Small-Molecule Tunnels in Metalloenzymes Viewed as Extensions of the Active Site.

ABSTRACT: Rigorous substrate selectivity is a hallmark of enzyme catalysis. This selectivity is generally ascribed to a thermodynamically favorable process of substrate binding to the enzyme active site based upon complementary physiochemical characteristics, which allows both acquisition and orientation. However, this chemical selectivity is more difficult to rationalize for diminutive molecules that possess too narrow a range of physical characteristics to allow either precise positioning or discrimination between a substrate and an inhibitor. Foremost among these small molecules are dissolved gases such as H₂, N₂, O₂, CO, CO₂, NO, N₂O, NH₃, and CH₄ so often encountered in metalloenzyme catalysis. Nevertheless, metalloenz

SUBMITTER: Banerjee R 

PROVIDER: S-EPMC8130187 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature