Type II DNA topoisomerases actively reduce the fractions of knotted and cat
enated circular DNA below thermodynamic equilibrium values. To explain this
surprising finding, we designed a model in which topoisomerases introduce
a sharp bend in DNA. Because the enzymes have a specific orientation relati
ve to the bend, they act like Maxwell's demon, providing unidirectional str
and passage. Quantitative analysis of the model by computer simulations pro
ved that it can explain much of the experimental data. The required sharp D
NA bend was demonstrated by a greatly increased cyclization of short DNA fr
agments from topoisomerase binding and by direct visualization with electro
n microscopy.