New Protein Reagents. N-(4-Chloromercuriphenyl)-4-Chloro-3,5-Dinitrobenzamide and Its Use as a Probe of the Quaternary Structure of Yeast Alcohol Dehydrogenase

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Abstract
The new bifunctional reagent, N-(4-chloromercuriphenyl)-4-chloro-3,5-dinitrobenzamide was used to investigate the quaternary structure of yeast alcohol dehydrogenase [EC 1.1.1.1]. The 4 essential -SH groups of the enzyme were substituted by the mercuriphenyl moiety of compound I in the course of the reaction of 1 mol of protein with 4 mol of the reagent (1 molecule of compound I incorporated by yeast alcohol dehydrogenase monomer). In a 2nd step only 2 of the 4 chlorodinitrophenyl fragments bound to the protein established intermonomeric cross-links with non-essential -NH2 groups. The resulting dimers could be re-dissociated with mercaptoethanol. This result suggests that the 4 protomers of the enzyme could be arranged as a dimer of dimers.