![](https://d3ilqtpdwi981i.cloudfront.net/HU2f7ar0LYYrpHHn62iq2WlTKXk=/425x550/smart/https://bepress-attached-resources.s3.amazonaws.com/uploads/62/72/fa/6272fa41-841e-4072-a6ed-963aadb91451/thumbnail_BPFile%20object.jpg)
Article
Auto-hydroxylation of FIH-1: an Fe(II), α-ketoglutarate-dependent human hypoxia sensor
Chemical Communications
(2008)
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.
Disciplines
Publication Date
2008
Publisher Statement
This article was harvested from PubMed Central. Please use this link to view the publisher’s version:
http://pubs.rsc.org/en/content/articlelanding/2008/cc/b809099h
doi:10.1039/b809099h
Citation Information
Yuan-Han Chen, Lindsay M Comeaux, Stephen J. Eyles and Michael J. Knapp. "Auto-hydroxylation of FIH-1: an Fe(II), α-ketoglutarate-dependent human hypoxia sensor" Chemical Communications Vol. 39 (2008) Available at: http://works.bepress.com/stephen_eyles/2/