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Article

Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis.

Biochemistry - 1 Nov 2005

Papadopoulou Nektaria D, Mewies Martin, McLean Kirsty J, Seward Harriet E, Svistunenko Dimitri A, Munro Andrew W, Raven Emma Lloyd

Abstract excerpt

Indoleamine 2,3-dioxygenase is an important mammalian target that catalyses the oxidative cleavage of l-tryptophan to N-formylkynurenine. In this work, the redox properties of recombinant human indoleamine 2,3-dioxygenase (rhIDO) and its H303A variant have been examined for the first time and the spectroscopic and substrate-binding properties of rhIDO and H303A in the presence and absence of substrate are...

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PMID: 16245948
DOI: 10.1021/bi0513958

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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