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Inhibition of the mitochondrial tricarboxylate carrier by arginine‐specific reagents
Author(s) -
Stipani I.,
Zara V.,
Zaki L.,
Prezioso G.,
Palmieri F.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80913-9
Subject(s) - arginine , chemistry , reagent , biochemistry , mitochondrial carrier , amino acid , escherichia coli , organic chemistry , bacterial outer membrane , gene
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.

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