Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052931 | FEBS Letters | 2006 | 4 Pages |
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 b5 and cytochrome b5 reductase in maintaining IDO activity in vivo.
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Authors
Eduardo Vottero, David A. Mitchell, Michael J. Page, Ross T.A. MacGillivray, Ivan J. Sadowski, Michel Roberge, A. Grant Mauk,