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The enzyme is an oxygenase which means it uses molecular oxygen to hydroxylate its substrates.
Notably, perfluoroalkyloxaziridines have the ability to hydroxylate certain C-H bonds with high selectivity.
The hot (often bubbling) solution will clean organic compounds off substrates, and oxidize or hydroxylate most metal surfaces.
Perfluorinated oxaziridines are known to hydroxylate unactivated hydrocarbons with remarkable regio, and diastereospecificity.
Some bacteria are able to hydroxylate biphenyl and its polychlorinated biphenyls (PCBs).
Instead of reversibly binding oxygen, these proteins hydroxylate substrates, illustrated by their role in the formation of lacquers.
The demethylation occurs when JmjC utilizes multiple cofactors to hydroxylate the methyl group, thereby removing it.
Kirsch and co-workers were able to hydroxylate keto compounds with IBX in α-position under mild conditions.
Finally, testosterone and DHT may be deactivated or cleared by enzymes that hydroxylate at the 6, 7, 15 or 16 positions.
Tryptophan is a poor substrate for tyrosine hydroxylate, however it can hydroxylate -phenylalanine to form -tyrosine and small amounts of 3-hydroxyphenylalanine.
Because the mixture is a strong oxidizing agent, it will remove most organic matter, and it will also hydroxylate most surfaces (add OH groups), making them highly hydrophilic (water compatible).
PHDs rely on iron among other molecules to hydroxylate HIF-1alpha; as such, iron chelators such as DFO have proven successful in HIF-1alpha stabilization.
One of the oxygen atoms in O is used to hydroxylate the tyrosine molecule to obtain -DOPA and the other one is used to hydroxylate the cofactor.
These are luciferases, which are used by bioluminescent animals and bacteria to produce light, and cytochrome P450, which is a group of heme proteins that hydroxylate a diverse group of compounds, including fatty acids, steroids, and xenobiotics such as phenobarbital.