The protein binding by quinone pigment: Covalent binding of juglone to protein and inhibition on mitochondrial ATPase activity

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概要

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• The mode of protein binding by juglone, a naphthoquinone pigment which shows an uncoupling effect on oxidative phosphorylation of isolated mitochondria, was spectrophotometrically studied. Juglone was found to covalently bind to bovine serum albumin (BSA) with a molar ratio of unity. It was suggested that not 5-hydroxyl group but 2-or 3-carbon atom of the naphthoquinone ring linked to SH group of BSA to form a thioether. Juglone inhibited the ATPase activity of mitochondria but the potency in the inhibitory effect was markedly decreased by adding cysteine to the system. The ATPase activity of mitochondria mechanically destroyed was merely weakly inhibited. These results suggested that juglone inhibits the ATPase activity of mitochondria not by a direct interaction with coupling factor but by an inhibition on the translocation system of inorganic phosphate or adenine nucleotide(s), which is sensitive to the inhibitions by SH reagents.

• 日本マイコトキシン学会の論文

日本マイコトキシン学会 | 論文

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