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Oxidative addition model oxygen-binding

Oxidative Addition Model of Oxygen Binding to Iron and Copper Proteins... [Pg.382]

The oxidative addition model for reversible O2 binding by metal proteins is also reasonable for hemocyanin. Hemocyanin is a copper protein which binds one O2 molecule for every two copper atoms. The deoxy Cu(I) form has no appreciable absorption in the visible region. When oxygenated, the protein is blue and exhibits a rich visible spectrum, wiA bands at 700 (c 75), 570 (c 500), 440 (c 65), and 347 nm (c 8900) (53). The pattern of bands around 570 nm leaves little doubt that oxyhemocyanin contains Cu(II) (53). The enhanced LF band intensities further suggest a dimeric Cu(II) complex. For comparison. [Pg.385]

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