A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase
Mary Ortmayer, Florence J. Hardy, Matthew G. Quesne, Karl Fisher, Colin Levy, Derren J. Heyes, C. Richard A. Catlow, Sam P. de Visser, Stephen E. J. Rigby, Sam Hay, Anthony P. Green
Abstract
. Our data highlight how Trp51 tunes the lifetimes of key ferryl intermediates and works in synergy with the redox active Trp191 and a well-defined substrate binding site to regulate catalytic function. More broadly, this work shows how noncanonical substitutions can advance our understanding of active site features governing metal-oxo structure and reactivity.
Topics & Concepts
ChemistryActive siteHemeReactivity (psychology)PeroxidasePorphyrinRedoxStereochemistryPhotochemistryCytochrome c peroxidaseCombinatorial chemistryCatalysisEnzymeOrganic chemistryPathologyMedicineAlternative medicineMetal-Catalyzed Oxygenation MechanismsPhotosynthetic Processes and MechanismsHemoglobin structure and function