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| Decker, Carole; Zorn, N.; Le Bruchec, J.; Caprais, Jean-claude; Potier, N.; Leize-wagner, E.; Lallier, F. H.; Olu, Karine; Andersen, A. C.. |
| Vesicomyids live in endosymbiosis with sulfur-oxidizing bacteria and therefore need hydrogen sulfide to survive. They can nevertheless live in a wide range of sulfide and oxygen levels and depths, which may explain the exceptional diversity of this clam family in deep-sea habitats. In the Gulf of Guinea, nine species of vesicomyid clams are known to live in cold-seep areas with pockmarks from 600 to 3200 m deep, as well as in the organic-rich sediments of the Congo deep-sea fan at 5000 m deep. Our previous study showed that two species living in a giant pockmark have different oxygen carriers, suggesting different adaptations to hypoxia. Here, we studied the hemoglobin structure and oxygen affinity in three other species, Calyptogena valdiviae, Elenaconcha... |
| Tipo: Text |
Palavras-chave: Hemoglobin; Mass spectrometry; Oxygen affinity; Symbiont-bearing bivalve; Blood-clams; Cold seeps; Sulfide-rich sediments. |
| Ano: 2017 |
URL: http://archimer.ifremer.fr/doc/00358/46961/46875.pdf |
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| Tosqui,P.; Bonini-Domingos,C.R.; Colombo,M.F.. |
| The role of chloride in the stabilization of the deoxy conformation of hemoglobin (Hb), the low oxygen affinity state, has been studied in order to identify the nature of this binding. Previous studies have shown that arginines 141α could be involved in the binding of this ion to the protein. Thus, des-Arg Hb, human hemoglobin modified by removal of the α-chain C-terminal residue Arg141α, is a possible model for studies of these interactions. The loss of Arg141α and all the salt bridges in which it participates is associated with subtle structural perturbations of the α-chains, which include an increase in the conformational flexibility and further shift to the oxy state, increasing oxygen affinity. Thus, this Hb has been the target of many studies of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Des-Arg hemoglobin; Oxygen affinity. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000600004 |
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