Results 11 to 20 of about 82,259 (373)

Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases

open access: yesNature Communications, 2020
Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and
April L. Lukowski   +3 more
doaj   +2 more sources

Controlled depolymerization of cellulose by light-driven lytic polysaccharide oxygenases

open access: yesNature Communications, 2020
Lytic polysaccharide (mono)oxygenases (LPMOs) perform oxidative cleavage of polysaccharides. Here, the authors showed that the light-driven activity of LPMOs is dependent on hydrogen peroxide availability and can be controlled via the light intensity ...
Bastien Bissaro   +3 more
doaj   +2 more sources

Palmitoylation of Metazoan Carotenoid Oxygenases [PDF]

open access: goldMolecules, 2020
Abundant in nature, carotenoids are a class of fat-soluble pigments with a polyene tetraterpenoid structure. They possess antioxidant properties and their consumption leads to certain health benefits in humans. Carotenoid cleavage oxygenases (CCOs) are a
Sheetal Uppal   +3 more
doaj   +2 more sources

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases

open access: yesNature Communications, 2021
The human 2-oxoglutarate (2OG) oxygenases FIH and AspH are relevant drug targets. Here, the authors show that synthetic and naturally occurring 2OG derivatives can selectively modulate FIH and AspH activities, suggesting that these compounds may serve as
Yu Nakashima   +4 more
doaj   +2 more sources

Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis

open access: yesNature Communications, 2018
Non-heme iron and α-ketoglutarate (αKG) oxygenases play a major role in fungal meroterpenoid biosynthesis, but their mechanism remains elusive. Here the authors present crystal structures of two oxygenases, AusE and PrhA, which provide insights into the ...
Yu Nakashima   +7 more
doaj   +2 more sources

Discovery and characterization of a new family of lytic polysaccharide monooxygenases [PDF]

open access: yesNature Chemical Biology, 2014
Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the ...
A Levasseur   +38 more
core   +3 more sources

Oxygenases as Powerful Weapons in the Microbial Degradation of Pesticides.

open access: yesAnnual Review of Microbiology, 2022
Oxygenases, which catalyze the reductive activation of O2 and incorporation of oxygen atoms into substrates, are widely distributed in aerobes. They function by switching the redox states of essential cofactors that include flavin, heme iron, Rieske non ...
Minggen Cheng   +3 more
semanticscholar   +1 more source

Charge Maintenance during Catalysis in Nonheme Iron Oxygenases.

open access: yesACS Catalysis, 2022
Here, the choice of the first coordination shell of the metal center is analyzed from the perspective of charge maintenance in a binary enzyme-substrate complex and an O2-bound ternary complex in the nonheme iron oxygenases.
Ephrahime S Traore, Aimin Liu
semanticscholar   +1 more source

Nature's Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases.

open access: yesACS Catalysis, 2020
Iron is an especially important redox-active cofactor in biology because of its ability to mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth-abundant transition metal for the insertion of oxygen atoms into organic ...
N. P. Dunham, F. Arnold
semanticscholar   +1 more source

Role of Structural Dynamics in Selectivity and Mechanism of Non-heme Fe(II) and 2-Oxoglutarate-Dependent Oxygenases Involved in DNA Repair

open access: yesACS Central Science, 2020
AlkB and its human homologue AlkBH2 are Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenases that repair alkylated DNA bases occurring as a consequence of reactions with mutagenic agents.

semanticscholar   +1 more source

Home - About - Disclaimer - Privacy