction and enhances the capacity for breath-hold diving. To investigate evolved changes in Hb function associated with the aquatic specialization of penguins, we integrated comparative measurements of whole-blood and purified native Hb with protein engineering experiments based on site-directed mutagenesis. We reconstructed and resurrected ancestral Hb representing the common ancestor of penguins and the more ancient ancestor shared by penguins and their closest nondiving relatives (order Procellariiformes, which includes albatrosses, shearwaters, petrels, and storm petrels). These two ancestors bracket the phylogenetic interval in which penguin-specific changes in Hb function would have evolved. The experiments revealed that penguins evolved a derived increase in Hb-O2 affinity and a greatly augmented Bohr effect (i.e., reduced Hb-O2 affinity at low pH). Although an increased Hb-O2 affinity reduces the gradient for O2 diffusion from systemic capillaries to metabolizing cells, this can be compensated by a concomitant enhancement of the Bohr effect, thereby promoting O2 unloading in acidified tissues. We suggest that the evolved increase in Hb-O2 affinity in combination with the augmented Bohr effect maximizes both O2 extraction from the lungs and O2 unloading from the blood, allowing penguins to fully utilize their onboard O2 stores and maximize underwater foraging time. © 2021 National Academy of Sciences. All rights reserved. |
英文关键词 | Adaptation; Bohr effect; Hemoglobin; Hypoxia; Penguins |
语种 | 英语 |
scopus关键词 | hemoglobin; oxygen; adaptation; aquatic species; Article; binding affinity; Bohr effect; ecological specialization; evolution; hypoxia; nonhuman; oxygen diffusion; penguin; phylogeny; priority journal; protein function |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America
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文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/180076 |
作者单位 | School of Biological Sciences, University of Nebraska, Lincoln, NE 68588, United States; Department of Biology and Marine Biology, University of North Carolina, Wilmington, NC 28403, United States; Department of Biochemistry, Molecular Biology, Entomology, and Plant Pathology, Mississippi State University, Starkville, MS 39762, United States; Institute for Genomics,, Biocomputing and Biotechnology, Mississippi State University, Starkville, MS 39762, United States; Veterinary Services, SeaWorld of California, San Diego, CA 92109, United States |
推荐引用方式 GB/T 7714 | Signore A.V.,Tift M.S.,Hoffmann F.G.,et al. Evolved increases in hemoglobin-oxygen affinity and the Bohr effect coincided with the aquatic specialization of penguins[J],2021,118(13). |
APA | Signore A.V.,Tift M.S.,Hoffmann F.G.,Schmitt T.L.,Moriyama H.,&Storz J.F..(2021).Evolved increases in hemoglobin-oxygen affinity and the Bohr effect coincided with the aquatic specialization of penguins.Proceedings of the National Academy of Sciences of the United States of America,118(13). |
MLA | Signore A.V.,et al."Evolved increases in hemoglobin-oxygen affinity and the Bohr effect coincided with the aquatic specialization of penguins".Proceedings of the National Academy of Sciences of the United States of America 118.13(2021). |
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