Abstract
AbstractTransient electric dichroism has been measured for a Cu(II)–bovine serum albumin (BSA)–2‐(2‐pyridylazo)‐1‐naphthol (αPAN) complex at pH 5.5–12. From the magnitude of the reduced linear dichroism and the disorientation rate of the oriented chromophore, at least three kinds of binding states of Cu(αPAN)+ complex exist. They are present predominantly at pH 5.5–10, 7.5–10, and 10–12, with the αPAN plane approximately parallel, vertical, and parallel with respect to the oriented axis of a BSA molecule.
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