Chemistry

Copper-Containing Proteins by Joan Selverstone Valentine, Edith Butler Gralla (Eds.)

By Joan Selverstone Valentine, Edith Butler Gralla (Eds.)

A variety of researchers are at present investigating diverse houses and purposes for copper-containing proteins. Biochemists learning steel metabolism in organisms starting from micro organism to crops to animals are operating in a very assorted sector of discovery than scientists learning the transportation and law of minerals and small molecule nutrition. they're either operating with copper-containing proteins, yet in very alternative ways and with differing expected results.

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These spectroscopic observations provided the initial basis for assignment of a redox function to the Tyr±Cys side chain. Although this assignment is quite convincing in itself, positive identi®cation of a Tyr±Cys radical as the origin of the free radical EPR signal in oxidized apoGAOX requires further evidence. One line of evidence draws on the isotope sensitivity of EPR spectroscopy. Isotope perturbations can be very important in making structural assignments for EPR spectra, de®ning contributions from speci®c atoms in a sample.

Since the intense absorption of the active enzyme is associated with the presence of a free radical-copper active site, the spectra directly identify these two tyrosines as being involved in the free radical complex. The ligand-binding experiments on IAGO establishing the TyrON or TyrOFF character of the differ- GALACTOSE OXIDASE 25 ent ligation states suggest assignment of the normal and perturbed spectra to the coordinated Tyr±495 and Tyr±272, respectively. , 1996b). C. Electron Paramagnetic Resonance Electron paramagnetic resonance (EPR) spectroscopy is speci®cally sensitive to the presence of unpaired electrons in a sample that may be associated with transition metal ions and free radicals.

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