Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific reagents

FEBS Letters
I StipaniF Palmieri

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.

References

Jan 1, 1979·Annual Review of Biochemistry·K F LaNoue, A C Schoolwerth
Jul 31, 1979·Molecular and Cellular Biochemistry·J F Riordan
May 1, 1975·Canadian Journal of Biochemistry·B H Robinson, J Oei
Nov 1, 1982·European Journal of Biochemistry·P MendeF Palmieri
Mar 16, 1981·Biochemical and Biophysical Research Communications·L Zaki
Oct 15, 1971·FEBS Letters·Francis E. SluseJoseph M. Tager

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