Structure of a Model Transient Peroxide Intermediate of Peroxidases by ab Initio Methods

摘要: Peroxidases are oxidative metabolizing heme proteins that require hydrogen peroxide to be transformed the catalytically active, compound I, species from ferric resting state. Although a complex has been proposed as key intermediate in this reaction, is too transient have thus far definitively characterized. Results of previous molecular dynamics (MD) simulations with cytochrome C peroxidase (CCP) indicated forms stable and binds nonsymmetric, end-on mode which oxygen atoms systematically exchange places ligands for iron. These results provided support plausible pathway involving participation nearby histidine arginine residues. To further explore reliability bonding description, we report here, first time, use ab initio methods determine optimized geometry stability model hem...