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Tetrathiomolybdate inhibition of the Enterococcus hirae CopB copper ATPase
Author(s) -
Bissig Karl-Dimiter,
Voegelin Thomas Christophe,
Solioz Marc
Publication year - 2001
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/s0014-5793(01)03009-5
Subject(s) - enterococcus hirae , copper , atpase , chemistry , ic50 , biochemistry , enzyme , enterococcus , in vitro , organic chemistry , antibiotics
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.