Meso-tetra(2,6-dichlorophenyl)porphinatoiron(iii) chloride and meso-tetra(pentachlorophenyl)porphinatoiron(iii) chloride, which resist y-0x0 dimer formation and oxidative destruction, are found to be unusually efficient catalysts for high-turnover, high-yield al kene epoxidation and alkane hydroxylation.

the active site increases the local concentration of the reagent in the site as compared with the concentration in free solution, and thus results in the preferential formation of covalent bonds with amino acid residues within the site as compared with similar residues elsewhere on the protein molecule.The method has been tested successfully with three different antihapten rabbit Ab systems so far: (1)

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The blue copper proteins have been the focus of many spectroscopic and structural studies,1 with much of the interest centering on the nature of the copper site. X-ray crystallographic results have previously been reported for two single-copper proteins, plastocyanin and azurin. The structure of the oxidized, Cu(II),

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