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• W193624147 endingPage "197" @default.
• W193624147 startingPage "145" @default.
• W193624147 abstract "The structural comparison of copper-containing proteins provides a new dimension to the relationships suggested by sequence similarities. The structures reveal the fact that the differences reside primarily in the insertions and deletions at junctions between secondary-structure elements. Copper is critical to a variety of proteins with functions ranging from electron transfer to oxygen transport to active chemistry, such as insertion of oxygen in a substrate. Selected copper-containing proteins are tabulated. Copper proteins are classified according to their spectroscopic properties as type I, II, and III. Type I blue copper proteins are characterized by an extraordinarily intense absorption near 600 nm and by unusually small hyperfine coupling constants for the paramagnetic [oxidized Cu (II)] form of the protein. Type II sites have normal extinction coefficients, are found to have larger hyperfine coupling constants, and are paramagnetic in the Cu (II) form. Type III copper is characterized by antiferromagnetic coupling of a pair of copper atoms and strong absorbance at 330 nm. This chapter focuses on the copper protein structures for which there are X-ray structures, such as cupredoxins, superoxide dismutase, or hemocyanin, and includes others in as much as they are known to be related to the structurally characterized ones." @default.
• W193624147 created "2016-06-24" @default.
• W193624147 creator A5089029176 @default.
• W193624147 date "1991-01-01" @default.
• W193624147 modified "2023-10-10" @default.
• W193624147 title "Copper Protein Structures" @default.
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