2-Oxoglutarate oxygenases are inhibited by a range of transition metals
Rok Sekirnik1, Nathan R Rose, Jasmin Mecinović
1Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK.
Abstract:
2-Oxoglutarate oxygenases are inhibited by a range of transition metals, as exemplified by studies on human histone demethylases and prolyl hydroxylase domain 2 (PHD2 or EGLN1). The biological effects associated with 2-oxoglutarate oxygenase inhibition may result from inhibition of more than one enzyme and by mechanisms in addition to simple competition with the Fe(ii) cofactor.
More Related Videos
08:31Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Related Concept Videos
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Properties of Transition Metals
Oxygen Requirements and Growth Patterns
Enzyme Inhibition
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Complexation Equilibria: Factors Influencing Stability of Complexes
