ArticleNature communications2024
The unique allosteric property of crocodilian haemoglobin elucidated by cryo-EM.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Laser phase plate improves structure determination of small proteins by cryo-EM.Science (New York, N.Y.) · 2026Article
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- Developmental and Evolutionary Heart Adaptations Through Structure-Function Relationships.Journal of cardiovascular development and disease · 2025Review
- Effects of allosteric effectors on oxygen binding to crystals of hemoglobin in the R-quaternary structure.Protein science : a publication of the Protein Society · 2025Article
- Hemoglobin as an oxygen gasoreceptor.Acta biochimica Polonica · 2025Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The principal effect controlling the oxygen affinity of vertebrate haemoglobins (Hbs) is the allosteric switch between R and T forms with relatively high and low oxygen affinity respectively. Uniquely among jawed vertebrates, crocodilians possess Hb that shows a profound drop in oxygen affinity in the presence of bicarbonate ions. This allows them to stay underwater for extended periods by consuming almost all the oxygen present in the blood-stream, as metabolism releases carbon dioxide, whose conversion to bicarbonate and hydrogen ions is catalysed by carbonic anhydrase. Despite the apparent universal utility of bicarbonate as an allosteric regulator of Hb, this property evolved only in crocodilians. We report here the molecular structures of both human and a crocodilian Hb in the deoxy and liganded states, solved by cryo-electron microscopy. We reveal the precise interactions between two bicarbonate ions and the crocodilian protein at symmetry-related sites found only in the T state. No other known effector of vertebrate Hbs binds anywhere near these sites.
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