Tetrathiomolybdate inhibition of the Enterococcus hirae CopB copper ATPase.
Tetrathiomolybdate (TTM) avidly interacts with copper and has recently been employed to reduce excess copper in patients with Wilson disease. We found that TTM inhibits the purified Enterococcus hirae CopB copper ATPase with an IC(50) of 34 nM. Dithiomolybdate and trithiomolybdate, which commonly contaminate TTM, inhibited the copper ATPases with similar potency. Inhibition could be reversed by copper or silver, suggesting inhibition by substrate binding. These findings for the first time allowed an estimate of the high affinity of CopB for copper and silver. TTM is a new tool for the study of copper ATPases.
Bissig
K D
KD
Department of Clinical Pharmacology, University of Berne, Murtenstrasse 35, 3010, Berne, Switzerland.
Voegelin
T C
TC
Solioz
M
M
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D027682:Cation Transport Proteins / Q000037:antagonists & inhibitors*; D003300:Copper / Q000494:pharmacology; D000079922:Copper Transport Proteins; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D008982:Molybdenum / Q000494:pharmacology*; D011804:Quinolines / Q000494:pharmacology; D012834:Silver / Q000494:pharmacology
D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; D004791:Enzyme Inhibitors; D011804:Quinolines; D012834:Silver; D003300:Copper; D008982:Molybdenum; C020809:tetrathiomolybdate; C047117:bicinchoninic acid; D000251:Adenosine Triphosphatases; C088359:CopB ATPase, Enterococcus hirae