ATP-ADP translocase (the adenine nucleotide translocator) is just one of several targets that classic oxidative phosphorylation inhibitors act on, so this question is best answered by pinning down exactly where each drug binds.
- Oligomycin: Binds the $F_o$ portion of ATP synthase and blocks the proton channel through the enzyme. This stops ATP synthesis at the synthase itself, upstream of where the translocator works, so it does not act on the translocase.
- Atractyloside: A glycoside from a thistle plant that binds the adenine nucleotide translocator on its cytoplasmic-facing side, freezing it in the outward-open state and stopping it from binding ATP for export. This is a direct block of the translocase.
- Amytal: A barbiturate that blocks Complex I (NADH dehydrogenase), stopping electrons from NADH from entering the respiratory chain at all. This is far upstream of ATP export and does not touch the translocator.
- Bongkrekic acid: A toxin from Burkholderia gladioli that binds the same adenine nucleotide translocator, but from the matrix-facing side, locking it in the inward-open state instead. Like atractyloside, this directly blocks the ADP/ATP exchange, just by trapping the opposite conformation of the same carrier.
Since only atractyloside and bongkrekic acid physically bind and lock the ATP-ADP translocase (from opposite faces of the membrane), while oligomycin and amytal act on entirely different proteins in the respiratory chain, the translocase-specific inhibitors are atractyloside and bongkrekic acid.
Let's summarize:
- Oligomycin blocks ATP synthase, not the translocase.
- Amytal blocks Complex I, not the translocase.
- Atractyloside and bongkrekic acid both bind the ATP-ADP translocase, locking it in opposite conformations.
The drugs that inhibit ATP-ADP translocase are atractyloside and bongkrekic acid.