Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).

Journal article

The hypoxic response in animals is mediated via the transcription factor hypoxia-inducible factor (HIF). An oxygen-sensing component of the HIF system is provided by Fe(II) and 2-oxoglutarate-dependent oxygenases that catalyse the posttranslational hydroxylation of the HIF-α subunit. It is proposed that the activity of the HIF hydroxylases can be regulated by their reaction with nitric oxide. We describe biochemical and biophysical studies on the reaction of prolyl hydroxylase domain-containi...

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Authors: Chowdhury, R; Flashman, E; Mecinović, J; Kramer, H; Kessler, B

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 410
• Issue: 2
• Pages: 268-279
• Publication date: 2011-07-01
• DOI: 10.1016/j.jmb.2011.04.075
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Anoxia; Nitric Oxide; Humans; Hypoxia-Inducible Factor 1; Protein Structure, Tertiary; Amino Acid Sequence; Tandem Mass Spectrometry; Procollagen-Proline Dioxygenase; Hypoxia-Inducible Factor-Proline Dioxygenases; Crystallography, X-Ray; Spectrometry, Mass, Electrospray Ionization; Molecular Sequence Data