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Rejigging Electron and Proton Transfer to Transition between Dioxygenase, Monooxygenase, Peroxygenase, and Oxygen Reduction Activity: Insights from Bioinspired Constructs of Heme Enzymes

Manjistha Mukherjee, Abhishek Dey

2021JACS Au25 citationsDOIOpen Access PDF

Abstract

derived intermediates has been developed. These findings suggest that the enzymatic activities of all these heme enzymes can be integrated into one general cycle which can be branched out to different catalytic pathways by regulating the lifetime and population of each of these intermediates. This regulation can further be achieved by tuning the electron and proton transfer steps. By strategically populating one of these intermediates during oxygen reduction, one can navigate through different catalytic processes to a desired direction by altering proton and electron transfer steps.

Topics & Concepts

HemeChemistryCofactorElectron transferHemeproteinEnzymeSubstrate (aquarium)CatalysisCatalytic cycleEnzyme catalysisPhotochemistryResonance Raman spectroscopyStereochemistryBiochemistryRaman spectroscopyBiologyPhysicsEcologyOpticsMetal-Catalyzed Oxygenation MechanismsHeme Oxygenase-1 and Carbon MonoxideHemoglobin structure and function
Rejigging Electron and Proton Transfer to Transition between Dioxygenase, Monooxygenase, Peroxygenase, and Oxygen Reduction Activity: Insights from Bioinspired Constructs of Heme Enzymes | Litcius