Chemical modification of the brown fat mitochondrial uncoupling protein with tetranitromethane

Abstract
Tetranitromethane reacts with the uncoupling protein of intact brown fat mitochondria. The chloride permeability in the absence of the inhibitory nucleotide GDP is not affected, but the affinity with which GDP binds is decreased, and the coupling between binding of nucleotide and inhibition of chloride permeation is broken.