Cytochrome b(5) is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast

Eduardo Vottero; David A Mitchell; Michael J Page; Ross T A MacGillivray; Ivan J Sadowski; Michel Roberge; A Grant Mauk

doi:10.1016/j.febslet.2006.03.034

Cytochrome b(5) is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast

FEBS Lett. 2006 Apr 17;580(9):2265-8. doi: 10.1016/j.febslet.2006.03.034. Epub 2006 Mar 20.

Authors

Eduardo Vottero¹, David A Mitchell, Michael J Page, Ross T A MacGillivray, Ivan J Sadowski, Michel Roberge, A Grant Mauk

Affiliation

¹ Department of Biochemistry and Molecular Biology, Life Sciences Centre, University of British Columbia, Vancouver, BC, Canada V6T 1Z3.

PMID: 16574111
DOI: 10.1016/j.febslet.2006.03.034

Abstract

The evolutionary relationship of indoleamine 2,3-dioxygenase (IDO) to some gastropod myoglobins suggests that IDO may undergo autoxidation in vivo such that one or more currently unidentified electron donors are required to maintain IDO heme iron in the active, ferrous state. To evaluate this hypothesis we have used yeast knockout mutants in combination with a recently developed yeast growth assay for IDO activity in vivo to demonstrate a role for cytochrome b(5) and cytochrome b(5) reductase in maintaining IDO activity in vivo.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cytochrome-B(5) Reductase / genetics
Cytochrome-B(5) Reductase / metabolism*
Gene Expression / genetics
Heme / metabolism
Humans
Indoleamine-Pyrrole 2,3,-Dioxygenase / genetics
Indoleamine-Pyrrole 2,3,-Dioxygenase / metabolism*
Mutation
Oxidation-Reduction
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / metabolism*

Substances

Indoleamine-Pyrrole 2,3,-Dioxygenase
Recombinant Proteins
Saccharomyces cerevisiae Proteins
Heme
Cytochrome-B(5) Reductase