Ligand migration in human indoleamine-2,3 dioxygenase

Karin Nienhaus, Elena Nickel, Changyuan Lu, Syun Ru Yeh, G. Ulrich Nienhaus

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Human indoleamine 2,3-dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L-tryptophan (L-Trp) and other indoleamine derivatives. Its activity follows typical Michaelis-Menten behavior only for L-Trp concentrations up to 50 μM; a further increase in the concentration of L-Trp causes a decrease in the activity. This substrate inhibition of hIDO is a result of the binding of a second L-Trp molecule in an inhibitory substrate binding site of the enzyme. The molecular details of the reaction and the inhibition are not yet known. In the following, we summarize the present knowledge about this heme enzyme.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
JournalIUBMB Life
Issue number3
StatePublished - Mar 2011


  • FTIR spectroscopy
  • enzyme mechanisms
  • hemeproteins
  • substrate
  • temperature derivative spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology


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