Proton-Electron Transfer to the Active Site Is Essential for the Reaction Mechanism of Soluble Δ⁹-Desaturase.

ABSTRACT: A full understanding of the catalytic action of non-heme iron (NHFe) and non-heme diiron (NHFe₂) enzymes is still beyond the grasp of contemporary computational and experimental techniques. Many of these enzymes exhibit fascinating chemo-, regio-, and stereoselectivity, in spite of employing highly reactive intermediates which are necessary for activations of most stable chemical bonds. Herein, we study in detail one intriguing representative of the NHFe₂ family of enzymes: soluble Δ⁹ desaturase (Δ⁹D), which desaturates rather than performing the thermodynamically favorable hydroxylation of substrate. Its catalytic mechanism has been explored in great detail by using QM(DFT)/MM and multireference wave function methods. Starting from the spectrosc

SUBMITTER: Bim D 

PROVIDER: S-EPMC7316153 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature