Globin's structure and function in vesicomyid bivalves from the Gulf of Guinea cold seeps as an adaptation to life in reduced sediments

Type Article
Date 2014-11
Language English
Author(s) Decker Carole1, 2, 3, Zorn N.4, Potier N.4, Leize-Wagner E.4, Lallier F.H.2, 3, Olu KarineORCID1, Andersen A. C.2, 3
Affiliation(s) 1 : IFREMER, Lab Environm Profond, Unite Rech Etud Ecosyst Profonds, F-29280 Plouzane, France.
2 : Univ Paris 06, Sorbonne Univ, Equipe Adaptat & Biol Invertebres Condit Extreme, UMR 7144,Stn Biol, F-29680 Roscoff, France.
3 : CNRS, UMR 7144, Stn Biol, F-29680 Roscoff, France.
4 : CNRS Univ Louis Pasteur Chim Mat Complexe, UMR 7140, Lab Spectrometrie Masse Interact & Syst, F-67008 Strasbourg, France.
Source Physiological And Biochemical Zoology (1522-2152) (Univ Chicago Press), 2014-11 , Vol. 87 , N. 6 , P. 855-869
DOI 10.1086/678131
WOS© Times Cited 12
Abstract Vesicomyid bivalves form dense clam beds in both deep-sea cold seeps and hydrothermal vents. The species diversity within this family raises questions about niche separation and specific adaptations. To compare their abilities to withstand hypoxia, we have studied the structure and function of erythrocyte hemoglobin (Hb) and foot myoglobin (Mb) from two vesicomyid species, Christineconcha regab and Laubiericoncha chuni, collected from the Regab pockmark in the Gulf of Guinea at a depth of 3,000 m. Laubiericoncha chuni possesses three monomeric globins, G1 (15,361 Da), G2 (15,668 Da), and G3 (15,682 Da) in circulating erythrocytes (Hb), and also three globins, G1, G3, and G4 (14,786 Da) in foot muscle (Mb). Therefore, globins G2 and G4 appear to be specific for erythrocytes and muscle, respectively, but globins G1 and G3 are common. In contrast, C. regab lacks erythrocyte Hb completely and possesses only globin monomers G1 (14,941 Da), G2 (15,169 Da), and G3 (15,683 Da) in foot muscle. Thus, these two vesicomyid species, C. regab and L. chuni, show a remarkable diversity in globin expression when examined by electrospray ionization mass spectrometry. Oxygen-binding affinities reveal extremely high oxygen affinities (P-50 < 1 Torr, from 5 degrees to 15 degrees C at pH 7.5), in particular L. chuni globins, which might be an advantage allowing L. chuni to dig deeply for sulfides and remain buried for long periods in reduced sediments.
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Decker Carole, Zorn N., Potier N., Leize-Wagner E., Lallier F.H., Olu Karine, Andersen A. C. (2014). Globin's structure and function in vesicomyid bivalves from the Gulf of Guinea cold seeps as an adaptation to life in reduced sediments. Physiological And Biochemical Zoology, 87(6), 855-869. Publisher's official version : , Open Access version :