Can Second Coordination Sphere and Long-Range Interactions Modulate Hydrogen Atom Transfer in a Non-Heme Fe(II)-Dependent Histone Demethylase?
Shobhit S. Chaturvedi, Simahudeen Bathir Jaber Sathik Rifayee, Sodiq O. Waheed, Jon Wildey, Cait Warner, Christopher J. Schofield, Tatyana G. Karabencheva‐Christova, Christo Christov
Abstract
K9me2 substrate. SCS and LR residues alter the intrinsic electric field of the enzyme along the reaction coordinate and change the individual energetic contributions of residues toward TS stabilization. The overall results suggest that DCCA can indeed identify non-active-site residues relevant for catalysis. The substitutions of such dynamically correlated residues might be used as a tool to tune HAT in non-heme Fe(II)- and 2OG-dependent enzymes.
Topics & Concepts
ChemistryDemethylaseActive siteMolecular dynamicsElectron transferSubstrate (aquarium)QM/MMProtein dynamicsMolecular mechanicsHeme oxygenaseStereochemistryHistoneEnzymeComputational chemistryHemeBiochemistryPhotochemistryDNABiologyEcologyMetal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteinsMetal complexes synthesis and properties