Publication | Closed Access
A Designed Functional Metalloenzyme that Reduces O<sub>2</sub> to H<sub>2</sub>O with Over One Thousand Turnovers
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Citations
29
References
2012
Year
Bioorganic ChemistryEngineeringFunctional MetalloenzymeMolecular BiologyChemistryRedox BiologyInorganic CompoundBiosynthesisBioenergeticsRational DesignMetabolic EngineeringComplex Active SiteBioorganometallic ChemistryStructure-function Enzyme KineticsThousand TurnoversMaterials ScienceInorganic ChemistryBiochemistrySpare TyrCatalysisOver OneNatural SciencesHeme DegradationEnzyme CatalysisProtein EngineeringFunctional MaterialsMetal Chain Compound
No spare Tyr: Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O2 to H2O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.
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