The stoichiometry of binding of the aurovertins to mitochondrial ATPases: revision of the molar absorption coefficient.
The purity of aurovertins A, B, and D, which inhibit the mitochondrial ATPase and show fluorescence enhancement when bound, has been determined by high-resolution proton nuclear magnetic resonance. This technique demonstrated that solvent molecules, especially water, are tightly bound to crystalline aurovertins B and D. The molar absorption coefficient for aurovertins A, B, and D at the longest wavelength maximum (367.5-369 nm) has been determined to be 38,500 liter x mol(-1) x cm(-1). This correct molar absorption coefficient should enable correct binding stoichiometries for aurovertin to ATPases to be determined.
Linnett
P E
PE
Sittingbourne Research Center, Sittingbourne, Kent ME9 8AG, United Kingdom.
Mulheirn
L J
LJ
Beechey
R B
RB
D001203:Ascomycota / Q000378:metabolism; D001313:Aurovertins / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D001665:Binding Sites; D005453:Fluorescence; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D025261:Mitochondrial Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012997:Solvents; D013056:Spectrophotometry, Ultraviolet
D001313:Aurovertins; D012997:Solvents; C034402:aurovertin B; C039026:aurovertin D; D025261:Mitochondrial Proton-Translocating ATPases