Premium
The F 1 F 0 ‐ATPase binding site of dibutyltin‐3‐hydroxyflavone: Interactions with venturicidin, oligomycin and DCCD
Author(s) -
Griffiths David E,
Usta Julnar,
Tian Ya Min
Publication year - 1993
Publication title -
applied organometallic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 71
eISSN - 1099-0739
pISSN - 0268-2605
DOI - 10.1002/aoc.590070607
Subject(s) - chemistry , oligomycin , atpase , stereochemistry , binding site , biophysics , crystallography , enzyme , biochemistry , biology
Dibutyltin‐3‐hydroxyflavone bromide, Bu 2 Sn(of), is a fluorescent probe inhibitor of mitochondrial F 1 F 0 ATPase which reacts with and titrates a component of F 0 with marked fluorescence enhancement and reacts similarly with chloroplast CF 1 CF 0 and V‐ATPases. Its use to monitor the interactions of other F 0 inhibitors (venturicidin, oligomycin, DCCD) with F 1 F 0 ATPase, both membrane‐bound and purified by solubilization is described. Trialkyltins (Bu 3 SnCl) back‐titrate all Bu 2 Sn(of) interaction sites; whereas the macrolide inhibitor venturicidin backtitrates 60±5% and oligomycin only 30±3% of Bu 2 Sn(of) interaction sites. Bafilomycin, the macrolide inhibitor of V‐ATPases, is inactive in this assay. DCCD acts in a different fashion from the other inhibitors. Current and potential applications of this fluorescent probe in mitochondrial bioenergetics and biogenesis are discussed.