Inhibition of Urease, a Ni‐Enzyme: The Reactivity of a Key Thiol With Mono‐ and Di‐Substituted Catechols Elucidated by Kinetic, Structural, and Theoretical Studies

The inhibition of urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) by a class six aromatic poly-hydroxylated molecules, namely mono- dimethyl-substituted catechols, was investigated on the basis inhibitory efficiency catechol scaffold. aim to probe key step mechanism proposed for SPU catechol, sulfanyl radical attack ring, as well obtain critical information effect substituents ring efficacy its derivatives. crystal structures all SPU-inhibitors complexes, determined at high resolution, kinetic data obtained JBU theoretical studies reaction using quantum mechanical calculations, revealed occurrence an irreversible inactivation means radical-based autocatalytic multistep mechanism, indicate that, among tested mono-substituted 3-methyl-catechol is most efficient inhibitor urease.