By Robert P. Hausinger

In this well timed monograph, the writer summarizes the quickly turning out to be physique of data relating to nickel by means of supplying a balanced dialogue of its damaging and worthy results. insurance encompasses a historical past of nickel; the chemistry of nickel, descriptions of the 4 identified enzymes which comprise nickel; and nickel metabolism in microbes, vegetation, and animals. Taken as an entire, Dr. Hausinger's paintings will spotlight key good points of this crucial aspect and aid outline destiny research.

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1 BM at room temperature. 0023), true nickel(III) complexes exhibit anisotropic signals with significant deviations from the free-electron value. The EPR spectroscopic properties ofnickel(III) in an octahedral environment are provided as a specific example. To facilitate this discussion, energy level diagrams for compressed and elongated octahedral nickel species are provided in Fig. 2-4. In the lowest energy state, the seven d electrons of nickel(III) include three pairs occupying the lowest three orbitals and a lone electron in the next highest orbital.

Urease proteins were purified from each of the ten mutants and characterized for activity and nickel contents. Five of the conserved histidines (residue 96 in the 'Y subunit, residues 39 and 41 in the f) subunit, and residues 312 and 321 in the a subunit) have no catalytic function as shown by the lack of any effect when they were changed to alanine. Evidence for a role in nickel ligation was obtained for three histidines (residues 134, 136, and 246 in the a subunit): when these histidines were substituted by alanine, the proteins were inactive and possessed approximately 1, 0, and 0 nickel ions bound per catalytic unit.

Kiick, R. P. Hausinger, and M. K. Johnson, unpublished observations). In summary, the urease active site possesses two nickel atoms that probably function in substrate binding. The metal ions are bound, at least in part, by histidinyl ligands. The two nickel atoms are located very close together and appear to be magnetically coupled under some conditions. 4 Chemical Modification Studies of the Urease Active Site Protein chemical modification approaches have been used to provide information regarding the types of residues that serve as ligands to the me- 36 Chapter 3 tallocenter and to identify other residues that function at the active site.

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