Oxygen binding by Helix pomatia alpha-haemocyanin studied by X-ray-absorption spectroscopy.
The X-ray absorption spectra of haemocyanin from Helix pomatia were obtained by using X-rays from synchrotron radiation. Cu K-edges were recorded at four conditions, namely fully oxygenated, 85% oxygenated, 12% oxygenated and fully deoxygenated. The percentage oxygenation calculated from the edge-shift of the partially oxygenated samples did not agree with the percentage oxygenation as determined by u.v. measurements. Two intermediates in the oxygenation process are presented to explain the observed dissimilarities.
D000818:Animals; D001665:Binding Sites; D003300:Copper; D006372:Helix, Snails / Q000032:analysis*; D006433:Hemocyanins / Q000378:metabolism*; D010100:Oxygen / Q000097:blood*; D011188:Potassium; D013057:Spectrum Analysis; D014965:X-Rays
D003300:Copper; D006433:Hemocyanins; D011188:Potassium; D010100:Oxygen