Studies directed toward the elucidation of the structures of the metal centers in cytochrome c oxidase are reviewed. Progress towards an understanding of the interactions between these centers and their spatial distributions within the protein is also presented. The authors have employed nitric oxide (NO), as well as other exogenous ligands, to probe the O//2 reduction site of the enzyme. In addition, we have isolated auxotrophs of Saccharomyces cerevisiae in order to metabolically incorporate isotopically substituted amino acids into the yeast protein.
|Number of pages||11|
|Publication status||Published - 1982|
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