Auto-hydroxylation of FIH-1: an Fe(ii), α-ketoglutarate-dependent human hypoxia sensor

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...

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Published inChemical communications (Cambridge, England) no. 39; pp. 4768 - 4770
Main Authors Chen, Yuan-Han, Comeaux, Lindsay M., Eyles, Stephen J., Knapp, Michael J.
Format Journal Article
LanguageEnglish
Published England 21.10.2008
Subjects
Catalytic Domain
chemical communication
Electrodes
enzymes
Ferrous Compounds - chemistry
Humans
Hydroxylation
Hypoxia
iron
Ketoglutaric Acids - chemistry
Mixed Function Oxygenases
oxygen
Oxygen - analysis
Repressor Proteins - chemistry
Sensitivity and Specificity
Spectrometry, Mass, Electrospray Ionization
Spectrophotometry
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1359-7345
1364-548X
1364-548X
DOI:10.1039/b809099h