Polar Interactions between Substrate and Flavin Control Iodotyrosine Deiodinase Function.

ABSTRACT: Flavin cofactors offer a wide range of chemical mechanisms to support a great diversity in catalytic function. As a corollary, such diversity necessitates careful control within each flavoprotein to limit its function to an appropriate subset of possible reactions and substrates. This task falls to the protein environment surrounding the flavin in most enzymes. For iodotyrosine deiodinase that catalyzes a reductive dehalogenation of halotyrosines, substrates can dictate the chemistry available to the flavin. Their ability to stabilize the necessary one-electron reduced semiquinone form of flavin strictly depends on a direct coordination between the flavin and α-ammonium and carboxylate groups of its substrates. While perturbations to the carboxylate group do not significantly affect bindin

SUBMITTER: Lemen D 

PROVIDER: S-EPMC11408085 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature