FN Archimer Export Format PT J TI Globin's structure and function in vesicomyid bivalves from the Gulf of Guinea cold seeps as an adaptation to life in reduced sediments BT AF DECKER, Carole ZORN, N. POTIER, N. LEIZE-WAGNER, E. LALLIER, F.H. OLU, Karine ANDERSEN, A. C. AS 1:1,2,3;2:4;3:4;4:4;5:2,3;6:1;7:2,3; FF 1:PDG-REM-EEP-LEP;2:;3:;4:;5:;6:PDG-REM-EEP-LEP;7:; C1 IFREMER, Lab Environm Profond, Unite Rech Etud Ecosyst Profonds, F-29280 Plouzane, France. Univ Paris 06, Sorbonne Univ, Equipe Adaptat & Biol Invertebres Condit Extreme, UMR 7144,Stn Biol, F-29680 Roscoff, France. CNRS, UMR 7144, Stn Biol, F-29680 Roscoff, France. CNRS Univ Louis Pasteur Chim Mat Complexe, UMR 7140, Lab Spectrometrie Masse Interact & Syst, F-67008 Strasbourg, France. C2 IFREMER, FRANCE UNIV PARIS 06, FRANCE CNRS, FRANCE CNRS, FRANCE SI BREST SE PDG-REM-EEP-LEP IN WOS Ifremer jusqu'en 2018 copubli-france copubli-univ-france IF 2.398 TC 12 TU Centre national de la recherche scientifique Université Pierre et Marie Curie Université de Strasbourg UR https://archimer.ifremer.fr/doc/00245/35602/34150.pdf LA English DT Article CR CONGOLOBE WACS BO Pourquoi pas ? AB 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. PY 2014 PD NOV SO Physiological And Biochemical Zoology SN 1522-2152 PU Univ Chicago Press VL 87 IS 6 UT 000345865800008 BP 855 EP 869 DI 10.1086/678131 ID 35602 ER EF