S. R. Pauleta

Thermal stability and kinetic unfolding of Neisseria gonorrhoeae copper nitrite reductase.

The results show that enzyme unfolding is irreversible and kinetically controlled and is best described by a three-state Lumry-Eyring model involving a reversible intermediate followed by an irreversible transition to an aggregated stated, likely contributing to enzyme robustness under the dynamic conditions encountered during host-pathogen interactions.