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 discovering steel metabolism in organisms starting from micro organism to vegetation to animals are operating in a totally diversified zone of discovery than scientists learning the transportation and law of minerals and small molecule food. they're either operating with copper-containing proteins, yet in very other ways and with differing expected results.
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This spectroscopic evidence gave the ®rst clear demonstration that redox activation involved interconversion between discrete IAGO and AGO forms and provided a direct method for quantitating the extent of conversion (Whittaker and Whittaker, 1988). The optical spectrum of reductively inactivated enzyme (IAGO) is perturbed by ligand binding, resulting in decreased intensity and a shift of the absorption maximum to higher energy (Fig. 13A). These spectral changes imply a change in the effective geometry at the Cu(II) center and are consistent with a distortion toward square planar coordination of the metal ion (Fig.
Essentially concerted despite the different character of the two redox sites in the protein. Dissociation of the aldehyde product would leave a low-coordinate, Cu(I) redox center associated with two protonated tyrosine phenols in the active site. , 1998). This extremely fast reaction makes it dif®cult to investigate by conventional rapid reaction techniques, and the nature of the 40 JAMES W. WHITTAKER oxygenated complex remains speculative. One clue to the nature of the oxy complex may be derived from a detailed inspection of the structure of the IAGO active site.
As mentioned earlier (Section V, C), the Cu(II) ion strongly interacts with the radical in the active enzyme (AGO), and the normal spectroscopic signatures of a free radical are absent. The strong interactions between the radical and the metal ion result in an EPR-silent complex and an unusual absorption spectrum that is clearly not a simple superposition of spectra for Cu(II) and a free radical (see below). However, a distinctive and unusual free radical EPR signal is consistently present as a minority species in EPR spectrum of oxidant-treated GAOX.
Copper-Containing Proteins by Joan Selverstone Valentine, Edith Butler Gralla (Eds.)