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NIH shift

Index NIH shift

An NIH shift is a chemical rearrangement where a hydrogen atom on an aromatic ring undergoes an intramolecular migration primarily during a hydroxylation reaction. [1]

10 relations: Deuterium, Hydrogen, Hydroxy group, Hydroxylation, Intramolecular force, Isotopic labeling, Methyl group, National Institutes of Health, Tetrahydrobiopterin, 4-Hydroxyphenylpyruvate dioxygenase.

Deuterium

Deuterium (or hydrogen-2, symbol or, also known as heavy hydrogen) is one of two stable isotopes of hydrogen (the other being protium, or hydrogen-1).

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Hydrogen

Hydrogen is a chemical element with symbol H and atomic number 1.

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Hydroxy group

A hydroxy or hydroxyl group is the entity with the formula OH.

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Hydroxylation

Hydroxylation is a chemical process that introduces a hydroxyl group (-OH) into an organic compound.

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Intramolecular force

An intramolecular force is any force that binds together the atoms making up a molecule or compound, not to be confused with intermolecular forces, which are the forces present between molecules.

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Isotopic labeling

Isotopic labeling (or isotopic labelling) is a technique used to track the passage of an isotope (an atom with a detectable variation) through a reaction, metabolic pathway, or cell.

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Methyl group

A methyl group is an alkyl derived from methane, containing one carbon atom bonded to three hydrogen atoms — CH3.

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National Institutes of Health

The National Institutes of Health (NIH) is the primary agency of the United States government responsible for biomedical and public health research, founded in the late 1870s.

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Tetrahydrobiopterin

Tetrahydrobiopterin (BH4, THB), also known as sapropterin, is a naturally occurring essential cofactor of the three aromatic amino acid hydroxylase enzymes, used in the degradation of amino acid phenylalanine and in the biosynthesis of the neurotransmitters serotonin (5-hydroxytryptamine, 5-HT), melatonin, dopamine, norepinephrine (noradrenaline), epinephrine (adrenaline), and is a cofactor for the production of nitric oxide (NO) by the nitric oxide synthases.

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4-Hydroxyphenylpyruvate dioxygenase

4-Hydroxyphenylpyruvate dioxygenase (HPPD), also known as α-ketoisocaproate dioxygenase (KIC dioxygenase), is an Fe(II)-containing non-heme oxygenase that catalyzes the second reaction in the catabolism of tyrosine - the conversion of 4-hydroxyphenylpyruvate into homogentisate.

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References

[1] https://en.wikipedia.org/wiki/NIH_shift

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