Premium
Quinacrine mustard and lipophilic cations inhibitory to both vacuolar H + ‐ATPase and F 0 F 1 ‐ATP synthase
Author(s) -
Moriyama Yoshinori,
Patel Vikram,
Futai Masamitsu
Publication year - 1995
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(95)00013-y
Subject(s) - atpase , dithiothreitol , protein subunit , atp synthase , biochemistry , chemistry , atp synthase gamma subunit , binding site , v atpase , enzyme , microbiology and biotechnology , biology , atp hydrolysis , gene
Various lipophilic cations, such as quinacrine mustard and dequalinium, which are known to inhibit mitochondrial F 1 ‐ATPase, strongly inhibited vacuolar H + ‐ATPase purified from bovine adrenal chromaffin granules. Quinacrine mustard bound irreversibly to vacuolar H + ‐ATPase subunit A , and the 115 kDa accessory polypeptide and dithiothreitol had no effect. The binding was competitively inhibited by chlorpromazine and quinacrine, and these compounds specifically reduced the amount of labeling of subunit A . Quinacrine mustard also prevented the binding of [α‐ 32 P]ATP to subunit A but had no effect on the binding of to either subunit A or the 115 kDa accessory polypeptide. These results suggest that the binding site of quinacrine mustard in subunit A is not related to the N ‐ethylmaleimide‐binding site(s), which is important for activity.