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• W1518784693 abstract "The soluble catalytic domain of NADH-cytochrome b5 reductase was radiolabeled with [14C]N-ethylmaleimide. Reaction for a limited time resulted in incorporation of 0.41 eq of N-ethylmaleimide and loss of 36% of the enzyme activity. Chromatography on a 5'-ADP affinity column separated the reductase which was modified with N-ethylmaleimide from the unreacted enzyme; the isolated derivative constituted 37% of the total material, was completely inactivated, and contained 1.00 eq of N-ethylmaleimide. Cyanogen bromide cleavage of the derivative demonstrated that radioactivity was limited to a single peptide which contained both Cys-283 and Cys-297. Tryptic hydrolysis of this cyanogen bromide peptide showed that the radioactivity was associated with Cys-283. Automated sequenator analysis confirmed that Cys-283 was the radiolabeled residue. These data demonstrate unambiguously that Cys-283 provides the essential thiol group of cytochrome b5 reductase." @default.
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• W1518784693 date "1986-07-01" @default.
• W1518784693 modified "2023-09-28" @default.
• W1518784693 title "Identification of the essential cysteine residue of NADH-cytochrome b5 reductase." @default.
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• W1518784693 doi "https://doi.org/10.1016/s0021-9258(18)67594-5" @default.
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• W1518784693 hasPublicationYear "1986" @default.
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