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- W1640097718 abstract "Abstract Purified beef heart cytochrome c oxidase is inactivated to the extent of 35 to 50% by the nonpolar mercurial reagents mercuric chloride and ethylmercuric chloride. The inactivation is complete within 5 min. In titrations of activity, the plateau level of inactivation is attained at added ethylmercuric chloride:heme a ratios of about 1:1. Up to 3 mercury atoms/heme a are bound to the oxidase, although only the first of these affects its enzymatic activity. Incubation of the ethylmercury-modified oxidase with sulfhydryl compounds reverses the inactivation, with 2,3-dimercaptopropanol being most effective of the reagents tested. Spectrophotometric and polarographic assays of enzymatic activity show that Km values for the native and the ethylmercury-modified enzymes are practically indistinguishable, and that the partial inactivation observed for the latter is reflected exclusively in a lower value of Vmax compared to that of the native enzyme. Based on these results, we propose that ethylmercuric chloride reacts with a single crucial--SH group per heme a, and that electron transfer processes in the modified product are partially inhibited." @default.
- W1640097718 created "2016-06-24" @default.
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- W1640097718 date "1980-01-01" @default.
- W1640097718 modified "2023-09-26" @default.
- W1640097718 title "Partial inactivation of cytochrome c oxidase by nonpolar mercurial reagents." @default.
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- W1640097718 doi "https://doi.org/10.1016/s0021-9258(19)86195-1" @default.
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