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Inhibition study of ADP,ATP transport in mitochondria with trinitrophenyl‐modified substrates
Author(s) -
Schlimme E.,
Boos K.-S.,
Onur G.,
Ponse G.
Publication year - 1983
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(83)80197-5
Subject(s) - moiety , mitochondrion , chemistry , nucleotide , biochemistry , atp–adp translocase , phosphate , electron transport chain , inhibitory postsynaptic potential , atp synthase , adenosine triphosphate , chemiosmosis , stereochemistry , enzyme , inner mitochondrial membrane , biology , neuroscience , gene
The ADP,ATP carrier of rat liver mitochondria is specifically inhibited by Meisenheimer‐type trinitrophenyl (TNP) derivatives of ADP and ATP. Due to a systematic inhibition study we could show that the TNP‐moiety itself, even in the 2′, 3′‐ O ‐cyclic Meisenheimer complex, revealed no inhibition of mitochondrial ADP,ATP transport. Nucleosidic TNP‐compounds are weak inhibitors. Introduction of a phosphate group at the 5′‐position, however, enhances the inhibitory power markedly. Our findings point to a synergistic effect of the 5′‐phosphate chain and the TNP‐moiety. Irreversible inhibition by TNP‐nucleotides can be ruled out due to the fact that the inhibited ADP,ATP‐transport system is fully reactivated by addition of albumin.