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EEDQ probably reacts with the Mg 2+ ‐ATP catalytic sites of mitochondrial and bacterial F 1 ‐ATPases
Author(s) -
Pougeois Richard
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)80872-2
Subject(s) - chemistry , reagent , catalysis , atpase , mitochondrion , stereochemistry , biochemistry , medicinal chemistry , enzyme , organic chemistry
The carboxyl reagent N ‐ethoxycarbonyl‐2‐ethoxy‐1,2‐dihydroquinoline (EEDQ) inactivated ATPase activities of isolated MF 1 and BF 1 when assayed in an MgCl 2 medium, but not in an EDTA medium. However, another carboxyl reagent, N,N′ ‐dicyclohexylcarbodiimide (DCCD) was found to inhibit MF 1 and BF 1 when assayed either in the presence of MgCl 2 or EDTA. These data suggest that EEDQ interferes with the binding of Mg 2+ at catalytic sites of both MF 1 and BF 1 and that EEDQ on one hand, and DCCD on the other, react with different carboxyl groups on MF 1 and BF 1 .