Conformational Differences Between Oxy- and Deoxy-Hemocyanin

摘要: As in the case of hemoglobin (1)the classic two-state allosteric model (2),based on presence two functionally relevant quaternary states macromolecule chemical equilibrium, is often adequate to describe cooperative effects binding O2 by hemocyanin (3,4). Nevertheless direct physical evidence for different conformational equilibrium (at best) very limited, with possible exception some observations(5,6). Recent spectroscopic studies have shown that upon at active site Cu-Cu distance and number ligands (7) bound metal atoms change, a strong involvement endogeneous protein bridge. This probably triggers change(s) involved 02. In order aquire experimental information ligand linked transition hemocyanins we applied autocorrelation spectroscopy probe internal mobility hydrodynamic properties oxy deoxy Helix p. β -hemocyanin (M.14.9 millions).