Abstract
HIF-asparaginyl hydroxylase (FIH-1) normally couples O(2)-activation to hydroxylation of Asn(803) on the alpha-subunit of the hypoxia-inducible factor (HIFalpha), a key step in pO(2) sensing; in the absence of HIFalpha, O(2)-activation becomes uncoupled, leading to self-hydroxylation at Trp(296) and a purple Fe(iii)-O-Trp chromophore-this alternative reactivity may affect human hypoxia sensing.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Catalytic Domain
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Electrodes
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Ferrous Compounds / chemistry*
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Humans
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Hydroxylation
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Hypoxia*
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Ketoglutaric Acids / chemistry*
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Mixed Function Oxygenases
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Oxygen / analysis*
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Repressor Proteins / chemistry*
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Sensitivity and Specificity
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Spectrometry, Mass, Electrospray Ionization
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Spectrophotometry
Substances
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Ferrous Compounds
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Ketoglutaric Acids
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Repressor Proteins
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Mixed Function Oxygenases
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HIF1AN protein, human
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Oxygen