A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase

Basran, Jaswir, Rafice, Sara A., Chauhan, Nishma, Efimov, Igor, Cheesman, Myles R., Ghamsari, Lila and Raven, Emma Lloyd (2008) A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase. Biochemistry, 47 (16). pp. 4752-4760. ISSN 0006-2960

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The family of heme dioxygenases, as exemplified by indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase, catalyzes the oxidative cleavage Of L-tryptophan to N-formylkynurenine. Here, we describe a bacterial expression system for human tryptophan 2,3-dioxygenase (rhTDO) together with spectroscopic, kinetic, and redox analyses. We find unexpected differences between human tryptophan 2,3-dioxygenase and human indoleamine 2,3-dioxygenase [Chauhan et al. (2008) Biochemistry 47, 4761-4769]. Thus, in contrast to indoleamine 2,3-dioxygenase, the catalytic ferrous-oxy complex of rhTDO is not observed, nor does the enzyme discriminate against substrate binding to the ferric derivative. In addition, we show that the rhTDO is also catalytically active in the ferric form. These new findings illustrate that significant mechanistic differences exist across the heme dioxygenase family, and the data are discussed within this broader framework.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Chemistry of Life Processes
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Chemistry of Light and Energy
Depositing User: Rachel Smith
Date Deposited: 10 May 2011 10:42
Last Modified: 24 Oct 2022 00:47
URI: https://ueaeprints.uea.ac.uk/id/eprint/30092
DOI: 10.1021/bi702393b

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