Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific 
reagents

Stipani, I.; Zara, V.; Zaki, Laila; Prezioso, G.; Palmieri, F.

doi:10.1016/0014-5793(86)80913-9

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Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific reagents

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Zaki, Laila
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Stipani, I., Zara, V., Zaki, L., Prezioso, G., & Palmieri, F. (1986). Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific reagents. FEBS Letters, 205(2), 282-286. doi:10.1016/0014-5793(86)80913-9.

Cite as: https://hdl.handle.net/21.11116/0000-0008-185B-8

Abstract

The effect of arginine-specific reagents on the activity of the partially purified and reconstituted tricarboxylate carrier of the inner mitochondrial membrane has been studied. It has been found that 1,2-cyclohexanedione, 2,3-butanedione, phenylglyoxal and phenylglyoxal derivatives inhibit the reconstituted citrate/citrate exchange activity. The inhibitory potency of the phenylglyoxal derivatives increases with increasing hydrophilic character of the molecule. Citrate protects the tricarboxylate carrier against inactivation caused by the arginine-specific reagents. Other tricarboxylates, which are not substrates of the carrier, have no protective effect. The results indicate that at least one essential arginine residue is located at the substrate-binding site of the tricarboxylate carrier and that the vicinity of the essential arginine(s) has a hydrophilic character.