C. Directed evolution of an iron(II)- and α-ketoglutarate-dependent dioxygenase for site-selective azidation of unactivated aliphatic C–H bonds. Angew. Chem. Int. Ed. 62, e202301370 (2023). CAS Google Scholar Neugebauer, M. E. et al. Reaction pathway engineering converts a radical ...
J. (2009) Bio-inspired arene cis-dihydroxylation by a non-heme iron catalyst modeling the action of naphthalene dioxygenase, Chemical Communications, 50-52.Feng, Y.; Ke, C.; Xue, G.; Que, L., Jr. Bio-inspired arene cis-dihydroxylation by a non-haem iron catalyst modeling the action ...
Objective: Non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenases (i2OGdd), are a taxonomically and functionally diverse group of enzymes. The active site comprises ferrous iron in a hexa-coordinated distorted octahedron with the apoenzyme, 2-oxoglutarate and a displaceable water molecule....
Leitgeb, S., Straganz, G. D., and Nidetzky, B. (2009) Biochemical characterization and mutational analysis of the mononuclear non-haem Fe2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii, Biochem J 418, 403-411....
For example, histidine and glutamate residues are ligands to the diiron center of methane monooxygenase hydroxylase =-=(5, 48)-=- and to Fe21 at the active site in 2,3-dihydroxybiphenyl 1,2dioxygenase (24). Histidine and tyrosine residues are ligands to Fe31 in protocatechuate 3,4-...