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013 vs. 0.5 s?1, respectively) and in an extremely high O2 affinity (215 vs. 46 ��M?1, respectively). Therefore, A. suum Hb cannot be deoxygenated at physiological O2 levels and cannot play a role in O2 transport/storage. For GLB-1 on the other hand, a function in O2 metabolism was proposed (14, 21). A second overlay was created to make a comparison between GLB-1 and the reference globin SwMb (Fig. 2b). The structural overlay between the globin domains of GLB-1 (PDB: 2WTG) and SwMb (PDB: 1MBN) results in a rmsd value of 3.107 ?, calculated over 85 C�� atom pairs. The structural differences are spread over the entire molecule, with residue insertions and deletions in the GLB-1 sequence toward http://www.selleckchem.com/products/Imatinib-Mesylate.html SwMb (14). The oxygenated state is very stable for both proteins. http://www.selleck.cn/products/mi-773-sar405838.html Indeed they were crystallized with an O2 molecule in the distal site coordinated to the heme Fe atom. The stabilization of the external ligand is achieved with an hydrogen bond to Tyr(35)B10 for GLB-1 and to His(65)E7 for SwMb. The heme group itself is stabilized by several van der Waals contacts and salt bridges. Within GLB-1, the heme A-propionate interacts with Arg(65)E3 and heme D-proprionate with Arg(99)F7. In contrast, the heme A- and D-propionates of SwMb interact with Ser(93)F7 and Arg(46)CD3, respectively. Several experiments on GLB-1 in solution were performed to study its physicochemical characteristics (14). First of all, ligand-binding kinetics were performed and revealed that the affinity for O2 was quite high (46 ��M?1), higher than the O2 affinity of SwMb (1.1 ��M?1), but lower than A. suum Hb (215��M?1). This difference is mainly due to the stronger stabilizing hydrogen bond by Tyr(48)B10 in A. suum Hb, resulting in a slower dissociation rate (0.013 s?1) compared with GLB-1 (0.5 s?1). From O2 equilibrium studies, the Hill coefficient could be calculated and showed to be smaller than 1 and independent of pH, suggesting that O2 binding has a negative cooperative behavior in the two subunits (14). CO binding kinetics are monophasic and interaction of CO with the heme environment is low (14). In vivo this protein is located in a small subset of neuronal http://www.selleckchem.com/products/VX-770.html cells and in the head muscular tissue (Supporting Information Table S2). During hypoxia, GLB-1 is upregulated 1.72 times (P