grant
Mechanisms and Control of O2 and C–H Activation within "Privileged" Enzyme Architectures
Organization PENNSYLVANIA STATE UNIVERSITY, THELocation UNIVERSITY PARK, UNITED STATESPosted 1 Apr 2026Deadline 31 Mar 2031
NIHUS FederalResearch GrantFY20262-ketoglutarate2-oxoglutarateArchitectureBiochemicalCarbonChemicalsComplexComputing MethodologiesCyclizationDNADeoxyribonucleic AcidDevelopmentDioxygenDirected Molecular EvolutionDrug Synthesis and ChemistryEngineeringEngineering / ArchitectureEnzyme GeneEnzymesFe elementFe(4+)FerroprotoporphyrinFlavinsH-bondHemeHydrogen BondingHydroxylationIndividualIonsIronLifeManganeseMetabolic PathwayMetalsMn elementMolecularNatureOrganismOutcomeOxygenasesPathway interactionsPeroxidesProtein ConformationProteinsProtohemeReactionRibonucleotide ReductaseScaffolding ProteinTestingTherapeuticTransition Elementsalpha ketoglutaratebiophysical approachesbiophysical methodologybiophysical methodsbiophysical techniquescofactorcomputational methodologycomputational methodscomputer based methodcomputer methodscomputing methoddevelopmentaldirected evolutiondrug synthesisexperimentexperimental researchexperimental studyexperimentsferrohemeferryl ionferryl ironhalogenationiron (4+) ioniron(IV)living systemmetalloenzymemimicrypathwayprogramsscaffoldscaffoldingtransition metalα-ketoglutarateα-oxoglutarateαKG
Description preview
Project Summary/Abstract
Enzymes that activate dioxygen or (su)peroxide at transition metal cofactors to cleave strong X–
H bonds (X = C/N/O) are prevalent in central and specialized metabolic pathways in organisms
from all three domains of life. Their abilities to generate highly reactive carbon and heteroatom
radicals and direct them down…
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