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Hemoglobin (Hb) is a tetrameric protein that consists of two α and two β subunits represented by α2β2 and transports oxygen from lungs to tissues for use in respirat ion. The α and β subunits are structurally and evolutionarily related to each other, and each subunit has an oxygen binding site which is called heme. Thus, Hb can bind a total of four oxygen molecules. It is well known that Hb is not only a s imple oxygen tank , bu t a lso func t ions as a sophisticated oxygen delivery system to provide the proper amount of oxygen to tissues under a wide variety of circumstances. This feature is closely related to a cooperative interaction between oxygen binding sites; that is, the binding of oxygen at one subunit increases the affinity for additional oxygen at another subunit. In this context, Hb has played a central role in exploring the mechanism of the cooperative interaction of proteins in general. It is well established by X-ray crystallographic studies that Hb has two end-structures which are called relaxed (or R) and tense (or T-) states, which correspond to high and low oxygen affinities, respectively [1]. However, intermediate structures between the two end-structures, which must be related to a key structure to understand the cooperative regulation mechanism of Hb, have not been directly observed yet. In particular, the essential part of the mechanism

3SB04 Direct observation of photolysis-induced structural changes in hemoglobin